SREC2_HUMAN
ID SREC2_HUMAN Reviewed; 871 AA.
AC Q96GP6; E5RFB8; Q58A83; Q8IXF3; Q9BW74;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 5.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Scavenger receptor class F member 2;
DE AltName: Full=SRECRP-1;
DE AltName: Full=Scavenger receptor expressed by endothelial cells 2 protein;
DE Short=SREC-II;
DE Flags: Precursor;
GN Name=SCARF2; Synonyms=SREC2, SREPCR;
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] (ISOFORM 2), AND VARIANT SER-174.
RA Adachi H., Tsujimoto M.;
RT "cDNA cloning of SRECRP (scavenger receptor expressed by endothelial cell
RT related protein).";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP ASP-778 AND VAL-779.
RC TISSUE=Epithelium;
RX PubMed=12154095; DOI=10.1074/jbc.m206140200;
RA Ishii J., Adachi H., Aoki J., Koizumi H., Tomita S., Suzuki T.,
RA Tsujimoto M., Inoue K., Arai H.;
RT "SREC-II, a new member of the scavenger receptor type F family, trans-
RT interacts with SREC-I through its extracellular domain.";
RL J. Biol. Chem. 277:39696-39702(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Vulva;
RA Kitaura M., Iwagami S., Tsuruta Y., Suzuki R.;
RT "A novel human nurse cell receptor NSR1.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
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] OF 272-871 (ISOFORM 2).
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651; SER-653 AND SER-718, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-653 AND SER-742, 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 [10]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-499.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [11]
RP VARIANT VDEGS TYR-258.
RX PubMed=20887961; DOI=10.1016/j.ajhg.2010.09.005;
RA Anastasio N., Ben-Omran T., Teebi A., Ha K.C., Lalonde E., Ali R.,
RA Almureikhi M., Der Kaloustian V.M., Liu J., Rosenblatt D.S., Majewski J.,
RA Jerome-Majewska L.A.;
RT "Mutations in SCARF2 are responsible for Van Den Ende-Gupta syndrome.";
RL Am. J. Hum. Genet. 87:553-559(2010).
CC -!- FUNCTION: Probable adhesion protein, which mediates homophilic and
CC heterophilic interactions. In contrast to SCARF1, it poorly mediates
CC the binding and degradation of acetylated low density lipoprotein (Ac-
CC LDL) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homophilic and heterophilic interaction via its extracellular
CC domain. Interacts with SCARF1. The heterophilic interaction with
CC SCARF1, which is stronger than the homophilic interaction with itself,
CC is suppressed by the presence of SCARF1 ligand such as Ac-LDL (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q96GP6; P16333: NCK1; NbExp=2; IntAct=EBI-1752088, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96GP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96GP6-2; Sequence=VSP_042462;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in endothelial cells.
CC Expressed in heart, placenta, lung, kidney, spleen, small intestine and
CC ovary. {ECO:0000269|PubMed:12154095}.
CC -!- DISEASE: Van den Ende-Gupta syndrome (VDEGS) [MIM:600920]: A syndrome
CC characterized by craniofacial and skeletal abnormalities that include
CC blepharophimosis, a flat and wide nasal bridge, narrow and beaked nose,
CC hypoplastic maxilla with or without cleft palate and everted lower lip,
CC prominent ears, down-slanting eyes, arachnodactyly, and camptodactyly.
CC Patients present congenital joint contractures that improve without
CC intervention, and normal growth and development. Intelligence is
CC normal. Rarely, enlarged cerebella can be present. Some patients
CC experience respiratory problems due to laryngeal abnormalities.
CC {ECO:0000269|PubMed:20887961}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN45861.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB052951; BAC53753.1; -; mRNA.
DR EMBL; AF522196; AAN45861.1; ALT_FRAME; mRNA.
DR EMBL; AB024433; BAD93345.1; -; mRNA.
DR EMBL; AC007731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471176; EAX02965.1; -; Genomic_DNA.
DR EMBL; BC000584; AAH00584.2; -; mRNA.
DR EMBL; BC009326; AAH09326.2; -; mRNA.
DR CCDS; CCDS13779.2; -. [Q96GP6-1]
DR CCDS; CCDS46666.1; -. [Q96GP6-2]
DR RefSeq; NP_699165.3; NM_153334.6. [Q96GP6-1]
DR RefSeq; NP_878315.2; NM_182895.4. [Q96GP6-2]
DR AlphaFoldDB; Q96GP6; -.
DR SMR; Q96GP6; -.
DR BioGRID; 124803; 14.
DR IntAct; Q96GP6; 8.
DR STRING; 9606.ENSP00000477564; -.
DR GlyGen; Q96GP6; 4 sites.
DR iPTMnet; Q96GP6; -.
DR PhosphoSitePlus; Q96GP6; -.
DR SwissPalm; Q96GP6; -.
DR BioMuta; SCARF2; -.
DR DMDM; 380865486; -.
DR jPOST; Q96GP6; -.
DR MassIVE; Q96GP6; -.
DR PaxDb; Q96GP6; -.
DR PeptideAtlas; Q96GP6; -.
DR PRIDE; Q96GP6; -.
DR ProteomicsDB; 76651; -. [Q96GP6-1]
DR ProteomicsDB; 76652; -. [Q96GP6-2]
DR Antibodypedia; 51072; 107 antibodies from 23 providers.
DR DNASU; 91179; -.
DR Ensembl; ENST00000622235.5; ENSP00000477564.2; ENSG00000244486.9. [Q96GP6-2]
DR Ensembl; ENST00000623402.1; ENSP00000485276.1; ENSG00000244486.9. [Q96GP6-1]
DR GeneID; 91179; -.
DR KEGG; hsa:91179; -.
DR MANE-Select; ENST00000622235.5; ENSP00000477564.2; NM_182895.5; NP_878315.2. [Q96GP6-2]
DR UCSC; uc062bsr.1; human. [Q96GP6-1]
DR CTD; 91179; -.
DR DisGeNET; 91179; -.
DR GeneCards; SCARF2; -.
DR HGNC; HGNC:19869; SCARF2.
DR HPA; ENSG00000244486; Low tissue specificity.
DR MalaCards; SCARF2; -.
DR MIM; 600920; phenotype.
DR MIM; 613619; gene.
DR neXtProt; NX_Q96GP6; -.
DR OpenTargets; ENSG00000244486; -.
DR Orphanet; 2460; Van den Ende-Gupta syndrome.
DR PharmGKB; PA134908523; -.
DR VEuPathDB; HostDB:ENSG00000244486; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00950000183101; -.
DR HOGENOM; CLU_017821_1_0_1; -.
DR InParanoid; Q96GP6; -.
DR OMA; KCTCHPN; -.
DR OrthoDB; 110992at2759; -.
DR PhylomeDB; Q96GP6; -.
DR TreeFam; TF332598; -.
DR PathwayCommons; Q96GP6; -.
DR SignaLink; Q96GP6; -.
DR BioGRID-ORCS; 91179; 40 hits in 1068 CRISPR screens.
DR ChiTaRS; SCARF2; human.
DR GenomeRNAi; 91179; -.
DR Pharos; Q96GP6; Tbio.
DR PRO; PR:Q96GP6; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q96GP6; protein.
DR Bgee; ENSG00000244486; Expressed in right coronary artery and 98 other tissues.
DR Genevisible; Q96GP6; HS.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR033327; Scarf2.
DR InterPro; IPR042635; SREC1/2.
DR PANTHER; PTHR24043; PTHR24043; 1.
DR PANTHER; PTHR24043:SF5; PTHR24043:SF5; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00180; EGF_Lam; 6.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Disease variant; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..871
FT /note="Scavenger receptor class F member 2"
FT /id="PRO_0000007739"
FT TOPO_DOM 44..441
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..871
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 71..110
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 122..153
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 148..182
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 183..212
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 213..241
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 236..270
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 372..403
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..824
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59222"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 628
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P59222"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59222"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 80..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 100..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 126..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 128..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 143..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 156..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 158..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 172..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 185..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 187..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 202..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 215..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 217..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 231..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 244..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 246..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 260..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 376..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 379..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 393..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 474..478
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.3"
FT /id="VSP_042462"
FT VARIANT 174
FT /note="P -> S (in dbSNP:rs361566)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_059274"
FT VARIANT 258
FT /note="C -> Y (in VDEGS; dbSNP:rs387907086)"
FT /evidence="ECO:0000269|PubMed:20887961"
FT /id="VAR_065302"
FT VARIANT 425
FT /note="T -> S (in dbSNP:rs2241230)"
FT /id="VAR_055776"
FT VARIANT 499
FT /note="R -> C (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035837"
FT VARIANT 522
FT /note="H -> L (in dbSNP:rs12484828)"
FT /id="VAR_055777"
FT VARIANT 778
FT /note="E -> D (in dbSNP:rs759611)"
FT /evidence="ECO:0000269|PubMed:12154095"
FT /id="VAR_015148"
FT VARIANT 779
FT /note="L -> V (in dbSNP:rs759612)"
FT /evidence="ECO:0000269|PubMed:12154095"
FT /id="VAR_015149"
FT VARIANT 820
FT /note="A -> G (in dbSNP:rs874100)"
FT /id="VAR_015150"
FT VARIANT 838
FT /note="A -> G (in dbSNP:rs874101)"
FT /id="VAR_015151"
FT CONFLICT 629..641
FT /note="ARVARREARPARA -> PTTTWITHSTAAS (in Ref. 6;
FT AAH00584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 871 AA; 92384 MW; E41852FABD1E47AD CRC64;
MEGAGPRGAG PARRRGAGGP PSPLLPSLLL LLLLWMLPDT VAPQELNPRG RNVCRAPGSQ
VPTCCAGWRQ QGDECGIAVC EGNSTCSENE VCVRPGECRC RHGYFGANCD TKCPRQFWGP
DCKELCSCHP HGQCEDVTGQ CTCHARRWGA RCEHACQCQH GTCHPRSGAC RCEPGWWGAQ
CASACYCSAT SRCDPQTGAC LCHAGWWGRS CNNQCACNSS PCEQQSGRCQ CRERTFGARC
DRYCQCFRGR CHPVDGTCAC EPGYRGKYCR EPCPAGFYGL GCRRRCGQCK GQQPCTVAEG
RCLTCEPGWN GTKCDQPCAT GFYGEGCSHR CPPCRDGHAC NHVTGKCTRC NAGWIGDRCE
TKCSNGTYGE DCAFVCADCG SGHCDFQSGR CLCSPGVHGP HCNVTCPPGL HGADCAQACS
CHEDTCDPVT GACHLETNQR KGVMGAGALL VLLVCLLLSL LGCCCACRGK DPTRRPRPRR
ELSLGRKKAP HRLCGRFSRI SMKLPRIPLR RQKLPKVVVA HHDLDNTLNC SFLEPPSGLE
QPSPSWSSRA SFSSFDTTDE GPVYCVPHEE APAESRDPEV PTVPAEAPAP SPVPLTTPAS
AEEAIPLPAS SDSERSASSV EGPGGALYAR VARREARPAR ARGEIGGLSL SPSPERRKPP
PPDPATKPKV SWIHGKHSAA AAGRAPSPPP PGSEAAPSPS KRKRTPSDKS AHTVEHGSPR
TRDPTPRPPG LPEEATALAA PSPPRARARG RGPGLLEPTD AGGPPRSAPE AASMLAAELR
GKTRSLGRAE VALGAQGPRE KPAPPQKAKR SVPPASPARA PPATETPGPE KAATDLPAPE
TPRKKTPIQK PPRKKSREAA GELGRAGAPT L
