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Heat-stable enterotoxin receptor (STA receptor) (hSTAR) (EC 4.6.1.2) (Guanylyl cyclase C) (GC-C) (Intestinal guanylate cyclase)

 GUC2C_HUMAN             Reviewed;        1073 AA.
P25092; B2RMY6;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 2.
28-FEB-2018, entry version 181.
RecName: Full=Heat-stable enterotoxin receptor;
Short=STA receptor;
Short=hSTAR;
EC=4.6.1.2;
AltName: Full=Guanylyl cyclase C;
Short=GC-C;
AltName: Full=Intestinal guanylate cyclase;
Flags: Precursor;
Name=GUCY2C; Synonyms=GUC2C, STAR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-281.
PubMed=1718270; DOI=10.1016/0006-291X(91)91736-V;
Singh S., Singh G., Heim J.-M., Gerzer R.;
"Isolation and expression of a guanylate cyclase-coupled heat stable
enterotoxin receptor cDNA from a human colonic cell line.";
Biochem. Biophys. Res. Commun. 179:1455-1463(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-281.
PubMed=1680854;
de Sauvage F.J., Camerato T.R., Goeddel D.V.;
"Primary structure and functional expression of the human receptor for
Escherichia coli heat-stable enterotoxin.";
J. Biol. Chem. 266:17912-17918(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-281.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-281.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
TISSUE=Placenta;
PubMed=8605253; DOI=10.1016/0167-4781(95)00190-5;
Mann E.A., Jump M.L., Giannella R.A.;
"Cell line-specific transcriptional activation of the promoter of the
human guanylyl cyclase C/heat-stable enterotoxin receptor gene.";
Biochim. Biophys. Acta 1305:7-10(1996).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-1073, AND VARIANT LEU-281.
TISSUE=Colon carcinoma;
PubMed=8381596;
Mann E.A., Cohen M.B., Giannella R.A.;
"Comparison of receptors for Escherichia coli heat-stable enterotoxin:
novel receptor present in IEC-6 cells.";
Am. J. Physiol. 264:G172-G178(1993).
[8]
SUBUNIT.
PubMed=11123935; DOI=10.1021/bi0013849;
Vijayachandra K., Guruprasad M., Bhandari R., Manjunath U.H.,
Somesh B.P., Srinivasan N., Suguna K., Visweswariah S.S.;
"Biochemical characterization of the intracellular domain of the human
guanylyl cyclase C receptor provides evidence for a catalytically
active homotrimer.";
Biochemistry 39:16075-16083(2000).
[9]
INTERACTION WITH PDZK2.
PubMed=11950846; DOI=10.1074/jbc.M202434200;
Scott R.O., Thelin W.R., Milgram S.L.;
"A novel PDZ protein regulates the activity of guanylyl cyclase C, the
heat-stable enterotoxin receptor.";
J. Biol. Chem. 277:22934-22941(2002).
[10]
GLYCOSYLATION AT ASN-32; ASN-75; ASN-79; ASN-195; ASN-284; ASN-307;
ASN-345 AND ASN-402, LACK OF GLYCOSYLATION AT ASN-357, INTERACTION
WITH VIP36, AND SUBCELLULAR LOCATION.
PubMed=23269669; DOI=10.1074/jbc.M112.413906;
Arshad N., Ballal S., Visweswariah S.S.;
"Site-specific N-linked glycosylation of receptor guanylyl cyclase C
regulates ligand binding, ligand-mediated activation and interaction
with vesicular integral membrane protein 36, VIP36.";
J. Biol. Chem. 288:3907-3917(2013).
[11]
VARIANT MECIL GLY-387, AND CHARACTERIZATION OF VARIANT MECIL GLY-387.
PubMed=22521417; DOI=10.1016/j.ajhg.2012.03.022;
Romi H., Cohen I., Landau D., Alkrinawi S., Yerushalmi B.,
Hershkovitz R., Newman-Heiman N., Cutting G.R., Ofir R., Sivan S.,
Birk O.S.;
"Meconium ileus caused by mutations in GUCY2C, encoding the CFTR-
activating guanylate cyclase 2C.";
Am. J. Hum. Genet. 90:893-899(2012).
[12]
VARIANT DIAR6 ILE-840, AND CHARACTERIZATION OF VARIANT DIAR6 ILE-840.
PubMed=22436048; DOI=10.1056/NEJMoa1110132;
Fiskerstrand T., Arshad N., Haukanes B.I., Tronstad R.R., Pham K.D.,
Johansson S., Havik B., Tonder S.L., Levy S.E., Brackman D., Boman H.,
Biswas K.H., Apold J., Hovdenak N., Visweswariah S.S., Knappskog P.M.;
"Familial diarrhea syndrome caused by an activating GUCY2C mutation.";
N. Engl. J. Med. 366:1586-1595(2012).
[13]
VARIANTS [LARGE SCALE ANALYSIS] ARG-30; ARG-61; GLN-114; LEU-464;
LYS-610; VAL-859; ARG-1045 AND CYS-1072.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Receptor for the E.coli heat-stable enterotoxin (E.coli
enterotoxin markedly stimulates the accumulation of cGMP in
mammalian cells expressing GC-C). Also activated by the endogenous
peptides guanylin and uroguanylin.
-!- CATALYTIC ACTIVITY: GTP = 3',5'-cyclic GMP + diphosphate.
-!- SUBUNIT: Homotrimer. Interacts via its C-terminal region with
PDZK2. Interacts with the lectin chaperone VIP36.
{ECO:0000269|PubMed:11123935, ECO:0000269|PubMed:11950846,
ECO:0000269|PubMed:23269669}.
-!- INTERACTION:
Q86UT5-2:PDZD3; NbExp=4; IntAct=EBI-2816795, EBI-8299496;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23269669};
Single-pass type I membrane protein {ECO:0000269|PubMed:23269669}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:23269669};
Single-pass type I membrane protein {ECO:0000269|PubMed:23269669}.
Note=The 145 kDa plasma membrane form of GC-C contains sialic acid
and galactose residues, while a differencially glycosylated 130
Kda form is a high mannose form that is resident in the
endoplasmic reticulum and may serve as the precursor for the cell
surface form.
-!- DOMAIN: The protein kinase domain is predicted to be catalytically
inactive.
-!- PTM: Glycosylation at Asn-75 and/or Asn-79 is required for
interaction with VIP36 while glycosylation at Asn-345 and Asn-402
modulates ligand-mediated GC-C activation.
{ECO:0000269|PubMed:23269669}.
-!- DISEASE: Diarrhea 6 (DIAR6) [MIM:614616]: A relatively mild,
early-onset chronic diarrhea that may be associated with increased
susceptibility to inflammatory bowel disease, small bowel
obstruction, and esophagitis. {ECO:0000269|PubMed:22436048}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Meconium ileus (MECIL) [MIM:614665]: A condition
characterized by a intestinal obstruction due to inspissated
meconium in the distal ileum and cecum, which develops in utero
and presents shortly after birth as a failure to pass meconium.
Meconium ileus is a known clinical manifestation of cystic
fibrosis. {ECO:0000269|PubMed:22521417}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GUCY2CID43303ch12p13.html";
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EMBL; S57551; AAB19934.2; -; mRNA.
EMBL; M73489; AAA36655.1; -; mRNA.
EMBL; AC007545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471094; EAW96324.1; -; Genomic_DNA.
EMBL; BC136544; AAI36545.1; -; mRNA.
EMBL; BC136545; AAI36546.1; -; mRNA.
EMBL; U20230; AAC50381.1; -; Genomic_DNA.
CCDS; CCDS8664.1; -.
PIR; A40940; OYHUHX.
RefSeq; NP_004954.2; NM_004963.3.
UniGene; Hs.524278; -.
ProteinModelPortal; P25092; -.
BioGrid; 109239; 2.
IntAct; P25092; 3.
MINT; P25092; -.
STRING; 9606.ENSP00000261170; -.
ChEMBL; CHEMBL1795197; -.
DrugBank; DB08890; Linaclotide.
GuidetoPHARMACOLOGY; 1750; -.
TCDB; 8.A.85.1.1; the guanylate cyclase (gc) family.
iPTMnet; P25092; -.
PhosphoSitePlus; P25092; -.
BioMuta; GUCY2C; -.
DMDM; 311033390; -.
MaxQB; P25092; -.
PaxDb; P25092; -.
PeptideAtlas; P25092; -.
PRIDE; P25092; -.
DNASU; 2984; -.
Ensembl; ENST00000261170; ENSP00000261170; ENSG00000070019.
GeneID; 2984; -.
KEGG; hsa:2984; -.
UCSC; uc001rcd.4; human.
CTD; 2984; -.
DisGeNET; 2984; -.
EuPathDB; HostDB:ENSG00000070019.4; -.
GeneCards; GUCY2C; -.
H-InvDB; HIX0036867; -.
HGNC; HGNC:4688; GUCY2C.
HPA; HPA037655; -.
HPA; HPA073759; -.
MalaCards; GUCY2C; -.
MIM; 601330; gene.
MIM; 614616; phenotype.
MIM; 614665; phenotype.
neXtProt; NX_P25092; -.
OpenTargets; ENSG00000070019; -.
Orphanet; 314373; Chronic diarrhea due to guanylate cyclase 2C overactivity.
Orphanet; 314376; Intestinal obstruction in the newborn due to guanylate cyclase 2C deficiency.
PharmGKB; PA29069; -.
eggNOG; KOG1023; Eukaryota.
eggNOG; COG2114; LUCA.
GeneTree; ENSGT00760000118959; -.
HOGENOM; HOG000112833; -.
HOVERGEN; HBG106967; -.
InParanoid; P25092; -.
KO; K12320; -.
OMA; KYSTPME; -.
OrthoDB; EOG091G01F8; -.
PhylomeDB; P25092; -.
BRENDA; 4.6.1.2; 2681.
Reactome; R-HSA-8935690; Digestion.
Reactome; R-HSA-8942233; Intestinal infectious diseases.
SIGNOR; P25092; -.
ChiTaRS; GUCY2C; human.
GeneWiki; Guanylate_cyclase_2C; -.
GenomeRNAi; 2984; -.
PRO; PR:P25092; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000070019; -.
CleanEx; HS_GUCY2C; -.
CleanEx; HS_STAR; -.
Genevisible; P25092; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
GO; GO:0015643; F:toxic substance binding; IEA:Ensembl.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0007586; P:digestion; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; TAS:ProtInc.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
Gene3D; 3.30.70.1230; -; 1.
InterPro; IPR001054; A/G_cyclase.
InterPro; IPR018297; A/G_cyclase_CS.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR029787; Nucleotide_cyclase.
InterPro; IPR028082; Peripla_BP_I.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
Pfam; PF00211; Guanylate_cyc; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00044; CYCc; 1.
SUPFAM; SSF53822; SSF53822; 1.
SUPFAM; SSF55073; SSF55073; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
Cell membrane; cGMP biosynthesis; Complete proteome; Disease mutation;
Endoplasmic reticulum; Glycoprotein; GTP-binding; Lyase; Membrane;
Nucleotide-binding; Polymorphism; Receptor; Reference proteome;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 1073 Heat-stable enterotoxin receptor.
/FTId=PRO_0000012376.
TOPO_DOM 24 430 Extracellular. {ECO:0000255}.
TRANSMEM 431 454 Helical. {ECO:0000255}.
TOPO_DOM 455 1073 Cytoplasmic. {ECO:0000255}.
DOMAIN 489 749 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 824 954 Guanylate cyclase. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
SITE 357 357 Not glycosylated.
{ECO:0000269|PubMed:23269669}.
CARBOHYD 32 32 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23269669}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23269669}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23269669}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23269669}.
CARBOHYD 284 284 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23269669}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23269669}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23269669}.
CARBOHYD 402 402 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23269669}.
VARIANT 30 30 C -> R (in dbSNP:rs56142849).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042221.
VARIANT 61 61 G -> R (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042222.
VARIANT 114 114 R -> Q (in dbSNP:rs56275235).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042223.
VARIANT 281 281 F -> L (in dbSNP:rs1420635).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1680854,
ECO:0000269|PubMed:1718270,
ECO:0000269|PubMed:8381596,
ECO:0000269|Ref.4}.
/FTId=VAR_049253.
VARIANT 387 387 D -> G (in MECIL; activation of guanylate
cyclase activity is 60% lower than in
wild-type; dbSNP:rs587776905).
{ECO:0000269|PubMed:22521417}.
/FTId=VAR_068174.
VARIANT 464 464 R -> L (in dbSNP:rs55684775).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042224.
VARIANT 610 610 E -> K (in dbSNP:rs55897626).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042225.
VARIANT 840 840 S -> I (in DIAR6; activating mutation;
exposure of the mutant receptor to its
ligands results in markedly increased
production of cyclic guanosine
monophosphate; dbSNP:rs587776871).
{ECO:0000269|PubMed:22436048}.
/FTId=VAR_067724.
VARIANT 859 859 I -> V (in dbSNP:rs34890806).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042226.
VARIANT 1045 1045 Q -> R (in dbSNP:rs35617837).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042227.
VARIANT 1072 1072 Y -> C (in dbSNP:rs35179392).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042228.
CONFLICT 322 322 A -> R (in Ref. 1; AAB19934).
{ECO:0000305}.
CONFLICT 331 331 L -> V (in Ref. 1; AAB19934).
{ECO:0000305}.
CONFLICT 509 509 D -> V (in Ref. 1; AAB19934).
{ECO:0000305}.
CONFLICT 543 543 N -> T (in Ref. 1; AAB19934).
{ECO:0000305}.
SEQUENCE 1073 AA; 123403 MW; 486A4DE6F9097E22 CRC64;
MKTLLLDLAL WSLLFQPGWL SFSSQVSQNC HNGSYEISVL MMGNSAFAEP LKNLEDAVNE
GLEIVRGRLQ NAGLNVTVNA TFMYSDGLIH NSGDCRSSTC EGLDLLRKIS NAQRMGCVLI
GPSCTYSTFQ MYLDTELSYP MISAGSFGLS CDYKETLTRL MSPARKLMYF LVNFWKTNDL
PFKTYSWSTS YVYKNGTETE DCFWYLNALE ASVSYFSHEL GFKVVLRQDK EFQDILMDHN
RKSNVIIMCG GPEFLYKLKG DRAVAEDIVI ILVDLFNDQY FEDNVTAPDY MKNVLVLTLS
PGNSLLNSSF SRNLSPTKRD FALAYLNGIL LFGHMLKIFL ENGENITTPK FAHAFRNLTF
EGYDGPVTLD DWGDVDSTMV LLYTSVDTKK YKVLLTYDTH VNKTYPVDMS PTFTWKNSKL
PNDITGRGPQ ILMIAVFTLT GAVVLLLLVA LLMLRKYRKD YELRQKKWSH IPPENIFPLE
TNETNHVSLK IDDDKRRDTI QRLRQCKYDK KRVILKDLKH NDGNFTEKQK IELNKLLQID
YYNLTKFYGT VKLDTMIFGV IEYCERGSLR EVLNDTISYP DGTFMDWEFK ISVLYDIAKG
MSYLHSSKTE VHGRLKSTNC VVDSRMVVKI TDFGCNSILP PKKDLWTAPE HLRQANISQK
GDVYSYGIIA QEIILRKETF YTLSCRDRNE KIFRVENSNG MKPFRPDLFL ETAEEKELEV
YLLVKNCWEE DPEKRPDFKK IETTLAKIFG LFHDQKNESY MDTLIRRLQL YSRNLEHLVE
ERTQLYKAER DRADRLNFML LPRLVVKSLK EKGFVEPELY EEVTIYFSDI VGFTTICKYS
TPMEVVDMLN DIYKSFDHIV DHHDVYKVET IGDAYMVASG LPKRNGNRHA IDIAKMALEI
LSFMGTFELE HLPGLPIWIR IGVHSGPCAA GVVGIKMPRY CLFGDTVNTA SRMESTGLPL
RIHVSGSTIA ILKRTECQFL YEVRGETYLK GRGNETTYWL TGMKDQKFNL PTPPTVENQQ
RLQAEFSDMI ANSLQKRQAA GIRSQKPRRV ASYKKGTLEY LQLNTTDKES TYF


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