ADA15_HUMAN
ID ADA15_HUMAN Reviewed; 863 AA.
AC Q13444; B3KQU5; B4DLB5; B4DMH8; E9PN65; Q13493; Q53XQ0; Q5SR68; Q5SR69;
AC Q6R267; Q71S61; Q71S62; Q71S63; Q71S64; Q71S65; Q71S66; Q71S67; Q71S68;
AC Q71S69; Q96C78; U3KQL5;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 4.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 15;
DE Short=ADAM 15;
DE EC=3.4.24.-;
DE AltName: Full=Metalloprotease RGD disintegrin protein;
DE AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15;
DE Short=MDC-15;
DE AltName: Full=Metargidin;
DE Flags: Precursor;
GN Name=ADAM15; Synonyms=MDC15;
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 THR-191.
RC TISSUE=Mammary carcinoma;
RX PubMed=8617717; DOI=10.1074/jbc.271.9.4593;
RA Kraetzschmar J., Lum L., Blobel C.P.;
RT "Metargidin, a membrane-anchored metalloprotease-disintegrin protein with
RT an RGD integrin binding sequence.";
RL J. Biol. Chem. 271:4593-4596(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT THR-191.
RC TISSUE=Umbilical vein;
RX PubMed=9039960; DOI=10.1096/fasebj.11.2.9039960;
RA Herren B., Raines E.W., Ross R.;
RT "Expression of a disintegrin-like protein in cultured human vascular cells
RT and in vivo.";
RL FASEB J. 11:173-180(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), FUNCTION, TISSUE SPECIFICITY, AND
RP ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=15358598; DOI=10.1152/ajpgi.00262.2004;
RA Charrier L., Yan Y., Driss A., Laboisse C.L., Sitaraman S.V., Merlin D.;
RT "ADAM-15 inhibits wound healing in human intestinal epithelial cell
RT monolayers.";
RL Am. J. Physiol. 288:G346-G353(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3;
RP 4; 5; 6; 7; 8; 9; 10), AND VARIANT THR-191.
RX PubMed=17937806; DOI=10.1186/1471-2199-8-90;
RA Kleino I., Ortiz R.M., Huovila A.P.;
RT "ADAM15 gene structure and differential alternative exon use in human
RT tissues.";
RL BMC Mol. Biol. 8:90-90(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 10), ALTERNATIVE SPLICING,
RP AND INTERACTION WITH GRB2; MAPK1; MAPK3; NCK1; PTK6; SH3PXD2A AND SRC.
RX PubMed=18296648; DOI=10.1158/1541-7786.mcr-07-2028;
RA Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M.,
RA Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C.,
RA Edwards D.R.;
RT "Distinct functions of natural ADAM-15 cytoplasmic domain variants in human
RT mammary carcinoma.";
RL Mol. Cancer Res. 6:383-394(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8 AND 9), AND
RP VARIANT THR-191.
RA Karkkainen I., Ortiz R.M., Huovila A.-P.J.;
RT "Characterization of human ADAM15 gene and promoter, and evidence for
RT alternative exon use.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-191.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 12 AND 13), AND VARIANTS
RP THR-191 AND LYS-216.
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11).
RC TISSUE=Embryo;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-191.
RC TISSUE=Kidney;
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 [12]
RP TISSUE SPECIFICITY.
RX PubMed=9016778; DOI=10.1006/bbrc.1996.5957;
RA McKie N., Edwards T., Dallas D.J., Houghton A., Stringer B., Graham R.,
RA Russell G., Croucher P.I.;
RT "Expression of members of a novel membrane linked metalloproteinase family
RT (ADAM) in human articular chondrocytes.";
RL Biochem. Biophys. Res. Commun. 230:335-339(1997).
RN [13]
RP INTERACTION WITH INTEGRIN ALPHAV-BETA3.
RX PubMed=9516430; DOI=10.1074/jbc.273.13.7345;
RA Zhang X.P., Kamata T., Yokoyama K., Puzon-McLaughlin W., Takada Y.;
RT "Specific interaction of the recombinant disintegrin-like domain of MDC-15
RT (metargidin, ADAM-15) with integrin alphavbeta3.";
RL J. Biol. Chem. 273:7345-7350(1998).
RN [14]
RP INTERACTION WITH SH3GL2 AND SNX9.
RX PubMed=10531379; DOI=10.1074/jbc.274.44.31693;
RA Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
RT "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two
RT SH3 domain-containing proteins, endophilin I and SH3PX1.";
RL J. Biol. Chem. 274:31693-31699(1999).
RN [15]
RP INTERACTION WITH INTEGRIN ALPHAV-BETA3 AND INTEGRIN ALPHA5-BETA1.
RX PubMed=9914169; DOI=10.1242/jcs.112.4.579;
RA Nath D., Slocombe P.M., Stephens P.E., Warn A., Hutchinson G.R.,
RA Yamada K.M., Docherty A.J., Murphy G.;
RT "Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1
RT integrins on different haemopoietic cells.";
RL J. Cell Sci. 112:579-587(1999).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=12243749; DOI=10.1006/excr.2002.5606;
RA Ham C., Levkau B., Raines E.W., Herren B.;
RT "ADAM15 is an adherens junction molecule whose surface expression can be
RT driven by VE-cadherin.";
RL Exp. Cell Res. 279:239-247(2002).
RN [17]
RP PHOSPHORYLATION AT TYR-715 AND TYR-735, AND INTERACTION WITH GRB2; LCK AND
RP HCK.
RX PubMed=11741929; DOI=10.1074/jbc.m107430200;
RA Poghosyan Z., Robbins S.M., Houslay M.D., Webster A., Murphy G.,
RA Edwards D.R.;
RT "Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain
RT and Src family protein-tyrosine kinases.";
RL J. Biol. Chem. 277:4999-5007(2002).
RN [18]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12091380; DOI=10.1074/jbc.m200988200;
RA Martin J., Eynstone L.V., Davies M., Williams J.D., Steadman R.;
RT "The role of ADAM 15 in glomerular mesangial cell migration.";
RL J. Biol. Chem. 277:33683-33689(2002).
RN [19]
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 and
RT localizes to podosomes of Src-transformed cells.";
RL J. Biol. Chem. 278:16844-16851(2003).
RN [20]
RP FUNCTION.
RX PubMed=15818704; DOI=10.1002/art.20974;
RA Bohm B.B., Aigner T., Roy B., Brodie T.A., Blobel C.P., Burkhardt H.;
RT "Homeostatic effects of the metalloproteinase disintegrin ADAM15 in
RT degenerative cartilage remodeling.";
RL Arthritis Rheum. 52:1100-1109(2005).
RN [21]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17575078; DOI=10.1165/rcmb.2006-0364oc;
RA Lu D., Xie S., Sukkar M.B., Lu X., Scully M.F., Chung K.F.;
RT "Inhibition of airway smooth muscle adhesion and migration by the
RT disintegrin domain of ADAM-15.";
RL Am. J. Respir. Cell Mol. Biol. 37:494-500(2007).
RN [22]
RP FUNCTION, AND MUTAGENESIS OF 484-ARG-GLY-485.
RX PubMed=17416588; DOI=10.1074/jbc.m700158200;
RA Charrier L., Yan Y., Nguyen H.T., Dalmasso G., Laboisse C.L., Gewirtz A.T.,
RA Sitaraman S.V., Merlin D.;
RT "ADAM-15/metargidin mediates homotypic aggregation of human T lymphocytes
RT and heterotypic interactions of T lymphocytes with intestinal epithelial
RT cells.";
RL J. Biol. Chem. 282:16948-16958(2007).
RN [23]
RP FUNCTION.
RX PubMed=18387333; DOI=10.1016/j.biocel.2008.02.021;
RA Chen Q., Meng L.H., Zhu C.H., Lin L.P., Lu H., Ding J.;
RT "ADAM15 suppresses cell motility by driving integrin alpha5beta1 cell
RT surface expression via Erk inactivation.";
RL Int. J. Biochem. Cell Biol. 40:2164-2173(2008).
RN [24]
RP FUNCTION.
RX PubMed=18434311; DOI=10.1074/jbc.m801329200;
RA Najy A.J., Day K.C., Day M.L.;
RT "The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor
RT activation.";
RL J. Biol. Chem. 283:18393-18401(2008).
RN [25]
RP ACTIVITY REGULATION.
RX PubMed=19207106; DOI=10.1042/bj20082127;
RA Maretzky T., Yang G., Ouerfelli O., Overall C.M., Worpenberg S.,
RA Hassiepen U., Eder J., Blobel C.P.;
RT "Characterization of the catalytic activity of the membrane-anchored
RT metalloproteinase ADAM15 in cell-based assays.";
RL Biochem. J. 420:105-113(2009).
RN [26]
RP INTERACTION WITH HCK; ITSN1; ITSN2; LYN; NCF1; NEPHROCYSTIN; SH3PXD2A;
RP SNX33; SNX9 AND SRC.
RX PubMed=19718658; DOI=10.1002/jcb.22317;
RA Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.;
RT "Alternative splicing of ADAM15 regulates its interactions with cellular
RT SH3 proteins.";
RL J. Cell. Biochem. 108:877-885(2009).
CC -!- FUNCTION: Active metalloproteinase with gelatinolytic and
CC collagenolytic activity. Plays a role in the wound healing process.
CC Mediates both heterotypic intraepithelial cell/T-cell interactions and
CC homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell
CC adhesion and migration of airway smooth muscle cells. Suppresses cell
CC motility on or towards fibronectin possibly by driving alpha-v/beta-1
CC integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation.
CC Cleaves E-cadherin in response to growth factor deprivation. Plays a
CC role in glomerular cell migration. Plays a role in pathological
CC neovascularization. May play a role in cartilage remodeling. May be
CC proteolytically processed, during sperm epididymal maturation and the
CC acrosome reaction. May play a role in sperm-egg binding through its
CC disintegrin domain. {ECO:0000269|PubMed:12091380,
CC ECO:0000269|PubMed:15358598, ECO:0000269|PubMed:15818704,
CC ECO:0000269|PubMed:17416588, ECO:0000269|PubMed:17575078,
CC ECO:0000269|PubMed:18387333, ECO:0000269|PubMed:18434311}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by hydroxamate-type metalloproteinase
CC inhibitors such as marimastat. Inhibited by metalloproteinase inhibitor
CC 2 (TIMP-2) and TIMP-3 at nanomolar concentrations. Not significantly
CC inhibited by TIMP-1 at concentrations of up to 100 nM. Not activated by
CC PMA or ionomycin. {ECO:0000269|PubMed:19207106}.
CC -!- SUBUNIT: Interacts with ITAGV-ITGB3 (vitronectin receptor). Interacts
CC with SH3GL2 and SNX9; this interaction occurs preferentially with
CC ADAM15 precursor, rather than the processed form, suggesting it occurs
CC in a secretory pathway compartment prior to the medial Golgi. Interacts
CC with ITAG9-ITGB1 (By similarity). Interacts specifically with Src
CC family protein-tyrosine kinases (PTKs). Interacts with SH3PXD2A.
CC Interacts with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2,
CC LYN, MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC.
CC {ECO:0000250, ECO:0000269|PubMed:10531379, ECO:0000269|PubMed:11741929,
CC ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:18296648,
CC ECO:0000269|PubMed:19718658, ECO:0000269|PubMed:9516430,
CC ECO:0000269|PubMed:9914169}.
CC -!- INTERACTION:
CC Q13444; Q8N9N5: BANP; NbExp=3; IntAct=EBI-77818, EBI-744695;
CC Q13444; Q06187: BTK; NbExp=2; IntAct=EBI-77818, EBI-624835;
CC Q13444; Q13643: FHL3; NbExp=3; IntAct=EBI-77818, EBI-741101;
CC Q13444; P06241: FYN; NbExp=2; IntAct=EBI-77818, EBI-515315;
CC Q13444; P62993: GRB2; NbExp=4; IntAct=EBI-77818, EBI-401755;
CC Q13444; P08631: HCK; NbExp=4; IntAct=EBI-77818, EBI-346340;
CC Q13444; P06239: LCK; NbExp=4; IntAct=EBI-77818, EBI-1348;
CC Q13444; P07948: LYN; NbExp=2; IntAct=EBI-77818, EBI-79452;
CC Q13444; O15259: NPHP1; NbExp=4; IntAct=EBI-77818, EBI-953828;
CC Q13444; P37198: NUP62; NbExp=3; IntAct=EBI-77818, EBI-347978;
CC Q13444; Q92882: OSTF1; NbExp=2; IntAct=EBI-77818, EBI-1051152;
CC Q13444; Q9UKS6: PACSIN3; NbExp=3; IntAct=EBI-77818, EBI-77926;
CC Q13444; Q93062: RBPMS; NbExp=3; IntAct=EBI-77818, EBI-740322;
CC Q13444; Q99962: SH3GL2; NbExp=2; IntAct=EBI-77818, EBI-77938;
CC Q13444; Q5TCZ1: SH3PXD2A; NbExp=4; IntAct=EBI-77818, EBI-2483234;
CC Q13444; Q8WV41: SNX33; NbExp=4; IntAct=EBI-77818, EBI-2481535;
CC Q13444; Q9Y5X1: SNX9; NbExp=4; IntAct=EBI-77818, EBI-77848;
CC Q13444; Q02446: SP4; NbExp=3; IntAct=EBI-77818, EBI-10198587;
CC Q13444; P12931: SRC; NbExp=4; IntAct=EBI-77818, EBI-621482;
CC Q13444-2; P54253: ATXN1; NbExp=3; IntAct=EBI-12137265, EBI-930964;
CC Q13444-2; A1E959: ODAM; NbExp=3; IntAct=EBI-12137265, EBI-5774125;
CC Q13444-2; Q8WV41: SNX33; NbExp=3; IntAct=EBI-12137265, EBI-2481535;
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:12243749}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12243749}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:12243749}. Cell projection, cilium, flagellum
CC {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250}. Note=The majority of the protein is localized in a
CC perinuclear compartment which may correspond to the trans-Golgi network
CC or the late endosome. The pro-protein is the major detectable form on
CC the cell surface, whereas the majority of the protein in the cell is
CC processed (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Name=1; Synonyms=6b;
CC IsoId=Q13444-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13444-2; Sequence=VSP_039527;
CC Name=3; Synonyms=6a;
CC IsoId=Q13444-3; Sequence=VSP_039529;
CC Name=4; Synonyms=4a;
CC IsoId=Q13444-4; Sequence=VSP_039531;
CC Name=5;
CC IsoId=Q13444-5; Sequence=VSP_039528;
CC Name=6; Synonyms=7b;
CC IsoId=Q13444-6; Sequence=VSP_039533;
CC Name=7; Synonyms=7a;
CC IsoId=Q13444-7; Sequence=VSP_039529, VSP_039533;
CC Name=8;
CC IsoId=Q13444-8; Sequence=VSP_039528, VSP_039533;
CC Name=9; Synonyms=3a;
CC IsoId=Q13444-9; Sequence=VSP_039526, VSP_039532;
CC Name=10; Synonyms=1;
CC IsoId=Q13444-10; Sequence=VSP_039525, VSP_039530;
CC Name=11;
CC IsoId=Q13444-11; Sequence=VSP_039524, VSP_039527;
CC Name=12;
CC IsoId=Q13444-12; Sequence=VSP_044695, VSP_039527;
CC Name=13;
CC IsoId=Q13444-13; Sequence=VSP_055143, VSP_055144, VSP_055145;
CC -!- TISSUE SPECIFICITY: Expressed in colon and small intestine. Expressed
CC in airway smooth muscle and glomerular mesangial cells (at protein
CC level). Ubiquitously expressed. Overexpressed in atherosclerotic
CC lesions. Constitutively expressed in cultured endothelium and smooth
CC muscle. Expressed in chondrocytes. Expressed in airway smooth muscle
CC and glomerular mesangial cells. {ECO:0000269|PubMed:12091380,
CC ECO:0000269|PubMed:15358598, ECO:0000269|PubMed:17575078,
CC ECO:0000269|PubMed:9016778}.
CC -!- DOMAIN: The cytoplasmic domain is required for SH3GL2- and SNX9-
CC binding.
CC -!- DOMAIN: Disintegrin domain binds to integrin alphaV-beta3.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC -!- PTM: Phosphorylation increases association with PTKs.
CC {ECO:0000269|PubMed:11741929}.
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DR EMBL; U41767; AAC50404.1; -; mRNA.
DR EMBL; U46005; AAC51112.1; -; mRNA.
DR EMBL; AY518542; AAR99331.1; -; mRNA.
DR EMBL; AF314227; AAM44189.1; -; Genomic_DNA.
DR EMBL; AF314227; AAS48590.1; -; Genomic_DNA.
DR EMBL; AF314227; AAS48591.1; -; Genomic_DNA.
DR EMBL; AF314227; AAS48592.1; -; Genomic_DNA.
DR EMBL; AF314227; AAS48593.1; -; Genomic_DNA.
DR EMBL; AF314227; AAS48594.1; -; Genomic_DNA.
DR EMBL; AF314227; AAS48595.1; -; Genomic_DNA.
DR EMBL; AF314227; AAS48596.1; -; Genomic_DNA.
DR EMBL; AF314227; AAS48597.1; -; Genomic_DNA.
DR EMBL; AF314227; AAS72298.1; -; Genomic_DNA.
DR EMBL; AY560593; AAS72991.1; -; mRNA.
DR EMBL; AY560594; AAS72992.1; -; mRNA.
DR EMBL; AY560595; AAS72993.1; -; mRNA.
DR EMBL; AY560596; AAS72994.1; -; mRNA.
DR EMBL; AY560597; AAS72995.1; -; mRNA.
DR EMBL; AY560598; AAS72996.1; -; mRNA.
DR EMBL; AY560599; AAS72997.1; -; mRNA.
DR EMBL; AY560600; AAS72998.1; -; mRNA.
DR EMBL; AY560601; AAS72999.1; -; mRNA.
DR EMBL; AY576417; AAS73000.1; -; mRNA.
DR EMBL; BT009764; AAP88766.1; -; mRNA.
DR EMBL; AK296925; BAG59477.1; -; mRNA.
DR EMBL; AK297468; BAG59890.1; -; mRNA.
DR EMBL; AK075498; BAG52157.1; -; mRNA.
DR EMBL; AL451085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014566; AAH14566.1; -; mRNA.
DR CCDS; CCDS1084.1; -. [Q13444-2]
DR CCDS; CCDS1085.1; -. [Q13444-4]
DR CCDS; CCDS1086.1; -. [Q13444-5]
DR CCDS; CCDS1087.1; -. [Q13444-1]
DR CCDS; CCDS1088.1; -. [Q13444-10]
DR CCDS; CCDS44236.1; -. [Q13444-3]
DR CCDS; CCDS58031.1; -. [Q13444-12]
DR CCDS; CCDS58032.1; -. [Q13444-9]
DR CCDS; CCDS60282.1; -. [Q13444-13]
DR PIR; G02390; G02390.
DR RefSeq; NP_001248393.1; NM_001261464.1. [Q13444-12]
DR RefSeq; NP_001248394.1; NM_001261465.1. [Q13444-9]
DR RefSeq; NP_001248395.1; NM_001261466.1. [Q13444-13]
DR RefSeq; NP_003806.3; NM_003815.4. [Q13444-2]
DR RefSeq; NP_997074.1; NM_207191.2. [Q13444-10]
DR RefSeq; NP_997077.1; NM_207194.2. [Q13444-4]
DR RefSeq; NP_997078.1; NM_207195.2. [Q13444-5]
DR RefSeq; NP_997079.1; NM_207196.2. [Q13444-3]
DR RefSeq; NP_997080.1; NM_207197.2. [Q13444-1]
DR AlphaFoldDB; Q13444; -.
DR SMR; Q13444; -.
DR BioGRID; 114287; 92.
DR CORUM; Q13444; -.
DR ELM; Q13444; -.
DR IntAct; Q13444; 48.
DR MINT; Q13444; -.
DR STRING; 9606.ENSP00000349436; -.
DR ChEMBL; CHEMBL2331050; -.
DR MEROPS; M12.215; -.
DR GlyConnect; 1179; 22 N-Linked glycans (2 sites).
DR GlyGen; Q13444; 5 sites, 21 N-linked glycans (2 sites).
DR iPTMnet; Q13444; -.
DR PhosphoSitePlus; Q13444; -.
DR BioMuta; ADAM15; -.
DR DMDM; 300669614; -.
DR EPD; Q13444; -.
DR jPOST; Q13444; -.
DR MassIVE; Q13444; -.
DR MaxQB; Q13444; -.
DR PaxDb; Q13444; -.
DR PeptideAtlas; Q13444; -.
DR PRIDE; Q13444; -.
DR ProteomicsDB; 22321; -.
DR ProteomicsDB; 59442; -. [Q13444-1]
DR ProteomicsDB; 59443; -. [Q13444-10]
DR ProteomicsDB; 59444; -. [Q13444-11]
DR ProteomicsDB; 59445; -. [Q13444-2]
DR ProteomicsDB; 59446; -. [Q13444-3]
DR ProteomicsDB; 59447; -. [Q13444-4]
DR ProteomicsDB; 59448; -. [Q13444-5]
DR ProteomicsDB; 59449; -. [Q13444-6]
DR ProteomicsDB; 59450; -. [Q13444-7]
DR ProteomicsDB; 59451; -. [Q13444-8]
DR ProteomicsDB; 59452; -. [Q13444-9]
DR ABCD; Q13444; 1 sequenced antibody.
DR Antibodypedia; 2491; 447 antibodies from 37 providers.
DR DNASU; 8751; -.
DR Ensembl; ENST00000271836.10; ENSP00000271836.6; ENSG00000143537.14. [Q13444-2]
DR Ensembl; ENST00000355956.6; ENSP00000348227.2; ENSG00000143537.14. [Q13444-4]
DR Ensembl; ENST00000356955.7; ENSP00000349436.2; ENSG00000143537.14. [Q13444-1]
DR Ensembl; ENST00000359280.8; ENSP00000352226.4; ENSG00000143537.14. [Q13444-5]
DR Ensembl; ENST00000360674.8; ENSP00000353892.4; ENSG00000143537.14. [Q13444-10]
DR Ensembl; ENST00000368412.7; ENSP00000357397.3; ENSG00000143537.14. [Q13444-9]
DR Ensembl; ENST00000368413.5; ENSP00000357398.1; ENSG00000143537.14. [Q13444-11]
DR Ensembl; ENST00000447332.3; ENSP00000476000.1; ENSG00000143537.14. [Q13444-13]
DR Ensembl; ENST00000449910.6; ENSP00000403843.2; ENSG00000143537.14. [Q13444-3]
DR Ensembl; ENST00000526491.5; ENSP00000432347.1; ENSG00000143537.14. [Q13444-6]
DR Ensembl; ENST00000529473.5; ENSP00000434227.1; ENSG00000143537.14. [Q13444-8]
DR Ensembl; ENST00000531455.5; ENSP00000432927.1; ENSG00000143537.14. [Q13444-12]
DR GeneID; 8751; -.
DR KEGG; hsa:8751; -.
DR MANE-Select; ENST00000356955.7; ENSP00000349436.2; NM_207197.3; NP_997080.1.
DR UCSC; uc001fgr.3; human. [Q13444-1]
DR CTD; 8751; -.
DR DisGeNET; 8751; -.
DR GeneCards; ADAM15; -.
DR HGNC; HGNC:193; ADAM15.
DR HPA; ENSG00000143537; Low tissue specificity.
DR MIM; 605548; gene.
DR neXtProt; NX_Q13444; -.
DR OpenTargets; ENSG00000143537; -.
DR PharmGKB; PA24510; -.
DR VEuPathDB; HostDB:ENSG00000143537; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000159822; -.
DR HOGENOM; CLU_012714_7_2_1; -.
DR InParanoid; Q13444; -.
DR OMA; VCAAGHC; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q13444; -.
DR TreeFam; TF314733; -.
DR BRENDA; 3.4.24.B28; 2681.
DR PathwayCommons; Q13444; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-8941237; Invadopodia formation.
DR SignaLink; Q13444; -.
DR SIGNOR; Q13444; -.
DR BioGRID-ORCS; 8751; 6 hits in 1070 CRISPR screens.
DR ChiTaRS; ADAM15; human.
DR GeneWiki; ADAM15; -.
DR GenomeRNAi; 8751; -.
DR Pharos; Q13444; Tbio.
DR PRO; PR:Q13444; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13444; protein.
DR Bgee; ENSG00000143537; Expressed in lower esophagus mucosa and 122 other tissues.
DR Genevisible; Q13444; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005178; F:integrin binding; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IDA:UniProtKB.
DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR GO; GO:0002418; P:immune response to tumor cell; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:1900121; P:negative regulation of receptor binding; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:1990910; P:response to hypobaric hypoxia; IEA:Ensembl.
DR GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR033605; ADAM15.
DR InterPro; IPR006586; ADAM_Cys-rich.
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 PANTHER; PTHR11905:SF130; PTHR11905:SF130; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Cell adhesion; Cell junction;
KW Cell projection; Cilium; Cleavage on pair of basic residues;
KW Collagen degradation; Cytoplasmic vesicle; Disulfide bond; EGF-like domain;
KW Flagellum; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Reference proteome; SH3-binding;
KW Signal; Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..206
FT /evidence="ECO:0000250"
FT /id="PRO_0000029082"
FT CHAIN 207..863
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 15"
FT /id="PRO_0000029083"
FT TOPO_DOM 207..696
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..863
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 213..414
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 421..508
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 657..685
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 177..184
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT MOTIF 484..486
FT /note="Cell attachment site"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 815..821
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 850..856
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 809..825
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..863
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 715
FT /note="Phosphotyrosine; by HCK and LCK"
FT /evidence="ECO:0000269|PubMed:11741929"
FT MOD_RES 735
FT /note="Phosphotyrosine; by HCK and LCK"
FT /evidence="ECO:0000269|PubMed:11741929"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 323..409
FT /evidence="ECO:0000250"
FT DISULFID 365..393
FT /evidence="ECO:0000250"
FT DISULFID 367..376
FT /evidence="ECO:0000250"
FT DISULFID 480..500
FT /evidence="ECO:0000250"
FT DISULFID 657..667
FT /evidence="ECO:0000250"
FT DISULFID 661..673
FT /evidence="ECO:0000250"
FT DISULFID 675..684
FT /evidence="ECO:0000250"
FT VAR_SEQ 26
FT /note="I -> IVLSWGVLGPA (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044695"
FT VAR_SEQ 27..87
FT /note="GGTEEQQAESEKAPREPLEPQVLQDDLPISLKKVLQTSLPEPLRIKLELDGD
FT SHILELLQN -> VSACNVEAPQVALRSSRQSQRRPRGSPWSPRSFRTISQLASKRCF
FT (in isoform 13)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055143"
FT VAR_SEQ 94..387
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_039524"
FT VAR_SEQ 641..649
FT /note="CIDHRCQRV -> SSLGGQDQV (in isoform 13)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055144"
FT VAR_SEQ 650..863
FT /note="Missing (in isoform 13)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055145"
FT VAR_SEQ 736..772
FT /note="RAAQSGPSERPGPPQRALLARGTKQASALSFPAPPSR -> SLRGQPSPHPQ
FT GSHCLPTPRAGAHRVTCPAQGLESRP (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:15358598,
FT ECO:0000303|PubMed:18296648, ECO:0000303|Ref.6"
FT /id="VSP_039525"
FT VAR_SEQ 737..796
FT /note="AAQSGPSERPGPPQRALLARGTKQASALSFPAPPSRPLPPDPVSKRLQAELA
FT DRPNPPTR -> LVLSASRPPLPGRCRLTLCPRDSSLRGQPSPHPQGSHCLPTPRAGAH
FT RVTCPAQGLESRP (in isoform 9)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_039526"
FT VAR_SEQ 760..808
FT /note="Missing (in isoform 2, isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16303743,
FT ECO:0000303|PubMed:18296648, ECO:0000303|PubMed:8617717,
FT ECO:0000303|PubMed:9039960, ECO:0000303|Ref.6,
FT ECO:0000303|Ref.7"
FT /id="VSP_039527"
FT VAR_SEQ 760..784
FT /note="Missing (in isoform 5 and isoform 8)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_039528"
FT VAR_SEQ 760
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_039529"
FT VAR_SEQ 773..863
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:15358598,
FT ECO:0000303|PubMed:18296648, ECO:0000303|Ref.6"
FT /id="VSP_039530"
FT VAR_SEQ 785..808
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:18296648, ECO:0000303|Ref.6"
FT /id="VSP_039531"
FT VAR_SEQ 797..863
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_039532"
FT VAR_SEQ 809..863
FT /note="SQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSS
FT LYL -> VTVGGEKGTASPPT (in isoform 6, isoform 7 and isoform
FT 8)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_039533"
FT VARIANT 191
FT /note="K -> T (in dbSNP:rs6427128)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17937806,
FT ECO:0000269|PubMed:8617717, ECO:0000269|PubMed:9039960,
FT ECO:0000269|Ref.6, ECO:0000269|Ref.7"
FT /id="VAR_060315"
FT VARIANT 216
FT /note="E -> K (in dbSNP:rs115753757)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_068970"
FT VARIANT 294
FT /note="P -> H (in dbSNP:rs2306122)"
FT /id="VAR_060316"
FT MUTAGEN 484..485
FT /note="RG->SV: Reduces ADAM15-mediated T-cell aggregation."
FT /evidence="ECO:0000269|PubMed:17416588"
FT CONFLICT 81
FT /note="I -> V (in Ref. 9; BAG52157)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="G -> C (in Ref. 8; BAG59890)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="K -> T (in Ref. 8; BAG59890)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="H -> Y (in Ref. 8; BAG59477)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="V -> A (in Ref. 9; BAG52157)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="S -> G (in Ref. 2; AAC50404)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="A -> P (in Ref. 1; AAC51112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 863 AA; 92959 MW; 004936E9182629CA CRC64;
MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV
LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ
GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA
LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL
EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS
AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL
PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM
AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC
RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ
PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW
ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK
CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR
LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKQ ASALSFPAPP SRPLPPDPVS
KRLQAELADR PNPPTRPLPA DPVVRSPKSQ GPAKPPPPRK PLPADPQGRC PSGDLPGPGA
GIPPLVVPSR PAPPPPTVSS LYL
