MSRE_HUMAN
ID MSRE_HUMAN Reviewed; 451 AA.
AC P21757; D3DSP3; O60505; P21759; Q45F10;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Macrophage scavenger receptor types I and II;
DE AltName: Full=Macrophage acetylated LDL receptor I and II;
DE AltName: Full=Scavenger receptor class A member 1;
DE AltName: CD_antigen=CD204;
GN Name=MSR1; Synonyms=SCARA1;
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] (ISOFORMS I AND II), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=2251254; DOI=10.1073/pnas.87.23.9133;
RA Matsumoto A., Naito M., Itakura H., Ikemoto S., Asaoka H., Hayakawa I.,
RA Kanamori H., Aburatani H., Takaku F., Suzuki H., Kobari Y., Miyai T.,
RA Takahashi K., Cohen E.H., Wydro R., Housman D.E., Kodama T.;
RT "Human macrophage scavenger receptors: primary structure, expression, and
RT localization in atherosclerotic lesions.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9133-9137(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM III), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9548586;
RA Gough P.J., Greaves D.R., Gordon S.;
RT "A naturally occurring isoform of the human macrophage scavenger receptor
RT (SR-A) gene generated by alternative splicing blocks modified LDL uptake.";
RL J. Lipid Res. 39:531-543(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-23 AND ALA-275.
RG NIEHS SNPs program;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 155-272.
RX PubMed=8093617; DOI=10.1016/s0021-9258(18)53970-3;
RA Emi M., Asaoka H., Matsumoto A., Itakura H., Kurihara Y., Wada Y.,
RA Kanamori H., Yazaki Y., Takahashi E., Lepert M.;
RT "Structure, organization, and chromosomal mapping of the human macrophage
RT scavenger receptor gene.";
RL J. Biol. Chem. 268:2120-2125(1993).
RN [8]
RP DISULFIDE BONDS IN SRCR DOMAIN.
RX PubMed=8900177; DOI=10.1074/jbc.271.43.26924;
RA Resnick D., Chatterton J.E., Schwartz K., Slayter H., Krieger M.;
RT "Structures of class A macrophage scavenger receptors. Electron microscopic
RT study of flexible, multidomain, fibrous proteins and determination of the
RT disulfide bond pattern of the scavenger receptor cysteine-rich domain.";
RL J. Biol. Chem. 271:26924-26930(1996).
RN [9]
RP POSSIBLE INVOLVEMENT IN PC, AND VARIANTS ALA-36; TYR-41; ALA-113; TYR-174;
RP ALA-275; SER-369 AND ARG-441.
RX PubMed=12244320; DOI=10.1038/ng994;
RA Xu J., Zheng S.L., Komiya A., Mychaleckyj J.C., Isaacs S.D., Hu J.J.,
RA Sterling D., Lange E.M., Hawkins G.A., Turner A., Ewing C.M., Faith D.A.,
RA Johnson J.R., Suzuki H., Bujnovszky P., Wiley K.E., DeMarzo A.M.,
RA Bova G.S., Chang B., Hall M.C., McCullough D.L., Partin A.W.,
RA Kassabian V.S., Carpten J.D., Bailey-Wilson J.E., Trent J.M., Ohar J.,
RA Bleecker E.R., Walsh P.C., Isaacs W.B., Meyers D.A.;
RT "Germline mutations and sequence variants of the macrophage scavenger
RT receptor 1 gene are associated with prostate cancer risk.";
RL Nat. Genet. 32:321-325(2002).
RN [10]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP INVOLVEMENT IN BE, AND VARIANT VAL-254.
RX PubMed=21791690; DOI=10.1001/jama.2011.1029;
RA Orloff M., Peterson C., He X., Ganapathi S., Heald B., Yang Y.R., Bebek G.,
RA Romigh T., Song J.H., Wu W., David S., Cheng Y., Meltzer S.J., Eng C.;
RT "Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with Barrett
RT esophagus and esophageal adenocarcinoma.";
RL JAMA 306:410-419(2011).
RN [13]
RP INTERACTION WITH MYO18A.
RX PubMed=25965346; DOI=10.1371/journal.pone.0126576;
RA Yang L., Carrillo M., Wu Y.M., DiAngelo S.L., Silveyra P., Umstead T.M.,
RA Halstead E.S., Davies M.L., Hu S., Floros J., McCormack F.X.,
RA Christensen N.D., Chroneos Z.C.;
RT "SP-R210 (Myo18A) isoforms as intrinsic modulators of macrophage priming
RT and activation.";
RL PLoS ONE 10:E0126576-E0126576(2015).
CC -!- FUNCTION: Membrane glycoproteins implicated in the pathologic
CC deposition of cholesterol in arterial walls during atherogenesis. Two
CC types of receptor subunits exist. These receptors mediate the
CC endocytosis of a diverse group of macromolecules, including modified
CC low density lipoproteins (LDL) (PubMed:2251254). Isoform III does not
CC internalize acetylated LDL (PubMed:9548586).
CC {ECO:0000269|PubMed:2251254, ECO:0000269|PubMed:9548586}.
CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with MYO18A
CC (PubMed:25965346). {ECO:0000250|UniProtKB:P30204,
CC ECO:0000269|PubMed:25965346}.
CC -!- INTERACTION:
CC P21757; P27449: ATP6V0C; NbExp=6; IntAct=EBI-1776976, EBI-721179;
CC P21757; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-1776976, EBI-11337888;
CC P21757; Q86VS8: HOOK3; NbExp=4; IntAct=EBI-1776976, EBI-1777078;
CC P21757; O95214: LEPROTL1; NbExp=4; IntAct=EBI-1776976, EBI-750776;
CC P21757; Q6FHL7: LEPROTL1; NbExp=3; IntAct=EBI-1776976, EBI-10249700;
CC P21757; Q13021: MALL; NbExp=6; IntAct=EBI-1776976, EBI-750078;
CC P21757; Q16617: NKG7; NbExp=7; IntAct=EBI-1776976, EBI-3919611;
CC P21757; Q96IW7: SEC22A; NbExp=7; IntAct=EBI-1776976, EBI-8652744;
CC P21757; Q7TQ77; Xeno; NbExp=2; IntAct=EBI-1776976, EBI-1777000;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=I;
CC IsoId=P21757-1; Sequence=Displayed;
CC Name=II;
CC IsoId=P21757-2; Sequence=VSP_006229, VSP_006230;
CC Name=III;
CC IsoId=P21757-3; Sequence=VSP_036842;
CC -!- TISSUE SPECIFICITY: Isoform I, isoform II and isoform III are expressed
CC in monocyte-derived macrophages. Isoform I and isoform II are expressed
CC in the liver, placenta and brain. {ECO:0000269|PubMed:2251254,
CC ECO:0000269|PubMed:9548586}.
CC -!- DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy originating in
CC tissues of the prostate. Most prostate cancers are adenocarcinomas that
CC develop in the acini of the prostatic ducts. Other rare histopathologic
CC types of prostate cancer that occur in approximately 5% of patients
CC include small cell carcinoma, mucinous carcinoma, prostatic ductal
CC carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal
CC cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell
CC carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:12244320}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry. MSR1 variants may play a role in
CC susceptibility to prostate cancer. MSR1 variants have been found in
CC individuals with prostate cancer and co-segregate with the disease in
CC some families.
CC -!- DISEASE: Barrett esophagus (BE) [MIM:614266]: A condition characterized
CC by a metaplastic change in which normal esophageal squamous epithelium
CC is replaced by a columnar and intestinal-type epithelium. Patients with
CC Barrett esophagus have an increased risk of esophageal adenocarcinoma.
CC The main cause of Barrett esophagus is gastroesophageal reflux. The
CC retrograde movement of acid and bile salts from the stomach into the
CC esophagus causes prolonged injury to the esophageal epithelium and
CC induces chronic esophagitis, which in turn is believed to trigger the
CC pathologic changes. {ECO:0000269|PubMed:21791690}. Note=The disease may
CC be caused by variants affecting the gene represented in this entry.
CC Genetic variants in MSR1 have been found in individuals with Barrett
CC esophagus and are thought to contribute to disease susceptibility.
CC -!- MISCELLANEOUS: [Isoform II]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/msr1/";
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DR EMBL; D90187; BAA14208.1; -; mRNA.
DR EMBL; D90188; BAA14209.1; -; mRNA.
DR EMBL; AF037351; AAC09251.1; -; mRNA.
DR EMBL; DQ144993; AAZ38715.1; -; Genomic_DNA.
DR EMBL; AC023396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63832.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63830.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63833.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63834.1; -; Genomic_DNA.
DR EMBL; BC063878; AAH63878.1; -; mRNA.
DR EMBL; D13263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS5995.1; -. [P21757-1]
DR CCDS; CCDS5996.1; -. [P21757-3]
DR CCDS; CCDS5997.1; -. [P21757-2]
DR PIR; A38415; A38415.
DR PIR; B38415; B38415.
DR RefSeq; NP_002436.1; NM_002445.3. [P21757-2]
DR RefSeq; NP_619729.1; NM_138715.2. [P21757-1]
DR RefSeq; NP_619730.1; NM_138716.2. [P21757-3]
DR PDB; 7DPX; X-ray; 2.00 A; A=349-451.
DR PDBsum; 7DPX; -.
DR AlphaFoldDB; P21757; -.
DR SMR; P21757; -.
DR BioGRID; 110587; 20.
DR IntAct; P21757; 14.
DR MINT; P21757; -.
DR STRING; 9606.ENSP00000262101; -.
DR BindingDB; P21757; -.
DR ChEMBL; CHEMBL5811; -.
DR GlyGen; P21757; 7 sites.
DR iPTMnet; P21757; -.
DR PhosphoSitePlus; P21757; -.
DR BioMuta; MSR1; -.
DR DMDM; 127357; -.
DR jPOST; P21757; -.
DR MassIVE; P21757; -.
DR PaxDb; P21757; -.
DR PeptideAtlas; P21757; -.
DR PRIDE; P21757; -.
DR ProteomicsDB; 53900; -. [P21757-1]
DR ProteomicsDB; 53901; -. [P21757-2]
DR ProteomicsDB; 53902; -. [P21757-3]
DR Antibodypedia; 601; 951 antibodies from 39 providers.
DR DNASU; 4481; -.
DR Ensembl; ENST00000262101.10; ENSP00000262101.5; ENSG00000038945.15. [P21757-1]
DR Ensembl; ENST00000350896.3; ENSP00000262100.3; ENSG00000038945.15. [P21757-3]
DR Ensembl; ENST00000355282.6; ENSP00000347430.2; ENSG00000038945.15. [P21757-3]
DR Ensembl; ENST00000381998.8; ENSP00000371428.4; ENSG00000038945.15. [P21757-2]
DR GeneID; 4481; -.
DR KEGG; hsa:4481; -.
DR MANE-Select; ENST00000262101.10; ENSP00000262101.5; NM_138715.3; NP_619729.1.
DR UCSC; uc003wwz.4; human. [P21757-1]
DR CTD; 4481; -.
DR DisGeNET; 4481; -.
DR GeneCards; MSR1; -.
DR HGNC; HGNC:7376; MSR1.
DR HPA; ENSG00000038945; Tissue enriched (lung).
DR MalaCards; MSR1; -.
DR MIM; 153622; gene.
DR MIM; 176807; phenotype.
DR MIM; 614266; phenotype.
DR neXtProt; NX_P21757; -.
DR OpenTargets; ENSG00000038945; -.
DR Orphanet; 1331; Familial prostate cancer.
DR PharmGKB; PA31181; -.
DR VEuPathDB; HostDB:ENSG00000038945; -.
DR eggNOG; ENOG502QUW0; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_041152_2_0_1; -.
DR InParanoid; P21757; -.
DR OMA; RGPHEGR; -.
DR OrthoDB; 900867at2759; -.
DR PhylomeDB; P21757; -.
DR TreeFam; TF330855; -.
DR PathwayCommons; P21757; -.
DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
DR SignaLink; P21757; -.
DR SIGNOR; P21757; -.
DR BioGRID-ORCS; 4481; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; MSR1; human.
DR GeneWiki; MSR1; -.
DR GenomeRNAi; 4481; -.
DR Pharos; P21757; Tbio.
DR PRO; PR:P21757; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P21757; protein.
DR Bgee; ENSG00000038945; Expressed in right lung and 128 other tissues.
DR ExpressionAtlas; P21757; baseline and differential.
DR Genevisible; P21757; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
DR GO; GO:0038024; F:cargo receptor activity; ISS:ARUK-UCL.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISS:BHF-UCL.
DR GO; GO:0005044; F:scavenger receptor activity; TAS:ARUK-UCL.
DR GO; GO:0097242; P:amyloid-beta clearance; ISS:ARUK-UCL.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0030301; P:cholesterol transport; ISS:BHF-UCL.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0042953; P:lipoprotein transport; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:ARUK-UCL.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:ARUK-UCL.
DR GO; GO:0034381; P:plasma lipoprotein particle clearance; ISS:BHF-UCL.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; ISS:BHF-UCL.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISS:BHF-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:ARUK-UCL.
DR Gene3D; 3.10.250.10; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR003543; SR-AI/II.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR19331:SF440; PTHR19331:SF440; 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF03523; Macscav_rec; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR01408; MACSCAVRCPTR.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Collagen; Disulfide bond;
KW Endocytosis; Glycoprotein; LDL; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..451
FT /note="Macrophage scavenger receptor types I and II"
FT /id="PRO_0000181627"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..76
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 273..341
FT /note="Collagen-like"
FT DOMAIN 350..450
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 77..109
FT /note="Spacer"
FT /evidence="ECO:0000305"
FT REGION 267..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 171..255
FT /evidence="ECO:0000255"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30204"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 375..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:8900177"
FT DISULFID 388..449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:8900177"
FT DISULFID 419..429
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:8900177"
FT VAR_SEQ 345..408
FT /note="TPFTKVRLVGGSGPHEGRVEILHSGQWGTICDDRWEVRVGQVVCRSLGYPGV
FT QAVHKAAHFGQG -> S (in isoform III)"
FT /evidence="ECO:0000303|PubMed:9548586"
FT /id="VSP_036842"
FT VAR_SEQ 345..358
FT /note="TPFTKVRLVGGSGP -> RPVQLTDHIRAGPS (in isoform II)"
FT /evidence="ECO:0000303|PubMed:2251254"
FT /id="VSP_006229"
FT VAR_SEQ 359..451
FT /note="Missing (in isoform II)"
FT /evidence="ECO:0000303|PubMed:2251254"
FT /id="VSP_006230"
FT VARIANT 23
FT /note="F -> C (in dbSNP:rs35175081)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025190"
FT VARIANT 36
FT /note="P -> A (found in a family with prostate cancer;
FT dbSNP:rs749666450)"
FT /evidence="ECO:0000269|PubMed:12244320"
FT /id="VAR_066581"
FT VARIANT 41
FT /note="S -> Y (found in patients with prostate cancer;
FT dbSNP:rs145597376)"
FT /evidence="ECO:0000269|PubMed:12244320"
FT /id="VAR_066582"
FT VARIANT 113
FT /note="V -> A (found in patients with prostate cancer;
FT dbSNP:rs117359034)"
FT /evidence="ECO:0000269|PubMed:12244320"
FT /id="VAR_066583"
FT VARIANT 174
FT /note="D -> Y (found in patients with prostate cancer;
FT dbSNP:rs72552387)"
FT /evidence="ECO:0000269|PubMed:12244320"
FT /id="VAR_066584"
FT VARIANT 254
FT /note="L -> V (found in patients with Barrett esophagus;
FT dbSNP:rs387906645)"
FT /evidence="ECO:0000269|PubMed:21791690"
FT /id="VAR_066585"
FT VARIANT 269
FT /note="T -> I (in dbSNP:rs13306543)"
FT /id="VAR_052061"
FT VARIANT 275
FT /note="P -> A (in dbSNP:rs2229388)"
FT /evidence="ECO:0000269|PubMed:12244320, ECO:0000269|Ref.3"
FT /id="VAR_025191"
FT VARIANT 369
FT /note="G -> S (found in a family with prostate cancer;
FT dbSNP:rs776370129)"
FT /evidence="ECO:0000269|PubMed:12244320"
FT /id="VAR_066586"
FT VARIANT 441
FT /note="H -> R (found in patients with prostate cancer;
FT dbSNP:rs138749399)"
FT /evidence="ECO:0000269|PubMed:12244320"
FT /id="VAR_066587"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:7DPX"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:7DPX"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:7DPX"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:7DPX"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:7DPX"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:7DPX"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:7DPX"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:7DPX"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:7DPX"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:7DPX"
FT STRAND 446..450
FT /evidence="ECO:0007829|PDB:7DPX"
SQ SEQUENCE 451 AA; 49762 MW; 915C03B56653BB41 CRC64;
MEQWDHFHNQ QEDTDSCSES VKFDARSMTA LLPPNPKNSP SLQEKLKSFK AALIALYLLV
FAVLIPLIGI VAAQLLKWET KNCSVSSTNA NDITQSLTGK GNDSEEEMRF QEVFMEHMSN
MEKRIQHILD MEANLMDTEH FQNFSMTTDQ RFNDILLQLS TLFSSVQGHG NAIDEISKSL
ISLNTTLLDL QLNIENLNGK IQENTFKQQE EISKLEERVY NVSAEIMAMK EEQVHLEQEI
KGEVKVLNNI TNDLRLKDWE HSQTLRNITL IQGPPGPPGE KGDRGPTGES GPRGFPGPIG
PPGLKGDRGA IGFPGSRGLP GYAGRPGNSG PKGQKGEKGS GNTLTPFTKV RLVGGSGPHE
GRVEILHSGQ WGTICDDRWE VRVGQVVCRS LGYPGVQAVH KAAHFGQGTG PIWLNEVFCF
GRESSIEECK IRQWGTRACS HSEDAGVTCT L
