ID ADA12_HUMAN Reviewed; 909 AA. AC O43184; O60470; Q5JRP0; Q5JRP1; Q6P9E3; Q6UWB0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 3. DT 13-FEB-2019, entry version 188. DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 12; DE Short=ADAM 12; DE EC=3.4.24.-; DE AltName: Full=Meltrin-alpha; DE Flags: Precursor; GN Name=ADAM12; Synonyms=MLTN; ORFNames=UNQ346/PRO545; 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 [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ARG-48. RC TISSUE=Placenta; RX PubMed=9417060; DOI=10.1074/jbc.273.1.157; RA Gilpin B.J., Loechel F., Mattei M.-G., Engvall E., Albrechtsen R., RA Wewer U.M.; RT "A novel, secreted form of human ADAM 12 (meltrin alpha) provokes RT myogenesis in vivo."; RL J. Biol. Chem. 273:157-166(1998). RN [2] RP SEQUENCE REVISION TO 36. RA Gilpin B.J., Loechel F., Mattei M.-G., Engvall E., Albrechtsen R., RA Wewer U.M.; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT RP ARG-48. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-48. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT RP ARG-48. RC TISSUE=Placenta; 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 [7] RP CHARACTERIZATION. RX PubMed=9642263; DOI=10.1074/jbc.273.27.16993; RA Loechel F., Gilpin B.J., Engvall E., Albrechtsen R., Wewer U.M.; RT "Human ADAM 12 (meltrin alpha) is an active metalloprotease."; RL J. Biol. Chem. 273:16993-16997(1998). RN [8] RP INTERACTION WITH SYNDECANS. RX PubMed=10831617; DOI=10.1083/jcb.149.5.1143; RA Iba K., Albrechtsen R., Gilpin B.J., Froehlich C., Loechel F., RA Zolkiewska A., Ishiguro K., Kojima T., Liu W., Langford J.K., RA Sanderson R.D., Brakebusch C., Faessler R., Wewer U.M.; RT "The cysteine-rich domain of human ADAM 12 supports cell adhesion RT through syndecans and triggers signaling events that lead to beta1 RT integrin-dependent cell spreading."; RL J. Cell Biol. 149:1143-1156(2000). RN [9] RP INTERACTION WITH SH3PXD2A. RX PubMed=12615925; DOI=10.1074/jbc.M300267200; RA Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M., RA Courtneidge S.A.; RT "The adaptor protein fish associates with members of the ADAMs family RT and localizes to podosomes of Src-transformed cells."; RL J. Biol. Chem. 278:16844-16851(2003). RN [10] RP INTERACTION WITH FST3. RX PubMed=15574124; DOI=10.1042/BC20040506; RA Bartholin L., Destaing O., Forissier S., Martel S., Maguer-Satta V., RA Jurdic P., Rimokh R.; RT "FLRG, a new ADAM12-associated protein, modulates osteoclast RT differentiation."; RL Biol. Cell 97:577-588(2005). RN [11] RP INTERACTION WITH RACK1. RX PubMed=18621736; DOI=10.1074/jbc.M709829200; RA Bourd-Boittin K., Le Pabic H., Bonnier D., L'Helgoualc'h A., RA Theret N.; RT "RACK1, a new ADAM12 interacting protein. Contribution to liver RT fibrogenesis."; RL J. Biol. Chem. 283:26000-26009(2008). RN [12] RP VARIANTS [LARGE SCALE ANALYSIS] HIS-301; GLU-479 AND PHE-792. 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., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [13] RP VARIANTS GLU-712 AND SER-893. RX PubMed=21618342; DOI=10.1002/humu.21477; RA Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J., RA Rudloff U., Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.; RT "Analysis of the disintegrin-metalloproteinases family reveals ADAM29 RT and ADAM7 are often mutated in melanoma."; RL Hum. Mutat. 32:E2148-E2175(2011). CC -!- FUNCTION: Involved in skeletal muscle regeneration, specifically CC at the onset of cell fusion. Also involved in macrophage-derived CC giant cells (MGC) and osteoclast formation from mononuclear CC precursors (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; CC -!- SUBUNIT: Interacts with alpha-actinin-2 and with syndecans (By CC similarity). Interacts with SH3PXD2A. Interacts with FST3. CC Interacts with RACK1; the interaction is required for PKC- CC dependent translocation of ADAM12 to the cell membrane. CC {ECO:0000250, ECO:0000269|PubMed:10831617, CC ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:15574124, CC ECO:0000269|PubMed:18621736}. CC -!- INTERACTION: CC A8MQ03:CYSRT1; NbExp=4; IntAct=EBI-12006944, EBI-3867333; CC O95633:FSTL3; NbExp=4; IntAct=EBI-2625865, EBI-2625790; CC Q6L8G9:KRTAP5-6; NbExp=4; IntAct=EBI-12006944, EBI-10250562; CC Q9BYQ4:KRTAP9-2; NbExp=4; IntAct=EBI-12006944, EBI-1044640; CC Q9BYQ0:KRTAP9-8; NbExp=4; IntAct=EBI-12006944, EBI-11958364; CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I CC membrane protein. CC -!- SUBCELLULAR LOCATION: Isoform 2: Secreted. CC -!- SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Isoform 4: Secreted {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=12L; CC IsoId=O43184-1; Sequence=Displayed; CC Name=2; Synonyms=12S; CC IsoId=O43184-2; Sequence=VSP_005476, VSP_005477; CC Name=3; CC IsoId=O43184-3; Sequence=VSP_031001, VSP_005476, VSP_005477; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=O43184-4; Sequence=VSP_031001, VSP_031002, VSP_031003; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in placenta and CC skeletal, cardiac, and smooth muscle. Isoform 2 seems to be CC expressed only in placenta or in embryo and fetus. Both forms were CC expressed in some tumor cells lines. Not detected in brain, lung, CC liver, kidney or pancreas. CC -!- DOMAIN: The cysteine-rich domain supports cell adhesion through CC syndecans and triggers signaling events that lead to beta-1 CC integrin-dependent cell spreading. In carcinomas cells the binding CC of this domain to syndecans does not allow the integrin-mediated CC cell spreading. CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch CC motif binds the catalytic zinc ion, thus inhibiting the enzyme. CC The dissociation of the cysteine from the zinc ion upon the CC activation-peptide release activates the enzyme. CC -!- PTM: The precursor is cleaved by a furin endopeptidase. CC {ECO:0000250}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/ADAM12ID44084ch10q26.html"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF023476; AAC08702.2; -; mRNA. DR EMBL; AF023477; AAC08703.2; -; mRNA. DR EMBL; AY358878; AAQ89237.1; -; mRNA. DR EMBL; AC022015; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026226; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC063963; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL589787; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49206.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49209.1; -; Genomic_DNA. DR EMBL; BC060804; AAH60804.1; -; mRNA. DR CCDS; CCDS7653.1; -. [O43184-1] DR CCDS; CCDS7654.1; -. [O43184-2] DR RefSeq; NP_001275903.1; NM_001288974.1. [O43184-4] DR RefSeq; NP_001275904.1; NM_001288975.1. [O43184-3] DR RefSeq; NP_003465.3; NM_003474.5. [O43184-1] DR RefSeq; NP_067673.2; NM_021641.4. [O43184-2] DR UniGene; Hs.594351; -. DR UniGene; Hs.741333; -. DR ProteinModelPortal; O43184; -. DR SMR; O43184; -. DR BioGrid; 113731; 5. DR CORUM; O43184; -. DR IntAct; O43184; 32. DR MINT; O43184; -. DR STRING; 9606.ENSP00000357668; -. DR BindingDB; O43184; -. DR ChEMBL; CHEMBL5030; -. DR GuidetoPHARMACOLOGY; 1660; -. DR MEROPS; M12.212; -. DR TCDB; 8.A.77.1.5; the sheddase (sheddase) family. DR CarbonylDB; O43184; -. DR iPTMnet; O43184; -. DR PhosphoSitePlus; O43184; -. DR BioMuta; ADAM12; -. DR jPOST; O43184; -. DR MaxQB; O43184; -. DR PaxDb; O43184; -. DR PeptideAtlas; O43184; -. DR PRIDE; O43184; -. DR ProteomicsDB; 48799; -. DR ProteomicsDB; 48800; -. [O43184-2] DR ProteomicsDB; 48801; -. [O43184-3] DR ProteomicsDB; 48802; -. [O43184-4] DR Ensembl; ENST00000368676; ENSP00000357665; ENSG00000148848. [O43184-2] DR Ensembl; ENST00000368679; ENSP00000357668; ENSG00000148848. [O43184-1] DR GeneID; 8038; -. DR KEGG; hsa:8038; -. DR UCSC; uc001ljk.4; human. [O43184-1] DR CTD; 8038; -. DR DisGeNET; 8038; -. DR EuPathDB; HostDB:ENSG00000148848.14; -. DR GeneCards; ADAM12; -. DR H-InvDB; HIX0009299; -. DR HGNC; HGNC:190; ADAM12. DR HPA; HPA030866; -. DR HPA; HPA030867; -. DR HPA; HPA030868; -. DR MIM; 602714; gene. DR neXtProt; NX_O43184; -. DR OpenTargets; ENSG00000148848; -. DR PharmGKB; PA24507; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00940000155495; -. DR HOGENOM; HOG000230883; -. DR HOVERGEN; HBG006978; -. DR InParanoid; O43184; -. DR KO; K06835; -. DR OMA; WARRHKR; -. DR OrthoDB; 278674at2759; -. DR PhylomeDB; O43184; -. DR TreeFam; TF314733; -. DR BRENDA; 3.4.24.B10; 2681. DR Reactome; R-HSA-177929; Signaling by EGFR. DR Reactome; R-HSA-8941237; Invadopodia formation. DR SIGNOR; O43184; -. DR ChiTaRS; ADAM12; human. DR GeneWiki; ADAM12; -. DR GenomeRNAi; 8038; -. DR PRO; PR:O43184; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000148848; Expressed in 147 organ(s), highest expression level in placenta. DR ExpressionAtlas; O43184; baseline and differential. DR Genevisible; O43184; HS. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc. DR GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0007520; P:myoblast fusion; TAS:ProtInc. DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell adhesion; Cell membrane; KW Cleavage on pair of basic residues; Complete proteome; Disulfide bond; KW EGF-like domain; Glycoprotein; Hydrolase; Membrane; Metal-binding; KW Metalloprotease; Phosphoprotein; Polymorphism; Protease; KW Reference proteome; Secreted; SH3-binding; Signal; Transmembrane; KW Transmembrane helix; Zinc; Zymogen. FT SIGNAL 1 28 {ECO:0000255}. FT PROPEP 29 207 {ECO:0000250}. FT /FTId=PRO_0000029078. FT CHAIN 208 909 Disintegrin and metalloproteinase domain- FT containing protein 12. FT /FTId=PRO_0000029079. FT TOPO_DOM 208 708 Extracellular. {ECO:0000255}. FT TRANSMEM 709 729 Helical. {ECO:0000255}. FT TOPO_DOM 730 909 Cytoplasmic. {ECO:0000255}. FT DOMAIN 214 416 Peptidase M12B. {ECO:0000255|PROSITE- FT ProRule:PRU00276}. FT DOMAIN 424 510 Disintegrin. {ECO:0000255|PROSITE- FT ProRule:PRU00068}. FT DOMAIN 656 688 EGF-like. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT MOTIF 177 184 Cysteine switch. {ECO:0000250}. FT MOTIF 828 834 SH3-binding; class II. {ECO:0000250}. FT MOTIF 834 841 SH3-binding; class I. {ECO:0000250}. FT MOTIF 885 891 SH3-binding; class I. {ECO:0000250}. FT COMPBIAS 514 649 Cys-rich. FT ACT_SITE 351 351 FT METAL 179 179 Zinc; in inhibited form. {ECO:0000250}. FT METAL 350 350 Zinc; catalytic. FT METAL 354 354 Zinc; catalytic. FT METAL 360 360 Zinc; catalytic. FT MOD_RES 907 907 Phosphotyrosine; by SRC. {ECO:0000250}. FT CARBOHYD 111 111 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 149 149 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 381 381 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 452 452 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 651 651 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 325 411 {ECO:0000250}. FT DISULFID 367 395 {ECO:0000250}. FT DISULFID 369 378 {ECO:0000250}. FT DISULFID 482 502 {ECO:0000250}. FT DISULFID 660 670 {ECO:0000250}. FT DISULFID 664 676 {ECO:0000250}. FT DISULFID 678 687 {ECO:0000250}. FT VAR_SEQ 114 116 Missing (in isoform 3 and isoform 4). FT {ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_031001. FT VAR_SEQ 705 740 DNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLLFT -> G FT KEARQEAAESNRERGQGQEPVGSQEHASTASLTLI (in FT isoform 4). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_031002. FT VAR_SEQ 705 738 DNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLL -> EAR FT QEAAESNRERGQGQEPVGSQEHASTASLTLI (in FT isoform 2 and isoform 3). FT {ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:9417060}. FT /FTId=VSP_005476. FT VAR_SEQ 739 909 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:9417060}. FT /FTId=VSP_005477. FT VAR_SEQ 741 909 Missing (in isoform 4). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_031003. FT VARIANT 48 48 G -> R (in dbSNP:rs3740199). FT {ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9417060, FT ECO:0000269|Ref.5}. FT /FTId=VAR_038542. FT VARIANT 301 301 D -> H (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036143. FT VARIANT 479 479 G -> E (in a breast cancer sample; FT somatic mutation; dbSNP:rs1459457663). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036144. FT VARIANT 712 712 G -> E (in a cutaneous metastatic FT melanoma sample; somatic mutation). FT {ECO:0000269|PubMed:21618342}. FT /FTId=VAR_066310. FT VARIANT 792 792 L -> F (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036145. FT VARIANT 893 893 P -> S (in a cutaneous metastatic FT melanoma sample; somatic mutation; FT dbSNP:rs151030407). FT {ECO:0000269|PubMed:21618342}. FT /FTId=VAR_066311. SQ SEQUENCE 909 AA; 99542 MW; E28131C64C4304AB CRC64; MAARPLPVSP ARALLLALAG ALLAPCEARG VSLWNQGRAD EVVSASVGSG DLWIPVKSFD SKNHPEVLNI RLQRESKELI INLERNEGLI ASSFTETHYL QDGTDVSLAR NYTVILGHCY YHGHVRGYSD SAVSLSTCSG LRGLIVFENE SYVLEPMKSA TNRYKLFPAK KLKSVRGSCG SHHNTPNLAA KNVFPPPSQT WARRHKRETL KATKYVELVI VADNREFQRQ GKDLEKVKQR LIEIANHVDK FYRPLNIRIV LVGVEVWNDM DKCSVSQDPF TSLHEFLDWR KMKLLPRKSH DNAQLVSGVY FQGTTIGMAP IMSMCTADQS GGIVMDHSDN PLGAAVTLAH ELGHNFGMNH DTLDRGCSCQ MAVEKGGCIM NASTGYPFPM VFSSCSRKDL ETSLEKGMGV CLFNLPEVRE SFGGQKCGNR FVEEGEECDC GEPEECMNRC CNATTCTLKP DAVCAHGLCC EDCQLKPAGT ACRDSSNSCD LPEFCTGASP HCPANVYLHD GHSCQDVDGY CYNGICQTHE QQCVTLWGPG AKPAPGICFE RVNSAGDPYG NCGKVSKSSF AKCEMRDAKC GKIQCQGGAS RPVIGTNAVS IETNIPLQQG GRILCRGTHV YLGDDMPDPG LVLAGTKCAD GKICLNRQCQ NISVFGVHEC AMQCHGRGVC NNRKNCHCEA HWAPPFCDKF GFGGSTDSGP IRQADNQGLT IGILVTILCL LAAGFVVYLK RKTLIRLLFT NKKTTIEKLR CVRPSRPPRG FQPCQAHLGH LGKGLMRKPP DSYPPKDNPR RLLQCQNVDI SRPLNGLNVP QPQSTQRVLP PLHRAPRAPS VPARPLPAKP ALRQAQGTCK PNPPQKPLPA DPLARTTRLT HALARTPGQW ETGLRLAPLR PAPQYPHQVP RSTHTAYIK //