(data stored in SCRATCH zone)

SWISSPROT: NEP_HUMAN

ID   NEP_HUMAN               Reviewed;         750 AA.
AC   P08473; A8K6U6; D3DNJ9; Q3MIX4;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   11-DEC-2019, entry version 228.
DE   RecName: Full=Neprilysin;
DE            EC=3.4.24.11 {ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:27588448, ECO:0000269|PubMed:8168535};
DE   AltName: Full=Atriopeptidase;
DE   AltName: Full=Common acute lymphocytic leukemia antigen;
DE            Short=CALLA;
DE   AltName: Full=Enkephalinase;
DE   AltName: Full=Neutral endopeptidase 24.11;
DE            Short=NEP;
DE            Short=Neutral endopeptidase;
DE   AltName: Full=Skin fibroblast elastase;
DE            Short=SFE;
DE   AltName: CD_antigen=CD10;
GN   Name=MME; Synonyms=EPN;
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 [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=2971756; DOI=10.1084/jem.168.4.1247;
RA   Letarte M., Vera S., Tran R., Addis J.B.L., Onizuka R.J., Quackenbush E.J.,
RA   Jongeneel C.V., McInnes R.R.;
RT   "Common acute lymphocytic leukemia antigen is identical to neutral
RT   endopeptidase.";
RL   J. Exp. Med. 168:1247-1253(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2968607; DOI=10.1073/pnas.85.13.4819;
RA   Shipp M.A., Richardson N.E., Sayre P.H., Brown N.R., Masteller E.L.,
RA   Clayton L.K., Ritz J., Reinherz E.L.;
RT   "Molecular cloning of the common acute lymphoblastic leukemia antigen
RT   (CALLA) identifies a type II integral membrane protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:4819-4823(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2528730; DOI=10.1073/pnas.86.18.7103;
RA   D'Adamio L., Shipp M.A., Masteller E.L., Reinherz E.L.;
RT   "Organization of the gene encoding common acute lymphoblastic leukemia
RT   antigen (neutral endopeptidase 24.11): multiple miniexons and separate 5'
RT   untranslated regions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:7103-7107(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-750.
RC   TISSUE=Placenta;
RX   PubMed=3162217; DOI=10.1016/0014-5793(88)80828-7;
RA   Malfroy B., Kuang W.-J., Seeburg P.H., Mason A.J., Schofield P.R.;
RT   "Molecular cloning and amino acid sequence of human enkephalinase (neutral
RT   endopeptidase).";
RL   FEBS Lett. 229:206-210(1988).
RN   [9]
RP   FUNCTION.
RX   PubMed=2972276; DOI=10.1042/bj2540531;
RA   Vanneste Y., Michel A., Dimaline R., Najdovski T., Deschodt-Lanckman M.;
RT   "Hydrolysis of alpha-human atrial natriuretic peptide in vitro by human
RT   kidney membranes and purified endopeptidase-24.11. Evidence for a novel
RT   cleavage site.";
RL   Biochem. J. 254:531-537(1988).
RN   [10]
RP   FUNCTION IN THE DEGRADATION OF ANF.
RX   PubMed=2531377; DOI=10.1016/0196-9781(89)90131-9;
RA   Yandle T.G., Brennan S.O., Espiner E.A., Nicholls M.G., Richards A.M.;
RT   "Endopeptidase-24.11 in human plasma degrades atrial natriuretic factor
RT   (ANF) to ANF(99-105/106-126).";
RL   Peptides 10:891-894(1989).
RN   [11]
RP   ACTIVE SITE ASP-651, AND CATALYTIC ACTIVITY.
RX   PubMed=8168535; DOI=10.1111/j.1432-1033.1994.tb18760.x;
RA   Le Moual H., Dion N., Roques B.P., Crine P., Boileau G.;
RT   "Asp650 is crucial for catalytic activity of neutral endopeptidase 24-11.";
RL   Eur. J. Biochem. 221:475-480(1994).
RN   [12]
RP   GLYCOSYLATION AT ASN-145 AND ASN-285.
RX   PubMed=12754519; DOI=10.1038/nbt827;
RA   Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT   "Identification and quantification of N-linked glycoproteins using
RT   hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL   Nat. Biotechnol. 21:660-666(2003).
RN   [13]
RP   FUNCTION IN ANGIOTENSIN PEPTIDE METABOLISM, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND CATALYTIC ACTIVITY.
RX   PubMed=15283675; DOI=10.1042/bj20040634;
RA   Rice G.I., Thomas D.A., Grant P.J., Turner A.J., Hooper N.M.;
RT   "Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and
RT   neprilysin in angiotensin peptide metabolism.";
RL   Biochem. J. 383:45-51(2004).
RN   [14]
RP   FUNCTION, AND INHIBITION BY OPIORPHIN.
RX   PubMed=17101991; DOI=10.1073/pnas.0605865103;
RA   Wisner A., Dufour E., Messaoudi M., Nejdi A., Marcel A., Ungeheuer M.-N.,
RA   Rougeot C.;
RT   "Human opiorphin, a natural antinociceptive modulator of opioid-dependent
RT   pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:17979-17984(2006).
RN   [15]
RP   IDENTIFICATION AS SKIN FIBROBLAST ELASTASE, AND FUNCTION.
RX   PubMed=20876573; DOI=10.1074/jbc.m110.161547;
RA   Morisaki N., Moriwaki S., Sugiyama-Nakagiri Y., Haketa K., Takema Y.,
RA   Imokawa G.;
RT   "Neprilysin is identical to skin fibroblast elastase: its role in skin
RT   aging and UV responses.";
RL   J. Biol. Chem. 285:39819-39827(2010).
RN   [16]
RP   MYRISTOYLATION AT GLY-2.
RX   PubMed=19756956; DOI=10.1007/s11010-009-0253-8;
RA   Zheng R., Horiguchi A., Iida K., Lee J., Shen R., Goodman O.B. Jr.,
RA   Nanus D.M.;
RT   "Neutral endopeptidase is a myristoylated protein.";
RL   Mol. Cell. Biochem. 335:173-180(2010).
RN   [17]
RP   GLYCOSYLATION AT ASN-628.
RX   PubMed=22766194; DOI=10.1016/j.bbagen.2012.06.017;
RA   Sato B., Katagiri Y.U., Iijima K., Yamada H., Ito S., Kawasaki N.,
RA   Okita H., Fujimoto J., Kiyokawa N.;
RT   "The human CD10 lacking an N-glycan at Asn(628) is deficient in surface
RT   expression and neutral endopeptidase activity.";
RL   Biochim. Biophys. Acta 1820:1715-1723(2012).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-6, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [19]
RP   FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN CMT2T, VARIANTS CMT2T ALA-12;
RP   CYS-347; PRO-348 AND ASP-422, AND CHARACTERIZATION OF VARIANTS CMT2T
RP   CYS-347 AND ASP-422.
RX   PubMed=27588448; DOI=10.1016/j.ajhg.2016.07.008;
RA   Auer-Grumbach M., Toegel S., Schabhuettl M., Weinmann D., Chiari C.,
RA   Bennett D.L., Beetz C., Klein D., Andersen P.M., Boehme I., Fink-Puches R.,
RA   Gonzalez M., Harms M.B., Motley W., Reilly M.M., Renner W.,
RA   Rudnik-Schoeneborn S., Schlotter-Weigel B., Themistocleous A.C.,
RA   Weishaupt J.H., Ludolph A.C., Wieland T., Tao F., Abreu L., Windhager R.,
RA   Zitzelsberger M., Strom T.M., Walther T., Scherer S.S., Zuechner S.,
RA   Martini R., Senderek J.;
RT   "Rare variants in MME, encoding metalloprotease neprilysin, are linked to
RT   late-onset autosomal-dominant axonal polyneuropathies.";
RL   Am. J. Hum. Genet. 99:607-623(2016).
RN   [20]
RP   INVOLVEMENT IN CMT2T, VARIANTS CMT2T CYS-411 DEL AND ARG-621, VARIANT
RP   HIS-497, AND CHARACTERIZATION OF VARIANT CMT2T ARG-621.
RX   PubMed=26991897; DOI=10.1002/ana.24612;
RA   Higuchi Y., Hashiguchi A., Yuan J., Yoshimura A., Mitsui J., Ishiura H.,
RA   Tanaka M., Ishihara S., Tanabe H., Nozuma S., Okamoto Y., Matsuura E.,
RA   Ohkubo R., Inamizu S., Shiraishi W., Yamasaki R., Ohyagi Y., Kira J.,
RA   Oya Y., Yabe H., Nishikawa N., Tobisawa S., Matsuda N., Masuda M.,
RA   Kugimoto C., Fukushima K., Yano S., Yoshimura J., Doi K., Nakagawa M.,
RA   Morishita S., Tsuji S., Takashima H.;
RT   "Mutations in MME cause an autosomal-recessive Charcot-Marie-Tooth disease
RT   type 2.";
RL   Ann. Neurol. 79:659-672(2016).
RN   [21]
RP   INVOLVEMENT IN SCA43, AND VARIANT SCA43 TYR-143.
RX   PubMed=27583304; DOI=10.1212/nxg.0000000000000094;
RA   Depondt C., Donatello S., Rai M., Wang F.C., Manto M., Simonis N.,
RA   Pandolfo M.;
RT   "MME mutation in dominant spinocerebellar ataxia with neuropathy (SCA43).";
RL   Neurol. Genet. 2:E94-E94(2016).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND GLYCOSYLATION AT ASN-145;
RP   ASN-325 AND ASN-628.
RX   PubMed=10669592; DOI=10.1006/jmbi.1999.3492;
RA   Oefner C., D'Arcy A., Hennig M., Winkler F.K., Dale G.E.;
RT   "Structure of human neutral endopeptidase (Neprilysin) complexed with
RT   phosphoramidon.";
RL   J. Mol. Biol. 296:341-349(2000).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 55-750 IN COMPLEXES WITH ZINC
RP   IONS AND SYNTHETIC INHIBITORS, DISULFIDE BONDS, COFACTOR, AND GLYCOSYLATION
RP   AT ASN-145; ASN-325 AND ASN-628.
RX   PubMed=14747736; DOI=10.1107/s0907444903027410;
RA   Oefner C., Roques B.P., Fournie-Zaluski M.-C., Dale G.E.;
RT   "Structural analysis of neprilysin with various specific and potent
RT   inhibitors.";
RL   Acta Crystallogr. D 60:392-396(2004).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 55-750 IN COMPLEX WITH ZINC IONS
RP   AND THE SYNTHETIC INHIBITOR MCB3937, DISULFIDE BONDS, COFACTOR, AND
RP   GLYCOSYLATION AT ASN-145; ASN-325 AND ASN-628.
RX   PubMed=17704566; DOI=10.1107/s0907444907036281;
RA   Oefner C., Pierau S., Schulz H., Dale G.E.;
RT   "Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV.";
RL   Acta Crystallogr. D 63:975-981(2007).
CC   -!- FUNCTION: Thermolysin-like specificity, but is almost confined on
CC       acting on polypeptides of up to 30 amino acids (PubMed:15283675,
CC       PubMed:8168535). Biologically important in the destruction of opioid
CC       peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond
CC       (PubMed:17101991). Able to cleave angiotensin-1, angiotensin-2 and
CC       angiotensin 1-9 (PubMed:15283675). Involved in the degradation of
CC       atrial natriuretic factor (ANF) (PubMed:2531377, PubMed:2972276).
CC       Displays UV-inducible elastase activity toward skin preelastic and
CC       elastic fibers (PubMed:20876573). {ECO:0000269|PubMed:15283675,
CC       ECO:0000269|PubMed:17101991, ECO:0000269|PubMed:20876573,
CC       ECO:0000269|PubMed:2531377, ECO:0000269|PubMed:27588448,
CC       ECO:0000269|PubMed:2972276}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of polypeptides between hydrophobic
CC         residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11;
CC         Evidence={ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:27588448,
CC         ECO:0000269|PubMed:8168535};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14747736,
CC       ECO:0000269|PubMed:17704566};
CC   -!- ACTIVITY REGULATION: Inhibited in a dose dependent manner by opiorphin.
CC       {ECO:0000269|PubMed:17101991}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=55.1 uM for angiotensin-1 {ECO:0000269|PubMed:15283675};
CC         KM=179 uM for angiotensin-2 {ECO:0000269|PubMed:15283675};
CC         KM=111.4 uM for angiotensin 1-9 {ECO:0000269|PubMed:15283675};
CC   -!- INTERACTION:
CC       P21926:CD9; NbExp=6; IntAct=EBI-353759, EBI-4280101;
CC       P08107:HSPA1B; NbExp=3; IntAct=EBI-353759, EBI-629985;
CC       P04792:HSPB1; NbExp=4; IntAct=EBI-353759, EBI-352682;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC       protein.
CC   -!- PTM: Myristoylation is a determinant of membrane targeting.
CC       {ECO:0000269|PubMed:19756956}.
CC   -!- PTM: Glycosylation at Asn-628 is necessary both for surface expression
CC       and neutral endopeptidase activity. {ECO:0000269|PubMed:10669592,
CC       ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14747736,
CC       ECO:0000269|PubMed:17704566, ECO:0000269|PubMed:22766194}.
CC   -!- DISEASE: Charcot-Marie-Tooth disease 2T (CMT2T) [MIM:617017]: An axonal
CC       form of Charcot-Marie-Tooth disease, a disorder of the peripheral
CC       nervous system, characterized by progressive weakness and atrophy,
CC       initially of the peroneal muscles and later of the distal muscles of
CC       the arms. Charcot-Marie-Tooth disease is classified in two main groups
CC       on the basis of electrophysiologic properties and histopathology:
CC       primary peripheral demyelinating neuropathies (designated CMT1 when
CC       they are dominantly inherited) and primary peripheral axonal
CC       neuropathies (CMT2). Neuropathies of the CMT2 group are characterized
CC       by signs of axonal degeneration in the absence of obvious myelin
CC       alterations, normal or slightly reduced nerve conduction velocities,
CC       and progressive distal muscle weakness and atrophy.
CC       {ECO:0000269|PubMed:26991897, ECO:0000269|PubMed:27588448}. Note=The
CC       disease is caused by mutations affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Spinocerebellar ataxia 43 (SCA43) [MIM:617018]: A form of
CC       spinocerebellar ataxia, a clinically and genetically heterogeneous
CC       group of cerebellar disorders. Patients show progressive incoordination
CC       of gait and often poor coordination of hands, speech and eye movements,
CC       due to degeneration of the cerebellum with variable involvement of the
CC       brainstem and spinal cord. SCA43 is a slowly progressive, autosomal
CC       dominant form. {ECO:0000269|PubMed:27583304}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: Important cell surface marker in the diagnostic of human
CC       acute lymphocytic leukemia.
CC   -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01233, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA30157.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/MMEID41386ch3q25.html";
DR   EMBL; Y00811; CAA68752.1; -; mRNA.
DR   EMBL; J03779; AAA51915.1; -; mRNA.
DR   EMBL; M26628; AAA52294.1; -; Genomic_DNA.
DR   EMBL; M26607; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26608; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26609; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26610; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26611; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26612; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26613; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26614; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26615; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26616; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26617; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26618; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26619; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26620; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26621; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26622; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26623; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26624; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26625; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26626; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; M26627; AAA52294.1; JOINED; Genomic_DNA.
DR   EMBL; AK291761; BAF84450.1; -; mRNA.
DR   EMBL; EU326307; ACA05913.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78754.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78755.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78756.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78757.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78758.1; -; Genomic_DNA.
DR   EMBL; BC101632; AAI01633.1; -; mRNA.
DR   EMBL; BC101658; AAI01659.1; -; mRNA.
DR   EMBL; X07166; CAA30157.1; ALT_INIT; mRNA.
DR   CCDS; CCDS3172.1; -.
DR   PIR; A41387; HYHUN.
DR   RefSeq; NP_000893.2; NM_000902.3.
DR   RefSeq; NP_009218.2; NM_007287.2.
DR   RefSeq; NP_009219.2; NM_007288.2.
DR   RefSeq; NP_009220.2; NM_007289.2.
DR   RefSeq; XP_006713709.1; XM_006713646.3.
DR   RefSeq; XP_006713710.1; XM_006713647.3.
DR   RefSeq; XP_011511157.1; XM_011512855.2.
DR   RefSeq; XP_011511158.1; XM_011512856.2.
DR   RefSeq; XP_011511159.1; XM_011512857.2.
DR   PDB; 1DL9; Model; -; A=508-750.
DR   PDB; 1DMT; X-ray; 2.10 A; A=55-750.
DR   PDB; 1QVD; Model; -; A=55-750.
DR   PDB; 1R1H; X-ray; 1.95 A; A=55-750.
DR   PDB; 1R1I; X-ray; 2.60 A; A=55-750.
DR   PDB; 1R1J; X-ray; 2.35 A; A=55-750.
DR   PDB; 1Y8J; X-ray; 2.25 A; A=55-750.
DR   PDB; 2QPJ; X-ray; 2.05 A; A=55-750.
DR   PDB; 2YB9; X-ray; 2.40 A; A=55-750.
DR   PDB; 4CTH; X-ray; 2.15 A; A=52-750.
DR   PDB; 5JMY; X-ray; 2.00 A; A/B=53-750.
DR   PDB; 6GID; X-ray; 1.90 A; A=55-750.
DR   PDB; 6SH1; X-ray; 2.10 A; AAA/CCC=55-750.
DR   PDB; 6SH2; X-ray; 2.60 A; AAA=55-750.
DR   PDBsum; 1DL9; -.
DR   PDBsum; 1DMT; -.
DR   PDBsum; 1QVD; -.
DR   PDBsum; 1R1H; -.
DR   PDBsum; 1R1I; -.
DR   PDBsum; 1R1J; -.
DR   PDBsum; 1Y8J; -.
DR   PDBsum; 2QPJ; -.
DR   PDBsum; 2YB9; -.
DR   PDBsum; 4CTH; -.
DR   PDBsum; 5JMY; -.
DR   PDBsum; 6GID; -.
DR   PDBsum; 6SH1; -.
DR   PDBsum; 6SH2; -.
DR   SMR; P08473; -.
DR   BioGrid; 110455; 106.
DR   IntAct; P08473; 100.
DR   MINT; P08473; -.
DR   STRING; 9606.ENSP00000418525; -.
DR   BindingDB; P08473; -.
DR   ChEMBL; CHEMBL1944; -.
DR   DrugBank; DB08575; 2-[(1S)-1-BENZYL-2-SULFANYLETHYL]-1H-IMIDAZO[4,5-C]PYRIDIN-5-IUM.
DR   DrugBank; DB02597; [2(R,S)-2-Sulfanylheptanoyl]-Phe-Ala.
DR   DrugBank; DB00616; Candoxatril.
DR   DrugBank; DB11623; Candoxatrilat.
DR   DrugBank; DB05796; Daglutril.
DR   DrugBank; DB06655; Liraglutide.
DR   DrugBank; DB02558; N-(3-Phenyl-2-Sulfanylpropanoyl)Phenylalanylalanine.
DR   DrugBank; DB02062; N-[3-[(1-Aminoethyl)(Hydroxy)Phosphoryl]-2-(1,1'-Biphenyl-4-Ylmethyl)Propanoyl]Alanine.
DR   DrugBank; DB00886; Omapatrilat.
DR   DrugBank; DB02557; Phosphoramidon.
DR   DrugBank; DB09292; Sacubitril.
DR   DrugBank; DB13928; Semaglutide.
DR   DrugBank; DB08626; Thiorphan.
DR   DrugCentral; P08473; -.
DR   GuidetoPHARMACOLOGY; 1611; -.
DR   MEROPS; M13.001; -.
DR   CarbonylDB; P08473; -.
DR   GlyConnect; 1541; -.
DR   iPTMnet; P08473; -.
DR   PhosphoSitePlus; P08473; -.
DR   BioMuta; MME; -.
DR   DMDM; 128062; -.
DR   EPD; P08473; -.
DR   jPOST; P08473; -.
DR   MassIVE; P08473; -.
DR   MaxQB; P08473; -.
DR   PaxDb; P08473; -.
DR   PeptideAtlas; P08473; -.
DR   PRIDE; P08473; -.
DR   ProteomicsDB; 52110; -.
DR   Ensembl; ENST00000360490; ENSP00000353679; ENSG00000196549.
DR   Ensembl; ENST00000460393; ENSP00000418525; ENSG00000196549.
DR   Ensembl; ENST00000462745; ENSP00000419653; ENSG00000196549.
DR   Ensembl; ENST00000492661; ENSP00000420389; ENSG00000196549.
DR   Ensembl; ENST00000493237; ENSP00000417079; ENSG00000196549.
DR   Ensembl; ENST00000615825; ENSP00000478173; ENSG00000196549.
DR   GeneID; 4311; -.
DR   KEGG; hsa:4311; -.
DR   UCSC; uc003fab.2; human.
DR   CTD; 4311; -.
DR   DisGeNET; 4311; -.
DR   EuPathDB; HostDB:ENSG00000196549.10; -.
DR   GeneCards; MME; -.
DR   GeneReviews; MME; -.
DR   HGNC; HGNC:7154; MME.
DR   HPA; CAB000013; -.
DR   HPA; HPA052583; -.
DR   HPA; HPA056072; -.
DR   MalaCards; MME; -.
DR   MIM; 120520; gene.
DR   MIM; 617017; phenotype.
DR   MIM; 617018; phenotype.
DR   neXtProt; NX_P08473; -.
DR   OpenTargets; ENSG00000196549; -.
DR   Orphanet; 495274; Charcot-Marie-Tooth disease type 2T.
DR   Orphanet; 497757; MME-related autosomal dominant Charcot Marie Tooth disease type 2.
DR   Orphanet; 497764; Spinocerebellar ataxia type 43.
DR   PharmGKB; PA30864; -.
DR   eggNOG; KOG3624; Eukaryota.
DR   eggNOG; COG3590; LUCA.
DR   GeneTree; ENSGT00940000156745; -.
DR   HOGENOM; HOG000245574; -.
DR   InParanoid; P08473; -.
DR   KO; K01389; -.
DR   OMA; LSQCMVY; -.
DR   OrthoDB; 1450599at2759; -.
DR   PhylomeDB; P08473; -.
DR   TreeFam; TF315192; -.
DR   BRENDA; 3.4.24.11; 2681.
DR   Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SIGNOR; P08473; -.
DR   ChiTaRS; MME; human.
DR   EvolutionaryTrace; P08473; -.
DR   GeneWiki; Neprilysin; -.
DR   GenomeRNAi; 4311; -.
DR   Pharos; P08473; Tclin.
DR   PRO; PR:P08473; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P08473; protein.
DR   Bgee; ENSG00000196549; Expressed in 156 organ(s), highest expression level in metanephric glomerulus.
DR   ExpressionAtlas; P08473; baseline and differential.
DR   Genevisible; P08473; HS.
DR   GO; GO:0030424; C:axon; IGI:ARUK-UCL.
DR   GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; NAS:ARUK-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:ARUK-UCL.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0005769; C:early endosome; IDA:ARUK-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IDA:ARUK-UCL.
DR   GO; GO:0044306; C:neuron projection terminus; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IGI:ARUK-UCL.
DR   GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:ARUK-UCL.
DR   GO; GO:1901612; F:cardiolipin binding; IDA:ARUK-UCL.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008238; F:exopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008237; F:metallopeptidase activity; EXP:Reactome.
DR   GO; GO:0070012; F:oligopeptidase activity; IEA:Ensembl.
DR   GO; GO:0042277; F:peptide binding; ISS:UniProtKB.
DR   GO; GO:0001786; F:phosphatidylserine binding; IDA:ARUK-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0007568; P:aging; IEP:ARUK-UCL.
DR   GO; GO:0097242; P:amyloid-beta clearance; IDA:ARUK-UCL.
DR   GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IDA:ARUK-UCL.
DR   GO; GO:0050435; P:amyloid-beta metabolic process; ISS:UniProtKB.
DR   GO; GO:0002003; P:angiotensin maturation; TAS:Reactome.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:UniProtKB.
DR   GO; GO:0071492; P:cellular response to UV-A; IDA:UniProtKB.
DR   GO; GO:0071493; P:cellular response to UV-B; IDA:UniProtKB.
DR   GO; GO:0046449; P:creatinine metabolic process; IMP:UniProtKB.
DR   GO; GO:0001822; P:kidney development; IEP:UniProtKB.
DR   GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0061837; P:neuropeptide processing; IGI:ARUK-UCL.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0006518; P:peptide metabolic process; ISS:UniProtKB.
DR   GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IGI:ARUK-UCL.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   GO; GO:0090399; P:replicative senescence; IEP:UniProtKB.
DR   GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR   CDD; cd08662; M13; 1.
DR   Gene3D; 1.10.1380.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR029727; MME/CD10/NEP.
DR   InterPro; IPR000718; Peptidase_M13.
DR   InterPro; IPR018497; Peptidase_M13_C.
DR   InterPro; IPR042089; Peptidase_M13_dom_2.
DR   InterPro; IPR008753; Peptidase_M13_N.
DR   PANTHER; PTHR11733; PTHR11733; 1.
DR   PANTHER; PTHR11733:SF114; PTHR11733:SF114; 1.
DR   Pfam; PF01431; Peptidase_M13; 1.
DR   Pfam; PF05649; Peptidase_M13_N; 1.
DR   PRINTS; PR00786; NEPRILYSIN.
DR   PROSITE; PS51885; NEPRILYSIN; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P08473.
DR   SWISS-2DPAGE; P08473.
KW   3D-structure; Cell membrane; Charcot-Marie-Tooth disease; Disease mutation;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lipoprotein; Membrane;
KW   Metal-binding; Metalloprotease; Myristate; Neurodegeneration; Neuropathy;
KW   Phosphoprotein; Protease; Reference proteome; Signal-anchor;
KW   Spinocerebellar ataxia; Transmembrane; Transmembrane helix; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..750
FT                   /note="Neprilysin"
FT                   /id="PRO_0000078213"
FT   TOPO_DOM        2..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        29..51
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..750
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          56..750
FT                   /note="Peptidase M13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   MOTIF           16..23
FT                   /note="Stop-transfer sequence"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        585
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        651
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000269|PubMed:8168535"
FT   METAL           584
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   METAL           588
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   METAL           647
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   BINDING         103
FT                   /note="Substrate carboxyl"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:19756956"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10669592,
FT                   ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14747736,
FT                   ECO:0000269|PubMed:17704566"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754519"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10669592,
FT                   ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566"
FT   CARBOHYD        628
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10669592,
FT                   ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566,
FT                   ECO:0000269|PubMed:22766194"
FT   DISULFID        57..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        80..735
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        88..695
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        143..411
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        234..242
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        621..747
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   VARIANT         12
FT                   /note="D -> A (in CMT2T; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:27588448"
FT                   /id="VAR_077684"
FT   VARIANT         143
FT                   /note="C -> Y (in SCA43; dbSNP:rs879255651)"
FT                   /evidence="ECO:0000269|PubMed:27583304"
FT                   /id="VAR_077685"
FT   VARIANT         347
FT                   /note="Y -> C (in CMT2T; results in reduction of neprilysin
FT                   activity; dbSNP:rs138218277)"
FT                   /evidence="ECO:0000269|PubMed:27588448"
FT                   /id="VAR_077686"
FT   VARIANT         348
FT                   /note="A -> P (in CMT2T; unknown pathological significance;
FT                   dbSNP:rs199567914)"
FT                   /evidence="ECO:0000269|PubMed:27588448"
FT                   /id="VAR_077687"
FT   VARIANT         411
FT                   /note="Missing (in CMT2T; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:26991897"
FT                   /id="VAR_077688"
FT   VARIANT         422
FT                   /note="A -> D (in CMT2T; late-onset form; results in
FT                   reduction of neprilysin activity; dbSNP:rs777476150)"
FT                   /evidence="ECO:0000269|PubMed:27588448"
FT                   /id="VAR_077689"
FT   VARIANT         497
FT                   /note="Y -> H (in dbSNP:rs200308207)"
FT                   /evidence="ECO:0000269|PubMed:26991897"
FT                   /id="VAR_077690"
FT   VARIANT         621
FT                   /note="C -> R (in CMT2T; decrease of protein expression;
FT                   dbSNP:rs879253752)"
FT                   /evidence="ECO:0000269|PubMed:26991897"
FT                   /id="VAR_077691"
FT   CONFLICT        26
FT                   /note="P -> R (in Ref. 4; AAA51915)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="T -> R (in Ref. 4; AAA51915)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="T -> R (in Ref. 4; AAA51915)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        304
FT                   /note="T -> R (in Ref. 4; AAA51915)"
FT                   /evidence="ECO:0000305"
FT   HELIX           60..72
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   TURN            79..81
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           83..94
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          102..105
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           106..123
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           131..144
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           146..152
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           155..160
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           161..164
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           168..170
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          171..173
FT                   /evidence="ECO:0000244|PDB:1R1H"
FT   HELIX           174..177
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   TURN            178..181
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           184..195
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          200..208
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          211..220
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          225..228
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           229..233
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           236..238
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           239..260
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           266..286
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           290..292
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           296..299
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          302..304
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           305..311
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          316..319
FT                   /evidence="ECO:0000244|PDB:1R1H"
FT   HELIX           323..331
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           332..334
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          343..347
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           349..359
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           364..379
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           380..382
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           385..399
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           407..418
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           420..431
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           436..457
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          459..461
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           463..475
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          477..481
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           485..488
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           490..496
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   TURN            497..499
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           507..523
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   TURN            524..527
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          545..547
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   TURN            548..551
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          552..556
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           557..559
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   TURN            562..564
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          567..569
FT                   /evidence="ECO:0000244|PDB:2YB9"
FT   HELIX           571..576
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           578..588
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           594..596
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           609..627
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           632..634
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          636..638
FT                   /evidence="ECO:0000244|PDB:2YB9"
FT   TURN            641..644
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           645..669
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           682..693
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   STRAND          696..698
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           700..709
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           715..724
FT                   /evidence="ECO:0000244|PDB:6GID"
FT   HELIX           727..733
FT                   /evidence="ECO:0000244|PDB:6GID"
SQ   SEQUENCE   750 AA;  85514 MW;  BCF3827C39898630 CRC64;
     MGKSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA TYDDGICKSS
     DCIKSAARLI QNMDATTEPC TDFFKYACGG WLKRNVIPET SSRYGNFDIL RDELEVVLKD
     VLQEPKTEDI VAVQKAKALY RSCINESAID SRGGEPLLKL LPDIYGWPVA TENWEQKYGA
     SWTAEKAIAQ LNSKYGKKVL INLFVGTDDK NSVNHVIHID QPRLGLPSRD YYECTGIYKE
     ACTAYVDFMI SVARLIRQEE RLPIDENQLA LEMNKVMELE KEIANATAKP EDRNDPMLLY
     NKMTLAQIQN NFSLEINGKP FSWLNFTNEI MSTVNISITN EEDVVVYAPE YLTKLKPILT
     KYSARDLQNL MSWRFIMDLV SSLSRTYKES RNAFRKALYG TTSETATWRR CANYVNGNME
     NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKRAE EKALAIKERI
     GYPDDIVSND NKLNNEYLEL NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA
     VVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
     GDLVDWWTQQ SASNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGLGQAYR
     AYQNYIKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII
     GTLQNSAEFS EAFHCRKNSY MNPEKKCRVW
//

If you have problems or comments...

PBIL Back to PBIL home page