(data stored in SCRATCH zone)

SWISSPROT: CNNM2_HUMAN

ID   CNNM2_HUMAN             Reviewed;         875 AA.
AC   Q9H8M5; Q5T569; Q5T570; Q8WU59; Q9H952; Q9NRK5; Q9NXT4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   30-AUG-2017, entry version 120.
DE   RecName: Full=Metal transporter CNNM2;
DE   AltName: Full=Ancient conserved domain-containing protein 2;
DE   AltName: Full=Cyclin-M2;
GN   Name=CNNM2; Synonyms=ACDP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 242-875 (ISOFORM 1).
RC   TISSUE=Colon, Placenta, and Teratocarcinoma;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [2]
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.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=B-cell;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 210-875 (ISOFORM 1).
RX   PubMed=12657465; DOI=10.1016/S0378-1119(02)01210-6;
RA   Wang C.-Y., Shi J.-D., Yang P., Kumar P.G., Li Q.-Z., Run Q.-G.,
RA   Su Y.-C., Scott H.S., Kao K.-J., She J.-X.;
RT   "Molecular cloning and characterization of a novel gene family of four
RT   ancient conserved domain proteins (ACDP).";
RL   Gene 306:37-44(2003).
RN   [5]
RP   TISSUE SPECIFICITY, VARIANT HOMG6 ILE-568, CHARACTERIZATION OF VARIANT
RP   HOMG6 ILE-568, AND VARIANT GLN-38.
RX   PubMed=21397062; DOI=10.1016/j.ajhg.2011.02.005;
RA   Stuiver M., Lainez S., Will C., Terryn S., Gunzel D., Debaix H.,
RA   Sommer K., Kopplin K., Thumfart J., Kampik N.B., Querfeld U.,
RA   Willnow T.E., Nemec V., Wagner C.A., Hoenderop J.G., Devuyst O.,
RA   Knoers N.V., Bindels R.J., Meij I.C., Muller D.;
RT   "CNNM2, encoding a basolateral protein required for renal Mg2+
RT   handling, is mutated in dominant hypomagnesemia.";
RL   Am. J. Hum. Genet. 88:333-343(2011).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-761, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [7]
RP   INVOLVEMENT IN HOMGSMR, VARIANTS HOMGSMR LYS-122; TRP-269; PHE-330 AND
RP   LYS-357, AND CHARACTERIZATION OF VARIANTS HOMGSMR LYS-122; TRP-269 AND
RP   LYS-357.
RX   PubMed=24699222; DOI=10.1371/journal.pgen.1004267;
RA   Arjona F.J., de Baaij J.H., Schlingmann K.P., Lameris A.L.,
RA   van Wijk E., Flik G., Regele S., Korenke G.C., Neophytou B., Rust S.,
RA   Reintjes N., Konrad M., Bindels R.J., Hoenderop J.G.;
RT   "CNNM2 mutations cause impaired brain development and seizures in
RT   patients with hypomagnesemia.";
RL   PLoS Genet. 10:E1004267-E1004267(2014).
CC   -!- FUNCTION: Divalent metal cation transporter. Mediates transport of
CC       divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) >
CC       Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+) (By similarity).
CC       {ECO:0000250|UniProtKB:Q3TWN3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9H8M5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H8M5-2; Sequence=VSP_027080;
CC       Name=3;
CC         IsoId=Q9H8M5-3; Sequence=VSP_027077, VSP_027078;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC       brain, kidney and placenta, while it is weakly expressed in
CC       skeletal muscle. In the kidney, it is expressed in the distal
CC       convoluted tubule and the thick ascending limb of Henle loop.
CC       {ECO:0000269|PubMed:21397062}.
CC   -!- DISEASE: Hypomagnesemia 6 (HOMG6) [MIM:613882]: A renal disease
CC       characterized by severely lowered serum magnesium levels in the
CC       absence of other electrolyte disturbances. Affected individuals
CC       show an inappropriately normal urinary magnesium excretion,
CC       demonstrating a defect in tubular reabsorption. Age of clinical
CC       onset is highly variable and some affected individuals are
CC       asymptomatic. {ECO:0000269|PubMed:21397062}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Hypomagnesemia, seizures, and mental retardation
CC       (HOMGSMR) [MIM:616418]: A disease characterized by renal wasting
CC       of magnesium, low serum magnesium, seizures, and variable degrees
CC       of delayed psychomotor development. {ECO:0000269|PubMed:24699222}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- MISCELLANEOUS: Shares weak sequence similarity with the cyclin
CC       family, hence its name. However, it has no cyclin-like function in
CC       vivo.
CC   -!- SIMILARITY: Belongs to the ACDP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF86374.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAA90926.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAB14386.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=CAI16511.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAI16512.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAI40076.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAI40077.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AK000071; BAA90926.1; ALT_INIT; mRNA.
DR   EMBL; AK023066; BAB14386.1; ALT_INIT; mRNA.
DR   EMBL; AK023479; BAB14585.1; -; mRNA.
DR   EMBL; AL356608; CAI16511.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL139817; CAI16511.1; JOINED; Genomic_DNA.
DR   EMBL; AL356608; CAI16512.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL139817; CAI16512.1; JOINED; Genomic_DNA.
DR   EMBL; AL356608; CAI16513.1; -; Genomic_DNA.
DR   EMBL; AL139817; CAI40076.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL356608; CAI40076.1; JOINED; Genomic_DNA.
DR   EMBL; AL139817; CAI40077.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL356608; CAI40077.1; JOINED; Genomic_DNA.
DR   EMBL; BC021222; AAH21222.3; -; mRNA.
DR   EMBL; AF216962; AAF86374.1; ALT_INIT; mRNA.
DR   CCDS; CCDS44474.1; -. [Q9H8M5-1]
DR   CCDS; CCDS44475.1; -. [Q9H8M5-2]
DR   CCDS; CCDS7543.1; -. [Q9H8M5-3]
DR   RefSeq; NP_060119.3; NM_017649.4. [Q9H8M5-1]
DR   RefSeq; NP_951058.1; NM_199076.2. [Q9H8M5-2]
DR   RefSeq; NP_951059.1; NM_199077.2. [Q9H8M5-3]
DR   UniGene; Hs.643509; -.
DR   PDB; 4IY0; X-ray; 1.90 A; A=429-584.
DR   PDB; 4IY2; X-ray; 3.60 A; A/C=430-584.
DR   PDB; 4IY4; X-ray; 2.90 A; A/C=429-584.
DR   PDB; 4IYS; X-ray; 1.80 A; A=430-584.
DR   PDBsum; 4IY0; -.
DR   PDBsum; 4IY2; -.
DR   PDBsum; 4IY4; -.
DR   PDBsum; 4IYS; -.
DR   ProteinModelPortal; Q9H8M5; -.
DR   SMR; Q9H8M5; -.
DR   BioGrid; 120162; 6.
DR   IntAct; Q9H8M5; 3.
DR   STRING; 9606.ENSP00000358894; -.
DR   iPTMnet; Q9H8M5; -.
DR   PhosphoSitePlus; Q9H8M5; -.
DR   BioMuta; CNNM2; -.
DR   DMDM; 156631023; -.
DR   MaxQB; Q9H8M5; -.
DR   PaxDb; Q9H8M5; -.
DR   PeptideAtlas; Q9H8M5; -.
DR   PRIDE; Q9H8M5; -.
DR   Ensembl; ENST00000369875; ENSP00000358891; ENSG00000148842. [Q9H8M5-3]
DR   Ensembl; ENST00000369878; ENSP00000358894; ENSG00000148842. [Q9H8M5-1]
DR   Ensembl; ENST00000433628; ENSP00000392875; ENSG00000148842. [Q9H8M5-2]
DR   GeneID; 54805; -.
DR   KEGG; hsa:54805; -.
DR   UCSC; uc001kwl.4; human. [Q9H8M5-1]
DR   CTD; 54805; -.
DR   DisGeNET; 54805; -.
DR   GeneCards; CNNM2; -.
DR   H-InvDB; HIX0009171; -.
DR   HGNC; HGNC:103; CNNM2.
DR   HPA; HPA059954; -.
DR   HPA; HPA071631; -.
DR   MalaCards; CNNM2; -.
DR   MIM; 607803; gene.
DR   MIM; 613882; phenotype.
DR   MIM; 616418; phenotype.
DR   neXtProt; NX_Q9H8M5; -.
DR   OpenTargets; ENSG00000148842; -.
DR   Orphanet; 34527; Familial primary hypomagnesemia with normocalciuria and normocalcemia.
DR   PharmGKB; PA26669; -.
DR   eggNOG; KOG2118; Eukaryota.
DR   eggNOG; COG1253; LUCA.
DR   GeneTree; ENSGT00390000002383; -.
DR   HOVERGEN; HBG074775; -.
DR   InParanoid; Q9H8M5; -.
DR   KO; K16302; -.
DR   OMA; VMASRMD; -.
DR   OrthoDB; EOG091G02YS; -.
DR   PhylomeDB; Q9H8M5; -.
DR   TreeFam; TF101012; -.
DR   ChiTaRS; CNNM2; human.
DR   GenomeRNAi; 54805; -.
DR   PRO; PR:Q9H8M5; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000148842; -.
DR   CleanEx; HS_CNNM2; -.
DR   Genevisible; Q9H8M5; HS.
DR   GO; GO:0016323; C:basolateral plasma membrane; IMP:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0010960; P:magnesium ion homeostasis; IMP:MGI.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR002550; DUF21.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF01595; DUF21; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
DR   PRODOM; Q9H8M5.
DR   SWISS-2DPAGE; Q9H8M5.
KW   3D-structure; Alternative splicing; CBS domain; Cell membrane;
KW   Complete proteome; Disease mutation; Epilepsy; Glycoprotein;
KW   Ion transport; Membrane; Mental retardation; Phosphoprotein;
KW   Polymorphism; Primary hypomagnesemia; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    875       Metal transporter CNNM2.
FT                                /FTId=PRO_0000295760.
FT   TOPO_DOM      1    250       Extracellular. {ECO:0000255}.
FT   TRANSMEM    251    271       Helical. {ECO:0000255}.
FT   TOPO_DOM    272    313       Cytoplasmic. {ECO:0000255}.
FT   INTRAMEM    314    334       Helical. {ECO:0000255}.
FT   TOPO_DOM    335    338       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    339    359       Helical. {ECO:0000255}.
FT   TOPO_DOM    360    368       Extracellular. {ECO:0000255}.
FT   TRANSMEM    369    389       Helical. {ECO:0000255}.
FT   TOPO_DOM    390    875       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      258    430       DUF21.
FT   DOMAIN      450    511       CBS 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00703}.
FT   DOMAIN      518    584       CBS 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00703}.
FT   MOD_RES     761    761       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CARBOHYD    112    112       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ     541    552       GKSHLAIVQRVN -> EHTNKKPKSYQH (in isoform
FT                                3). {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_027077.
FT   VAR_SEQ     553    875       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_027078.
FT   VAR_SEQ     721    742       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_027080.
FT   VARIANT      38     38       R -> Q (in dbSNP:rs76057237).
FT                                {ECO:0000269|PubMed:21397062}.
FT                                /FTId=VAR_065259.
FT   VARIANT     122    122       E -> K (in HOMGSMR; results in reduced
FT                                protein membrane expression;
FT                                dbSNP:rs786205909).
FT                                {ECO:0000269|PubMed:24699222}.
FT                                /FTId=VAR_073848.
FT   VARIANT     269    269       S -> W (in HOMGSMR; results in reduced
FT                                protein membrane expression; decreases
FT                                cellular uptake of magnesium;
FT                                dbSNP:rs794726858).
FT                                {ECO:0000269|PubMed:24699222}.
FT                                /FTId=VAR_073849.
FT   VARIANT     330    330       L -> F (in HOMGSMR).
FT                                {ECO:0000269|PubMed:24699222}.
FT                                /FTId=VAR_073850.
FT   VARIANT     357    357       E -> K (in HOMGSMR; results in decreased
FT                                cellular uptake of magnesium;
FT                                dbSNP:rs786205910).
FT                                {ECO:0000269|PubMed:24699222}.
FT                                /FTId=VAR_073851.
FT   VARIANT     568    568       T -> I (in HOMG6; reduced activity;
FT                                electrophysiological analysis shows that
FT                                magnesium-sensitive sodium currents are
FT                                significantly diminished and are blocked
FT                                by increased extracellular magnesium
FT                                concentrations; dbSNP:rs387906975).
FT                                {ECO:0000269|PubMed:21397062}.
FT                                /FTId=VAR_065260.
FT   CONFLICT    299    299       K -> N (in Ref. 1; BAB14585).
FT                                {ECO:0000305}.
FT   CONFLICT    354    354       I -> V (in Ref. 1; BAB14386).
FT                                {ECO:0000305}.
FT   CONFLICT    475    475       E -> V (in Ref. 1; BAB14386).
FT                                {ECO:0000305}.
FT   HELIX       430    443       {ECO:0000244|PDB:4IYS}.
FT   HELIX       446    449       {ECO:0000244|PDB:4IYS}.
FT   STRAND      450    452       {ECO:0000244|PDB:4IYS}.
FT   HELIX       453    455       {ECO:0000244|PDB:4IYS}.
FT   HELIX       467    476       {ECO:0000244|PDB:4IYS}.
FT   STRAND      479    487       {ECO:0000244|PDB:4IYS}.
FT   STRAND      491    496       {ECO:0000244|PDB:4IYS}.
FT   HELIX       497    500       {ECO:0000244|PDB:4IYS}.
FT   HELIX       505    507       {ECO:0000244|PDB:4IYS}.
FT   HELIX       511    518       {ECO:0000244|PDB:4IYS}.
FT   STRAND      524    526       {ECO:0000244|PDB:4IYS}.
FT   HELIX       531    539       {ECO:0000244|PDB:4IYS}.
FT   STRAND      540    542       {ECO:0000244|PDB:4IY0}.
FT   STRAND      544    552       {ECO:0000244|PDB:4IYS}.
FT   STRAND      554    558       {ECO:0000244|PDB:4IY0}.
FT   STRAND      560    568       {ECO:0000244|PDB:4IYS}.
FT   HELIX       569    579       {ECO:0000244|PDB:4IYS}.
FT   TURN        580    582       {ECO:0000244|PDB:4IYS}.
SQ   SEQUENCE   875 AA;  96623 MW;  6D19F35D1B7D9A30 CRC64;
     MIGCGACEPK VKMAGGQAAA ALPTWKMAAR RSLSARGRGI LQAAAGRLLP LLLLSCCCGA
     GGCAAVGENE ETVIIGLRLE DTNDVSFMEG GALRVSERTR VKLRVYGQNI NNETWSRIAF
     TEHERRRHSP GERGLGGPAP PEPDSGPQRC GIRTSDIIIL PHIILNRRTS GIIEIEIKPL
     RKMEKSKSYY LCTSLSTPAL GAGGSGSTGG AVGGKGGSGV AGLPPPPWAE TTWIYHDGED
     TKMIVGEEKK FLLPFWLQVI FISLLLCLSG MFSGLNLGLM ALDPMELRIV QNCGTEKEKN
     YAKRIEPVRR QGNYLLCSLL LGNVLVNTTL TILLDDIAGS GLVAVVVSTI GIVIFGEIVP
     QAICSRHGLA VGANTIFLTK FFMMMTFPAS YPVSKLLDCV LGQEIGTVYN REKLLEMLRV
     TDPYNDLVKE ELNIIQGALE LRTKTVEDVM TPLRDCFMIT GEAILDFNTM SEIMESGYTR
     IPVFEGERSN IVDLLFVKDL AFVDPDDCTP LKTITKFYNH PLHFVFNDTK LDAMLEEFKK
     GKSHLAIVQR VNNEGEGDPF YEVLGIVTLE DVIEEIIKSE ILDETDLYTD NRTKKKVAHR
     ERKQDFSAFK QTDSEMKVKI SPQLLLAMHR FLATEVEAFS PSQMSEKILL RLLKHPNVIQ
     ELKYDEKNKK APEYYLYQRN KPVDYFVLIL QGKVEVEAGK EGMKFEASAF SYYGVMALTA
     SPVPLSLSRT FVVSRTELLA AGSPGENKSP PRPCGLNHSD SLSRSDRIDA VTPTLGSSNN
     QLNSSLLQVY IPDYSVRALS DLQFVKISRQ QYQNALMASR MDKTPQSSDS ENTKIELTLT
     ELHDGLPDET ANLLNEQNCV THSKANHSLH NEGAI
//

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