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Canalicular multispecific organic anion transporter 2 (ATP-binding cassette sub-family C member 3) (Multi-specific organic anion transporter D) (MOAT-D) (Multidrug resistance-associated protein 3)

 MRP3_HUMAN              Reviewed;        1527 AA.
O15438; B2RPA9; D3DTX9; O60265; O60922; O75621; O95078; O95289;
O95290; Q86X85; Q9UN52;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 3.
25-OCT-2017, entry version 168.
RecName: Full=Canalicular multispecific organic anion transporter 2;
AltName: Full=ATP-binding cassette sub-family C member 3;
AltName: Full=Multi-specific organic anion transporter D;
Short=MOAT-D;
AltName: Full=Multidrug resistance-associated protein 3;
Name=ABCC3; Synonyms=CMOAT2, MLP2, MRP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=9813153; DOI=10.1006/bbrc.1998.9546;
Uchiumi T., Hinoshita E., Haga S., Nakamura T., Tanaka T., Toh S.,
Furukawa M., Kawabe T., Wada M., Kagotani K., Okumura K., Kohno K.,
Akiyama S., Kuwano M.;
"Isolation of a novel human canalicular multispecific organic anion
transporter, cMOAT2/MRP3, and its expression in cisplatin-resistant
cancer cells with decreased ATP-dependent drug transport.";
Biochem. Biophys. Res. Commun. 252:103-110(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9738950; DOI=10.1016/S0014-5793(98)00899-0;
Kiuchi Y., Suzuki H., Hirohashi T., Tyson C.A., Sugiyama Y.;
"cDNA cloning and inducible expression of human multidrug resistance
associated protein 3 (MRP3).";
FEBS Lett. 433:149-152(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9827529; DOI=10.1093/jnci/90.22.1735;
Belinsky M.G., Bain L.J., Balsara B.B., Testa J.R., Kruh G.D.;
"Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT
subfamily of transporter proteins.";
J. Natl. Cancer Inst. 90:1735-1741(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Liver;
PubMed=9889399; DOI=10.1016/S0005-2736(98)00233-8;
Fromm M.F., Leake B., Roden D.M., Wilkinson G.R., Kim R.B.;
"Human MRP3 transporter: identification of the 5'-flanking region,
genomic organization and alternative splice variants.";
Biochim. Biophys. Acta 1415:369-374(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=10094960; DOI=10.1002/hep.510290404;
Koenig J., Rost D., Cui Y., Keppler D.;
"Characterization of the human multidrug resistance protein isoform
MRP3 localized to the basolateral hepatocyte membrane.";
Hepatology 29:1156-1163(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Kool M., de Haas M., Ponne N.J., Baas F., Borst P.;
"Complete coding sequence of human MRP3, a homolog of the human
multidrug resistance-associated protein MRP1.";
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Colon carcinoma;
Auclair D., Alonso E., Chen L.B.;
"Identification of a novel splice variant of MRP3 involved in
resistance to DNA damaging agents.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
TISSUE=Blood;
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 1043-1527 (ISOFORM 1).
TISSUE=Liver;
PubMed=9270026;
Kool M., de Haas M., Scheffer G.L., Scheper R.J., van Eijk M.J.,
Juijn J.A., Baas F., Borst P.;
"Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5,
homologues of the multidrug resistance-associated protein gene (MRP1),
in human cancer cell lines.";
Cancer Res. 57:3537-3547(1997).
[12]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908 AND SER-911, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: May act as an inducible transporter in the biliary and
intestinal excretion of organic anions. Acts as an alternative
route for the export of bile acids and glucuronides from
cholestatic hepatocytes (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=MRP3;
IsoId=O15438-1; Sequence=Displayed;
Name=2; Synonyms=MRP3A;
IsoId=O15438-2; Sequence=VSP_000042;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3; Synonyms=MRP3B;
IsoId=O15438-3; Sequence=VSP_000040, VSP_000041;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=4; Synonyms=MRP3S1;
IsoId=O15438-4; Sequence=VSP_043864;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay. No
experimental confirmation available.;
Name=5;
IsoId=O15438-5; Sequence=VSP_039041, VSP_039042;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Mainly expressed in the liver. Also expressed
in small intestine, colon, prostate, testis, brain and at a lower
level in the kidney.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. Conjugate transporter (TC 3.A.1.208) subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB71756.1; Type=Frameshift; Positions=1334, 1338; Evidence={ECO:0000305};
Sequence=AAD01430.1; Type=Frameshift; Positions=355, 359, 361; Evidence={ECO:0000305};
Sequence=AAD38185.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=O15438";
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EMBL; AF083552; AAC34668.1; -; mRNA.
EMBL; AB010887; BAA28146.1; -; mRNA.
EMBL; AF104943; AAD04170.1; -; mRNA.
EMBL; AF085690; AAD02845.1; -; mRNA.
EMBL; AF085691; AAD02846.1; -; mRNA.
EMBL; AF085692; AAD02847.1; -; mRNA.
EMBL; Y17151; CAA76658.2; -; mRNA.
EMBL; AF009670; AAD01430.1; ALT_FRAME; mRNA.
EMBL; AF154001; AAD38185.1; ALT_SEQ; mRNA.
EMBL; AC004590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94592.1; -; Genomic_DNA.
EMBL; CH471109; EAW94590.1; -; Genomic_DNA.
EMBL; CH471109; EAW94593.1; -; Genomic_DNA.
EMBL; BC046126; AAH46126.1; -; mRNA.
EMBL; BC137347; AAI37348.1; -; mRNA.
EMBL; BC137348; AAI37349.1; -; mRNA.
EMBL; U83659; AAB71756.1; ALT_FRAME; mRNA.
CCDS; CCDS32681.1; -. [O15438-1]
CCDS; CCDS45739.1; -. [O15438-5]
PIR; JE0336; JE0336.
RefSeq; NP_001137542.1; NM_001144070.1. [O15438-5]
RefSeq; NP_003777.2; NM_003786.3. [O15438-1]
UniGene; Hs.463421; -.
ProteinModelPortal; O15438; -.
SMR; O15438; -.
BioGrid; 114255; 9.
IntAct; O15438; 5.
STRING; 9606.ENSP00000285238; -.
BindingDB; O15438; -.
ChEMBL; CHEMBL5918; -.
DrugBank; DB02659; Cholic Acid.
DrugBank; DB00515; Cisplatin.
DrugBank; DB00257; Clotrimazole.
DrugBank; DB00286; Conjugated Equine Estrogens.
DrugBank; DB00091; Cyclosporine.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB00773; Etoposide.
DrugBank; DB00973; Ezetimibe.
DrugBank; DB00544; Fluorouracil.
DrugBank; DB00158; Folic Acid.
DrugBank; DB08884; Gadoxetic acid.
DrugBank; DB00143; Glutathione.
DrugBank; DB01016; Glyburide.
DrugBank; DB00328; Indomethacin.
DrugBank; DB00709; Lamivudine.
DrugBank; DB00563; Methotrexate.
DrugBank; DB01011; Metyrapone.
DrugBank; DB01115; Nifedipine.
DrugBank; DB00338; Omeprazole.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB01032; Probenecid.
DrugBank; DB01045; Rifampicin.
DrugBank; DB01138; Sulfinpyrazone.
DrugBank; DB04348; Taurocholic Acid.
DrugBank; DB00661; Verapamil.
DrugBank; DB00541; Vincristine.
TCDB; 3.A.1.208.9; the atp-binding cassette (abc) superfamily.
iPTMnet; O15438; -.
PhosphoSitePlus; O15438; -.
BioMuta; ABCC3; -.
MaxQB; O15438; -.
PaxDb; O15438; -.
PeptideAtlas; O15438; -.
PRIDE; O15438; -.
Ensembl; ENST00000285238; ENSP00000285238; ENSG00000108846. [O15438-1]
Ensembl; ENST00000427699; ENSP00000395160; ENSG00000108846. [O15438-5]
Ensembl; ENST00000502426; ENSP00000427073; ENSG00000108846. [O15438-3]
Ensembl; ENST00000505699; ENSP00000427521; ENSG00000108846. [O15438-2]
GeneID; 8714; -.
KEGG; hsa:8714; -.
UCSC; uc002isk.5; human. [O15438-1]
CTD; 8714; -.
DisGeNET; 8714; -.
EuPathDB; HostDB:ENSG00000108846.15; -.
GeneCards; ABCC3; -.
HGNC; HGNC:54; ABCC3.
HPA; CAB037136; -.
HPA; HPA048483; -.
MIM; 604323; gene.
neXtProt; NX_O15438; -.
OpenTargets; ENSG00000108846; -.
PharmGKB; PA376; -.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00880000137856; -.
HOVERGEN; HBG108314; -.
InParanoid; O15438; -.
KO; K05667; -.
OMA; AFQVEQM; -.
OrthoDB; EOG091G00IN; -.
PhylomeDB; O15438; -.
TreeFam; TF105199; -.
Reactome; R-HSA-159418; Recycling of bile acids and salts.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
ChiTaRS; ABCC3; human.
GeneWiki; ABCC3; -.
GenomeRNAi; 8714; -.
PRO; PR:O15438; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108846; -.
CleanEx; HS_ABCC3; -.
ExpressionAtlas; O15438; baseline and differential.
Genevisible; O15438; HS.
GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; TAS:ProtInc.
GO; GO:0043225; F:ATPase-coupled anion transmembrane transporter activity; TAS:Reactome.
GO; GO:0015432; F:bile acid-exporting ATPase activity; TAS:Reactome.
GO; GO:0008514; F:organic anion transmembrane transporter activity; TAS:ProtInc.
GO; GO:0008559; F:xenobiotic-transporting ATPase activity; IBA:GO_Central.
GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
GO; GO:0015722; P:canalicular bile acid transport; ISS:UniProtKB.
GO; GO:0006855; P:drug transmembrane transport; IBA:GO_Central.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0006810; P:transport; TAS:ProtInc.
GO; GO:0042908; P:xenobiotic transport; IBA:GO_Central.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR005292; Multidrug-R_assoc.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
TIGRFAMs; TIGR00957; MRP_assoc_pro; 1.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Glycoprotein;
Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 1527 Canalicular multispecific organic anion
transporter 2.
/FTId=PRO_0000093360.
TOPO_DOM 1 32 Extracellular. {ECO:0000250}.
TRANSMEM 33 53 Helical; Name=1. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 54 73 Cytoplasmic. {ECO:0000250}.
TRANSMEM 74 94 Helical; Name=2. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 95 99 Extracellular. {ECO:0000250}.
TRANSMEM 100 120 Helical; Name=3. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 121 132 Cytoplasmic. {ECO:0000250}.
TRANSMEM 133 153 Helical; Name=4. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 154 171 Extracellular. {ECO:0000250}.
TRANSMEM 172 192 Helical; Name=5. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 193 302 Cytoplasmic. {ECO:0000250}.
TRANSMEM 303 323 Helical; Name=6. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 324 349 Extracellular. {ECO:0000250}.
TRANSMEM 350 370 Helical; Name=7. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 371 426 Cytoplasmic. {ECO:0000250}.
TRANSMEM 427 447 Helical; Name=8. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 448 450 Extracellular. {ECO:0000250}.
TRANSMEM 451 471 Helical; Name=9. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 472 533 Cytoplasmic. {ECO:0000250}.
TRANSMEM 534 554 Helical; Name=10. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 555 576 Extracellular. {ECO:0000250}.
TRANSMEM 577 597 Helical; Name=11. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 598 963 Cytoplasmic. {ECO:0000250}.
TRANSMEM 964 984 Helical; Name=12. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 985 1021 Extracellular. {ECO:0000250}.
TRANSMEM 1022 1042 Helical; Name=13. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1043 1085 Cytoplasmic. {ECO:0000250}.
TRANSMEM 1086 1106 Helical; Name=14. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1107 1107 Extracellular. {ECO:0000250}.
TRANSMEM 1108 1128 Helical; Name=15. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1129 1199 Cytoplasmic. {ECO:0000250}.
TRANSMEM 1200 1220 Helical; Name=16. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1221 1222 Extracellular. {ECO:0000250}.
TRANSMEM 1223 1243 Helical; Name=17. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1244 1527 Cytoplasmic. {ECO:0000250}.
DOMAIN 311 594 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 629 851 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 971 1252 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1291 1523 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 661 668 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1323 1330 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
MOD_RES 908 908 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 911 911 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 18 18 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1006 1006 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1007 1007 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 1 M -> MPACTVKESPNCKRNFCKADHIVNTSGGSNLERVGK
QKTIQKGQFSQRSVCT (in isoform 4).
{ECO:0000303|Ref.7}.
/FTId=VSP_043864.
VAR_SEQ 226 510 MAIYGYRHPLEEKDLWSLKEEDRSQMVVQQLLEAWRKQEKQ
TARHKASAAPGKNASGEDEVLLGARPRPRKPSFLKALLATF
GSSFLISACFKLIQDLLSFINPQLLSILIRFISNPMAPSWW
GFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVI
YRKALVITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLL
WSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAV
KMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSF
-> LLNPDPLRGCLPGFTSPQDGHLWLPASPGGEGPLVPKG
RGQIPDGGAAAAGGMEEAGKADGTTQGFSSTWEKCLRRGRG
AAGCPAQAPEALLPEGPAGHLRLQLPHQCLLQAYPGPALLH
QSTAAQHPDQVYLQPHGPLLVGLPGGWADVPVLHDAVADLT
TLLPLHLCDWGEVSYWDHGCHLQEGSGYHQLSQTCVHCGGN
CQPHVSGCPALHGPCPLPQSAVVSTPADHPGDLLPLAEPRS
LCPGWSRFHGLADSTQRSCGREDARLPGKANEIEGLAHQAD
E (in isoform 3).
{ECO:0000303|PubMed:9889399}.
/FTId=VSP_000040.
VAR_SEQ 511 1527 Missing (in isoform 3).
{ECO:0000303|PubMed:9889399}.
/FTId=VSP_000041.
VAR_SEQ 547 572 TLITLWVYVYVDPNNVLDAEKAFVSV -> RLGTGLGPCLQ
GSGCPGMARAHWTLP (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_039041.
VAR_SEQ 573 1527 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_039042.
VAR_SEQ 1194 1527 WLSIGVEFVGNCVVLFAALFAVIGRSSLNPGLVGLSVSYSL
QVTFALNWMIRMMSDLESNIVAVERVKEYSKTETEAPWVVE
GSRPPEGWPPRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGG
EKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADI
GLHDLRSQLTIIPQDPILFSGTLRMNLDPFGSYSEEDIWWA
LELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARA
LLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTI
AHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGMA
RDAGLA -> SEAASLAPCSSRNSQQALWCSGSLSLLSPKQ
KTGPALPLPHFLLI (in isoform 2).
{ECO:0000303|PubMed:9889399}.
/FTId=VSP_000042.
VARIANT 11 11 G -> D (in dbSNP:rs11568609).
/FTId=VAR_029119.
VARIANT 346 346 S -> F (in dbSNP:rs11568605).
/FTId=VAR_020235.
VARIANT 1286 1286 R -> G (in dbSNP:rs11568593).
/FTId=VAR_029120.
VARIANT 1297 1297 R -> H (in dbSNP:rs11568591).
/FTId=VAR_020237.
VARIANT 1365 1365 Q -> R (in dbSNP:rs11568590).
/FTId=VAR_020239.
VARIANT 1381 1381 R -> S (in dbSNP:rs45461799).
/FTId=VAR_020240.
CONFLICT 13 13 K -> N (in Ref. 10; AAH46126).
{ECO:0000305}.
CONFLICT 42 42 C -> R (in Ref. 5; CAA76658).
{ECO:0000305}.
CONFLICT 184 184 A -> T (in Ref. 4; AAD02846).
{ECO:0000305}.
CONFLICT 344 344 A -> G (in Ref. 1; AAC34668).
{ECO:0000305}.
CONFLICT 569 569 F -> Y (in Ref. 2; BAA28146).
{ECO:0000305}.
CONFLICT 1128 1128 F -> C (in Ref. 11; AAB71756).
{ECO:0000305}.
CONFLICT 1212 1212 L -> I (in Ref. 11; AAB71756).
{ECO:0000305}.
CONFLICT 1249 1249 D -> E (in Ref. 11; AAB71756).
{ECO:0000305}.
CONFLICT 1359 1359 L -> F (in Ref. 11; AAB71756).
{ECO:0000305}.
CONFLICT 1362 1362 L -> V (in Ref. 1; AAC34668 and 11;
AAB71756). {ECO:0000305}.
CONFLICT 1364 1364 S -> C (in Ref. 11; AAB71756).
{ECO:0000305}.
CONFLICT 1366 1366 L -> M (in Ref. 11; AAB71756).
{ECO:0000305}.
CONFLICT 1371 1371 Q -> R (in Ref. 11; AAB71756).
{ECO:0000305}.
SEQUENCE 1527 AA; 169343 MW; 0D1F879B6F18370C CRC64;
MDALCGSGEL GSKFWDSNLS VHTENPDLTP CFQNSLLAWV PCIYLWVALP CYLLYLRHHC
RGYIILSHLS KLKMVLGVLL WCVSWADLFY SFHGLVHGRA PAPVFFVTPL VVGVTMLLAT
LLIQYERLQG VQSSGVLIIF WFLCVVCAIV PFRSKILLAK AEGEISDPFR FTTFYIHFAL
VLSALILACF REKPPFFSAK NVDPNPYPET SAGFLSRLFF WWFTKMAIYG YRHPLEEKDL
WSLKEEDRSQ MVVQQLLEAW RKQEKQTARH KASAAPGKNA SGEDEVLLGA RPRPRKPSFL
KALLATFGSS FLISACFKLI QDLLSFINPQ LLSILIRFIS NPMAPSWWGF LVAGLMFLCS
MMQSLILQHY YHYIFVTGVK FRTGIMGVIY RKALVITNSV KRASTVGEIV NLMSVDAQRF
MDLAPFLNLL WSAPLQIILA IYFLWQNLGP SVLAGVAFMV LLIPLNGAVA VKMRAFQVKQ
MKLKDSRIKL MSEILNGIKV LKLYAWEPSF LKQVEGIRQG ELQLLRTAAY LHTTTTFTWM
CSPFLVTLIT LWVYVYVDPN NVLDAEKAFV SVSLFNILRL PLNMLPQLIS NLTQASVSLK
RIQQFLSQEE LDPQSVERKT ISPGYAITIH SGTFTWAQDL PPTLHSLDIQ VPKGALVAVV
GPVGCGKSSL VSALLGEMEK LEGKVHMKGS VAYVPQQAWI QNCTLQENVL FGKALNPKRY
QQTLEACALL ADLEMLPGGD QTEIGEKGIN LSGGQRQRVS LARAVYSDAD IFLLDDPLSA
VDSHVAKHIF DHVIGPEGVL AGKTRVLVTH GISFLPQTDF IIVLADGQVS EMGPYPALLQ
RNGSFANFLC NYAPDEDQGH LEDSWTALEG AEDKEALLIE DTLSNHTDLT DNDPVTYVVQ
KQFMRQLSAL SSDGEGQGRP VPRRHLGPSE KVQVTEAKAD GALTQEEKAA IGTVELSVFW
DYAKAVGLCT TLAICLLYVG QSAAAIGANV WLSAWTNDAM ADSRQNNTSL RLGVYAALGI
LQGFLVMLAA MAMAAGGIQA ARVLHQALLH NKIRSPQSFF DTTPSGRILN CFSKDIYVVD
EVLAPVILML LNSFFNAIST LVVIMASTPL FTVVILPLAV LYTLVQRFYA ATSRQLKRLE
SVSRSPIYSH FSETVTGASV IRAYNRSRDF EIISDTKVDA NQRSCYPYII SNRWLSIGVE
FVGNCVVLFA ALFAVIGRSS LNPGLVGLSV SYSLQVTFAL NWMIRMMSDL ESNIVAVERV
KEYSKTETEA PWVVEGSRPP EGWPPRGEVE FRNYSVRYRP GLDLVLRDLS LHVHGGEKVG
IVGRTGAGKS SMTLCLFRIL EAAKGEIRID GLNVADIGLH DLRSQLTIIP QDPILFSGTL
RMNLDPFGSY SEEDIWWALE LSHLHTFVSS QPAGLDFQCS EGGENLSVGQ RQLVCLARAL
LRKSRILVLD EATAAIDLET DNLIQATIRT QFDTCTVLTI AHRLNTIMDY TRVLVLDKGV
VAEFDSPANL IAARGIFYGM ARDAGLA


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