(data stored in ACNUC27125 zone)

SWISSPROT: ASAH2_HUMAN

ID   ASAH2_HUMAN             Reviewed;         780 AA.
AC   Q9NR71; Q3KNU1; Q5SNT7; Q5SZP6; Q5SZP7; Q5T1D5; Q71ME6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   11-DEC-2019, entry version 142.
DE   RecName: Full=Neutral ceramidase {ECO:0000305};
DE            Short=N-CDase;
DE            Short=NCDase;
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q9JHE3};
DE            EC=3.5.1.23 {ECO:0000269|PubMed:10781606, ECO:0000269|PubMed:11278489, ECO:0000269|PubMed:15946935, ECO:0000269|PubMed:16061940, ECO:0000269|PubMed:19345744, ECO:0000269|PubMed:26190575};
DE   AltName: Full=Acylsphingosine deacylase 2;
DE   AltName: Full=BCDase;
DE   AltName: Full=LCDase;
DE            Short=hCD;
DE   AltName: Full=N-acylsphingosine amidohydrolase 2;
DE   AltName: Full=Non-lysosomal ceramidase;
DE   Contains:
DE     RecName: Full=Neutral ceramidase soluble form {ECO:0000250|UniProtKB:Q91XT9};
GN   Name=ASAH2; Synonyms=HNAC1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14557071; DOI=10.1016/s0378-1119(03)00721-2;
RA   Choi M.S., Anderson M.A., Zhang Z., Zimonjic D.B., Popescu N.,
RA   Mukherjee A.B.;
RT   "Neutral ceramidase gene: role in regulating ceramide-induced apoptosis.";
RL   Gene 315:113-122(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RX   PubMed=15946935; DOI=10.1074/jbc.m503002200;
RA   Osawa Y., Uchinami H., Bielawski J., Schwabe R.F., Hannun Y.A.,
RA   Brenner D.A.;
RT   "Roles for C16-ceramide and sphingosine 1-phosphate in regulating
RT   hepatocyte apoptosis in response to tumor necrosis factor-alpha.";
RL   J. Biol. Chem. 280:27879-27887(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 20-780 (ISOFORM 1), FUNCTION, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=10781606; DOI=10.1074/jbc.m002522200;
RA   El Bawab S., Roddy P., Qian T., Bielawska A., Lemasters J.J., Hannun Y.A.;
RT   "Molecular cloning and characterization of a human mitochondrial
RT   ceramidase.";
RL   J. Biol. Chem. 275:21508-21513(2000).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11278489; DOI=10.1074/jbc.m009331200;
RA   El Bawab S., Birbes H., Roddy P., Szulc Z.M., Bielawska A., Hannun Y.A.;
RT   "Biochemical characterization of the reverse activity of rat brain
RT   ceramidase. A CoA-independent and fumonisin B1-insensitive ceramide
RT   synthase.";
RL   J. Biol. Chem. 276:16758-16766(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-780 (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX   PubMed=15845354; DOI=10.1016/j.bbrc.2005.03.134;
RA   Hwang Y.H., Tani M., Nakagawa T., Okino N., Ito M.;
RT   "Subcellular localization of human neutral ceramidase expressed in HEK293
RT   cells.";
RL   Biochem. Biophys. Res. Commun. 331:37-42(2005).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16061940; DOI=10.1194/jlr.m500268-jlr200;
RA   Tani M., Sano T., Ito M., Igarashi Y.;
RT   "Mechanisms of sphingosine and sphingosine 1-phosphate generation in human
RT   platelets.";
RL   J. Lipid Res. 46:2458-2467(2005).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF SER-258; ASP-352; SER-354;
RP   CYS-362; SER-374; SER-396; SER-595 AND SER-729.
RX   PubMed=16229686; DOI=10.1042/bj20050682;
RA   Galadari S., Wu B.X., Mao C., Roddy P., El Bawab S., Hannun Y.A.;
RT   "Identification of a novel amidase motif in neutral ceramidase.";
RL   Biochem. J. 393:687-695(2006).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=17475390; DOI=10.1016/j.biochi.2007.03.009;
RA   Ohlsson L., Palmberg C., Duan R.D., Olsson M., Bergman T., Nilsson A.;
RT   "Purification and characterization of human intestinal neutral
RT   ceramidase.";
RL   Biochimie 89:950-960(2007).
RN   [11]
RP   TISSUE SPECIFICITY.
RX   PubMed=17334805; DOI=10.1007/s10048-007-0081-5;
RA   Avramopoulos D., Wang R., Valle D., Fallin M.D., Bassett S.S.;
RT   "A novel gene derived from a segmental duplication shows perturbed
RT   expression in Alzheimer's disease.";
RL   Neurogenetics 8:111-120(2007).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INDUCTION BY GEMCITABINE.
RX   PubMed=19345744; DOI=10.1016/j.bbalip.2009.03.012;
RA   Wu B.X., Zeidan Y.H., Hannun Y.A.;
RT   "Downregulation of neutral ceramidase by gemcitabine: Implications for cell
RT   cycle regulation.";
RL   Biochim. Biophys. Acta 1791:730-739(2009).
RN   [13]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24798654; DOI=10.1111/febs.12826;
RA   Zhu Q., Kang J., Miao H., Feng Y., Xiao L., Hu Z., Liao D.F., Huang Y.,
RA   Jin J., He S.;
RT   "Low-dose cytokine-induced neutral ceramidase secretion from INS-1 cells
RT   via exosomes and its anti-apoptotic effect.";
RL   FEBS J. 281:2861-2870(2014).
RN   [14]
RP   CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=30154232; DOI=10.1194/jlr.m088187;
RA   Sakamoto W., Coant N., Canals D., Obeid L.M., Hannun Y.A.;
RT   "Functions of neutral ceramidase in the Golgi apparatus.";
RL   J. Lipid Res. 59:2116-2125(2018).
RN   [15] {ECO:0000244|PDB:4WGK}
RP   X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 99-780 IN COMPLEX WITH CALCIUM;
RP   ZINC AND PHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, GLYCOSYLATION
RP   AT ASN-151; ASN-217; ASN-308; ASN-440 AND ASN-730, DISULFIDE BONDS, AND
RP   MUTAGENESIS OF GLY-124; HIS-194; HIS-196; ALA-211; ARG-257; HIS-303;
RP   GLY-465; GLU-540; TYR-579 AND TYR-591.
RX   PubMed=26190575; DOI=10.1016/j.str.2015.06.013;
RA   Airola M.V., Allen W.J., Pulkoski-Gross M.J., Obeid L.M., Rizzo R.C.,
RA   Hannun Y.A.;
RT   "Structural Basis for Ceramide Recognition and Hydrolysis by Human Neutral
RT   Ceramidase.";
RL   Structure 23:1482-1491(2015).
CC   -!- FUNCTION: Plasma membrane ceramidase that hydrolyzes sphingolipid
CC       ceramides into sphingosine and free fatty acids at neutral pH
CC       (PubMed:10781606, PubMed:16229686, PubMed:26190575). Ceramides,
CC       sphingosine, and its phosphorylated form sphingosine-1-phosphate are
CC       bioactive lipids that mediate cellular signaling pathways regulating
CC       several biological processes including cell proliferation, apoptosis
CC       and differentiation (PubMed:15946935, PubMed:19345744,
CC       PubMed:24798654). Also catalyzes the reverse reaction allowing the
CC       synthesis of ceramides from fatty acids and sphingosine
CC       (PubMed:11278489, PubMed:17475390). Together with sphingomyelinase,
CC       participates in the production of sphingosine and sphingosine-1-
CC       phosphate from the degradation of sphingomyelin, a sphingolipid
CC       enriched in the plasma membrane of cells (PubMed:16061940). Also
CC       participates in the hydrolysis of ceramides from the extracellular
CC       milieu allowing the production of sphingosine-1-phosphate inside and
CC       outside cells (By similarity). This is the case for instance with the
CC       digestion of dietary sphingolipids in the intestinal tract (By
CC       similarity). {ECO:0000250|UniProtKB:Q9JHE3,
CC       ECO:0000269|PubMed:10781606, ECO:0000269|PubMed:11278489,
CC       ECO:0000269|PubMed:15946935, ECO:0000269|PubMed:16061940,
CC       ECO:0000269|PubMed:16229686, ECO:0000269|PubMed:17475390,
CC       ECO:0000269|PubMed:19345744, ECO:0000269|PubMed:24798654,
CC       ECO:0000269|PubMed:26190575}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine;
CC         Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23;
CC         Evidence={ECO:0000269|PubMed:10781606, ECO:0000269|PubMed:11278489,
CC         ECO:0000269|PubMed:15946935, ECO:0000269|PubMed:16061940,
CC         ECO:0000269|PubMed:19345744, ECO:0000269|PubMed:26190575};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20857;
CC         Evidence={ECO:0000250|UniProtKB:Q9JHE3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate + sphing-4-
CC         enine; Xref=Rhea:RHEA:41291, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:72956;
CC         Evidence={ECO:0000269|PubMed:16229686, ECO:0000269|PubMed:30154232};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41292;
CC         Evidence={ECO:0000305|PubMed:16229686};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41293;
CC         Evidence={ECO:0000250|UniProtKB:Q9JHE3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-
CC         enine; Xref=Rhea:RHEA:38891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:72959;
CC         Evidence={ECO:0000269|PubMed:10781606, ECO:0000269|PubMed:17475390};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38892;
CC         Evidence={ECO:0000305|PubMed:10781606};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38893;
CC         Evidence={ECO:0000305|PubMed:17475390};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-octanoylsphing-4-enine = octanoate + sphing-4-enine;
CC         Xref=Rhea:RHEA:45092, ChEBI:CHEBI:15377, ChEBI:CHEBI:25646,
CC         ChEBI:CHEBI:45815, ChEBI:CHEBI:57756;
CC         Evidence={ECO:0000269|PubMed:17475390};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45093;
CC         Evidence={ECO:0000305|PubMed:17475390};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(hexanoyl)sphing-4-enine = hexanoate + sphing-4-enine;
CC         Xref=Rhea:RHEA:41295, ChEBI:CHEBI:15377, ChEBI:CHEBI:17120,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:63867;
CC         Evidence={ECO:0000269|PubMed:15946935, ECO:0000269|PubMed:30154232};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41296;
CC         Evidence={ECO:0000269|PubMed:15946935, ECO:0000269|PubMed:30154232};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-octadecanoylsphing-4-enine = octadecanoate + sphing-4-
CC         enine; Xref=Rhea:RHEA:41279, ChEBI:CHEBI:15377, ChEBI:CHEBI:25629,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:72961;
CC         Evidence={ECO:0000269|PubMed:15946935};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41280;
CC         Evidence={ECO:0000269|PubMed:15946935};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-tetradecanoylsphing-4-enine = sphing-4-enine +
CC         tetradecanoate; Xref=Rhea:RHEA:41287, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30807, ChEBI:CHEBI:57756, ChEBI:CHEBI:72957;
CC         Evidence={ECO:0000250|UniProtKB:Q91XT9};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41289;
CC         Evidence={ECO:0000250|UniProtKB:Q91XT9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(9Z-octadecenoyl)-sphing-4-enine = (9Z)-octadecenoate
CC         + sphing-4-enine; Xref=Rhea:RHEA:41299, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:57756, ChEBI:CHEBI:77996;
CC         Evidence={ECO:0000269|PubMed:15946935};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41300;
CC         Evidence={ECO:0000269|PubMed:15946935};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41301;
CC         Evidence={ECO:0000250|UniProtKB:Q91XT9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(15Z-tetracosenoyl)-sphing-4-enine = (15Z)-
CC         tetracosenoate + sphing-4-enine; Xref=Rhea:RHEA:41267,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:32392, ChEBI:CHEBI:57756,
CC         ChEBI:CHEBI:74450; Evidence={ECO:0000250|UniProtKB:Q91XT9};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41269;
CC         Evidence={ECO:0000250|UniProtKB:Q91XT9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoate + sphinganine = H2O + N-hexadecanoylsphinganine;
CC         Xref=Rhea:RHEA:43440, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57817, ChEBI:CHEBI:67042;
CC         Evidence={ECO:0000250|UniProtKB:Q9JHE3};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43442;
CC         Evidence={ECO:0000250|UniProtKB:Q9JHE3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(octadecanoyl)-sphinganine = octadecanoate +
CC         sphinganine; Xref=Rhea:RHEA:45008, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:25629, ChEBI:CHEBI:57817, ChEBI:CHEBI:67033;
CC         Evidence={ECO:0000250|UniProtKB:Q9JHE3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45009;
CC         Evidence={ECO:0000250|UniProtKB:Q9JHE3};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:26190575};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:26190575};
CC   -!- ACTIVITY REGULATION: Inhibited by dithiothreitol (DTT) and 2-
CC       mercaptoethanol (PubMed:16229686). Activity is mildly stimulated by
CC       Ca(2+) and Mg(2+), but is not inhibited by EDTA (PubMed:10781606,
CC       PubMed:16229686). Activity is inhibited by millimolar levels of Fe(2+),
CC       Zn(2+) and Cu(2+) (PubMed:16229686, PubMed:17475390). Inhibited by
CC       cholesterol (PubMed:17475390). {ECO:0000269|PubMed:10781606,
CC       ECO:0000269|PubMed:16229686, ECO:0000269|PubMed:17475390}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=60.1 uM for D-erythro-C12-NBD-ceramide (at 37 degrees Celsius and
CC         pH 7.5) {ECO:0000269|PubMed:16229686};
CC         KM=13 uM for N-octanoylsphing-4-enine (at 37 degrees Celsius and pH
CC         7.0) {ECO:0000269|PubMed:17475390};
CC         Vmax=0.68 nmol/min/mg enzyme for the hydrolysis of D-erythro-C12-NBD-
CC         ceramide as substrate (at 37 degrees Celsius and pH 7.5)
CC         {ECO:0000269|PubMed:16229686};
CC         Vmax=0.8 umol/min/mg enzyme for the hydrolysis of N-octanoylsphing-4-
CC         enine (at 37 degrees Celsius and pH 7.0)
CC         {ECO:0000269|PubMed:17475390};
CC       pH dependence:
CC         Optimum pH is 7.5-9.5 for N-hexadecanoylsphing-4-enine
CC         (PubMed:10781606). Optimum pH is 7.5 for D-erythro-C12-NBD-ceramide
CC         (PubMed:16229686). Optimum pH is 7.5 for N-octanoylsphing-4-enine
CC         (PubMed:17475390). {ECO:0000269|PubMed:10781606,
CC         ECO:0000269|PubMed:16229686, ECO:0000269|PubMed:17475390};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000269|PubMed:15946935, ECO:0000269|PubMed:19345744}.
CC   -!- SUBCELLULAR LOCATION: [Neutral ceramidase]: Cell membrane
CC       {ECO:0000269|PubMed:15845354}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q91XT9}. Membrane raft
CC       {ECO:0000250|UniProtKB:Q9JHE3}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q91XT9}. Membrane, caveola
CC       {ECO:0000250|UniProtKB:Q9JHE3}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q91XT9}. Golgi apparatus membrane
CC       {ECO:0000269|PubMed:30154232}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q91XT9}. Mitochondrion
CC       {ECO:0000269|PubMed:10781606}. Secreted, extracellular exosome
CC       {ECO:0000269|PubMed:24798654}. Note=Enriched in exosomes upon
CC       stimulation by cytokine (PubMed:24798654). Enriched in caveolae and
CC       lipid rafts (By similarity). The localization to the mitochondrion
CC       could not be confirmed (PubMed:15845354).
CC       {ECO:0000250|UniProtKB:Q9JHE3, ECO:0000269|PubMed:15845354,
CC       ECO:0000269|PubMed:24798654}.
CC   -!- SUBCELLULAR LOCATION: [Neutral ceramidase soluble form]: Secreted
CC       {ECO:0000250|UniProtKB:Q91XT9}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NR71-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NR71-2; Sequence=VSP_019928;
CC   -!- TISSUE SPECIFICITY: Primarily expressed in intestine (PubMed:17334805).
CC       Ubiquitously expressed with higher levels in kidney, skeletal muscle
CC       and heart (PubMed:10781606). The ubiquitous expression observed for
CC       ASAH2 might be an experimental artifact due to the paralog ASAH2B
CC       (PubMed:17334805). {ECO:0000269|PubMed:10781606,
CC       ECO:0000269|PubMed:17334805}.
CC   -!- INDUCTION: Down-regulated by gemcitabine/GMZ (at protein level)
CC       (PubMed:19345744). Down-regulated upon serum starvation
CC       (PubMed:19345744). {ECO:0000269|PubMed:19345744}.
CC   -!- PTM: Proteolytic cleavage of the N-terminus removes the signal-anchor
CC       and produces a soluble form of the protein.
CC       {ECO:0000250|UniProtKB:Q91XT9}.
CC   -!- PTM: N-glycosylated. Required for enzyme activity.
CC       {ECO:0000250|UniProtKB:Q9JHE3}.
CC   -!- PTM: O-glycosylated. Required to retain it as a type II membrane
CC       protein at the cell surface. {ECO:0000269|PubMed:15845354}.
CC   -!- PTM: Phosphorylated. May prevent ubiquitination and subsequent
CC       degradation. {ECO:0000250|UniProtKB:Q91XT9}.
CC   -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC       Ubiquitination is triggered by nitric oxide.
CC       {ECO:0000250|UniProtKB:Q91XT9}.
CC   -!- SIMILARITY: Belongs to the neutral ceramidase family. {ECO:0000305}.
CC   -!- CAUTION: Was proposed to be mitochondrial, based on experiments with an
CC       N-terminal GFP-tag (PubMed:10781606). The in vivo localization to the
CC       mitochondrion could not be confirmed (PubMed:15845354). However, it has
CC       been observed for the mouse (AC Q9JHE3) and rat (AC Q91XT9) orthologs.
CC       {ECO:0000269|PubMed:10781606, ECO:0000269|PubMed:15845354,
CC       ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL06061.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; AY049008; AAL06061.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AF449759; AAQ04667.2; -; mRNA.
DR   EMBL; AL450382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL589794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL954360; CAI17190.1; -; Genomic_DNA.
DR   EMBL; AF250847; AAF86240.1; -; mRNA.
DR   EMBL; BC107105; AAI07106.1; -; mRNA.
DR   CCDS; CCDS44398.1; -. [Q9NR71-2]
DR   CCDS; CCDS7239.2; -. [Q9NR71-1]
DR   RefSeq; NP_001137446.1; NM_001143974.1. [Q9NR71-2]
DR   RefSeq; NP_063946.2; NM_019893.2. [Q9NR71-1]
DR   RefSeq; XP_011538272.1; XM_011539970.2. [Q9NR71-1]
DR   PDB; 4WGK; X-ray; 2.58 A; A/B=99-780.
DR   PDBsum; 4WGK; -.
DR   SMR; Q9NR71; -.
DR   STRING; 9606.ENSP00000378897; -.
DR   BindingDB; Q9NR71; -.
DR   ChEMBL; CHEMBL2021754; -.
DR   SwissLipids; SLP:000000163; -.
DR   iPTMnet; Q9NR71; -.
DR   PhosphoSitePlus; Q9NR71; -.
DR   BioMuta; ASAH2; -.
DR   DMDM; 110832757; -.
DR   MassIVE; Q9NR71; -.
DR   MaxQB; Q9NR71; -.
DR   PaxDb; Q9NR71; -.
DR   PeptideAtlas; Q9NR71; -.
DR   PRIDE; Q9NR71; -.
DR   ProteomicsDB; 82290; -. [Q9NR71-1]
DR   ProteomicsDB; 82291; -. [Q9NR71-2]
DR   Ensembl; ENST00000395526; ENSP00000378897; ENSG00000188611. [Q9NR71-1]
DR   Ensembl; ENST00000447815; ENSP00000388206; ENSG00000188611. [Q9NR71-2]
DR   Ensembl; ENST00000656090; ENSP00000499688; ENSG00000188611. [Q9NR71-1]
DR   GeneID; 56624; -.
DR   KEGG; hsa:56624; -.
DR   UCSC; uc001jjd.4; human. [Q9NR71-1]
DR   CTD; 56624; -.
DR   DisGeNET; 56624; -.
DR   EuPathDB; HostDB:ENSG00000188611.14; -.
DR   GeneCards; ASAH2; -.
DR   HGNC; HGNC:18860; ASAH2.
DR   HPA; HPA061171; -.
DR   MIM; 611202; gene.
DR   neXtProt; NX_Q9NR71; -.
DR   OpenTargets; ENSG00000188611; -.
DR   PharmGKB; PA134977109; -.
DR   eggNOG; KOG2232; Eukaryota.
DR   eggNOG; ENOG410XQWE; LUCA.
DR   GeneTree; ENSGT00390000015792; -.
DR   InParanoid; Q9NR71; -.
DR   KO; K12349; -.
DR   OMA; NADIAMG; -.
DR   OrthoDB; 967085at2759; -.
DR   PhylomeDB; Q9NR71; -.
DR   TreeFam; TF300786; -.
DR   BRENDA; 3.5.1.23; 2681.
DR   Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR   SABIO-RK; Q9NR71; -.
DR   UniPathway; UPA00222; -.
DR   ChiTaRS; ASAH2; human.
DR   GeneWiki; ASAH2; -.
DR   GenomeRNAi; 56624; -.
DR   Pharos; Q9NR71; Tbio.
DR   PRO; PR:Q9NR71; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q9NR71; protein.
DR   Bgee; ENSG00000188611; Expressed in 93 organ(s), highest expression level in intestine.
DR   ExpressionAtlas; Q9NR71; baseline and differential.
DR   Genevisible; Q9NR71; HS.
DR   GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071633; F:dihydroceramidase activity; IEA:Ensembl.
DR   GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; IDA:UniProtKB.
DR   GO; GO:0070774; F:phytoceramidase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:UniProtKB.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0046514; P:ceramide catabolic process; IDA:UniProtKB.
DR   GO; GO:0006672; P:ceramide metabolic process; IDA:UniProtKB.
DR   GO; GO:0044241; P:lipid digestion; ISS:UniProtKB.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:UniProtKB.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0006670; P:sphingosine metabolic process; IDA:UniProtKB.
DR   Gene3D; 2.60.40.2300; -; 1.
DR   InterPro; IPR006823; Ceramidase_alk.
DR   InterPro; IPR038445; NCDase_C_sf.
DR   InterPro; IPR031331; NEUT/ALK_ceramidase_C.
DR   InterPro; IPR031329; NEUT/ALK_ceramidase_N.
DR   PANTHER; PTHR12670; PTHR12670; 1.
DR   Pfam; PF04734; Ceramidase_alk; 1.
DR   Pfam; PF17048; Ceramidse_alk_C; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q9NR71.
DR   SWISS-2DPAGE; Q9NR71.
KW   3D-structure; Alternative splicing; Apoptosis; Calcium; Cell membrane;
KW   Disulfide bond; Glycoprotein; Golgi apparatus; Hydrolase; Lipid metabolism;
KW   Membrane; Metal-binding; Mitochondrion; Phosphoprotein; Polymorphism;
KW   Reference proteome; Secreted; Signal-anchor; Sphingolipid metabolism;
KW   Transmembrane; Transmembrane helix; Ubl conjugation; Zinc.
FT   CHAIN           1..780
FT                   /note="Neutral ceramidase"
FT                   /id="PRO_0000247099"
FT   CHAIN           99..780
FT                   /note="Neutral ceramidase soluble form"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XT9"
FT                   /id="PRO_0000247100"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..780
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          770..780
FT                   /note="Required for correct folding and localization"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XT9"
FT   ACT_SITE        354
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:16229686"
FT   METAL           134
FT                   /note="Calcium; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   METAL           194
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   METAL           303
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   METAL           540
FT                   /note="Zinc"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   METAL           579
FT                   /note="Zinc"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   METAL           712
FT                   /note="Calcium; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   METAL           714
FT                   /note="Calcium; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   METAL           717
FT                   /note="Calcium"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   SITE            98..99
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XT9"
FT   CARBOHYD        62
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        70
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        78
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        79
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   CARBOHYD        468
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        564
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        730
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   CARBOHYD        779
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        362..376
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   DISULFID        369..384
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   DISULFID        448..498
FT                   /evidence="ECO:0000244|PDB:4WGK,
FT                   ECO:0000269|PubMed:26190575"
FT   VAR_SEQ         410..444
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019928"
FT   VARIANT         51
FT                   /note="T -> A (in dbSNP:rs7067625)"
FT                   /id="VAR_027064"
FT   VARIANT         346
FT                   /note="A -> S (in dbSNP:rs993869)"
FT                   /id="VAR_027065"
FT   MUTAGEN         124
FT                   /note="G->R: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:26190575"
FT   MUTAGEN         194
FT                   /note="H->A: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:26190575"
FT   MUTAGEN         196
FT                   /note="H->A: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:26190575"
FT   MUTAGEN         211
FT                   /note="A->R: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:26190575"
FT   MUTAGEN         257
FT                   /note="R->A: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:26190575"
FT   MUTAGEN         258
FT                   /note="S->A: Decreased ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:16229686"
FT   MUTAGEN         303
FT                   /note="H->A: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:26190575"
FT   MUTAGEN         352
FT                   /note="D->S: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:16229686"
FT   MUTAGEN         354
FT                   /note="S->A: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:16229686"
FT   MUTAGEN         362
FT                   /note="C->A: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:16229686"
FT   MUTAGEN         374
FT                   /note="S->A: Decreased ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:16229686"
FT   MUTAGEN         396
FT                   /note="S->A: No effect on ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:16229686"
FT   MUTAGEN         465
FT                   /note="G->R: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:26190575"
FT   MUTAGEN         540
FT                   /note="E->A: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:26190575"
FT   MUTAGEN         579
FT                   /note="Y->F: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:26190575"
FT   MUTAGEN         591
FT                   /note="Y->F: Loss of ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:26190575"
FT   MUTAGEN         595
FT                   /note="S->A: Decreased ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:16229686"
FT   MUTAGEN         729
FT                   /note="S->A: Decreased ceramide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:16229686"
FT   CONFLICT        274
FT                   /note="S -> P (in Ref. 1; AAL06061 and 4; AAF86240)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        602
FT                   /note="T -> A (in Ref. 1; AAL06061 and 4; AAF86240)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        689
FT                   /note="T -> N (in Ref. 3; CAI17190)"
FT                   /evidence="ECO:0000305"
FT   STRAND          102..110
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          115..123
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          129..135
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          138..145
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          153..161
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           165..179
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          185..192
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          196..199
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           206..212
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           217..235
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          239..249
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          255..257
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           259..262
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           267..270
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          280..288
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          293..299
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           317..330
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          342..346
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          353..355
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          360..362
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   TURN            363..365
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   TURN            377..379
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           380..383
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          384..386
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          389..392
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           393..413
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          417..419
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          423..431
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          436..442
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          444..446
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           454..458
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           478..487
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           493..499
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          504..506
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           508..510
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          513..515
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          520..529
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          532..536
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          538..541
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           543..559
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          566..570
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          572..575
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          578..580
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           583..588
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           591..594
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           602..618
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           622..624
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          658..660
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          664..667
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          670..677
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   HELIX           681..684
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          693..700
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   TURN            701..704
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          705..711
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          717..723
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          729..736
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          744..756
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          764..771
FT                   /evidence="ECO:0000244|PDB:4WGK"
FT   STRAND          775..779
FT                   /evidence="ECO:0000244|PDB:4WGK"
SQ   SEQUENCE   780 AA;  85516 MW;  D2BD7947B022A619 CRC64;
     MAKRTFSNLE TFLIFLLVMM SAITVALLSL LFITSGTIEN HKDLGGHFFS TTQSPPATQG
     STAAQRSTAT QHSTATQSST ATQTSPVPLT PESPLFQNFS GYHIGVGRAD CTGQVADINL
     MGYGKSGQNA QGILTRLYSR AFIMAEPDGS NRTVFVSIDI GMVSQRLRLE VLNRLQSKYG
     SLYRRDNVIL SGTHTHSGPA GYFQYTVFVI ASEGFSNQTF QHMVTGILKS IDIAHTNMKP
     GKIFINKGNV DGVQINRSPY SYLQNPQSER ARYSSNTDKE MIVLKMVDLN GDDLGLISWF
     AIHPVSMNNS NHLVNSDNVG YASYLLEQEK NKGYLPGQGP FVAAFASSNL GDVSPNILGP
     RCINTGESCD NANSTCPIGG PSMCIAKGPG QDMFDSTQII GRAMYQRAKE LYASASQEVT
     GPLASAHQWV DMTDVTVWLN STHASKTCKP ALGYSFAAGT IDGVGGLNFT QGKTEGDPFW
     DTIRDQILGK PSEEIKECHK PKPILLHTGE LSKPHPWHPD IVDVQIITLG SLAITAIPGE
     FTTMSGRRLR EAVQAEFASH GMQNMTVVIS GLCNVYTHYI TTYEEYQAQR YEAASTIYGP
     HTLSAYIQLF RNLAKAIATD TVANLSRGPE PPFFKQLIVP LIPSIVDRAP KGRTFGDVLQ
     PAKPEYRVGE VAEVIFVGAN PKNSVQNQTH QTFLTVEKYE ATSTSWQIVC NDASWETRFY
     WHKGLLGLSN ATVEWHIPDT AQPGIYRIRY FGHNRKQDIL KPAVILSFEG TSPAFEVVTI
//

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