GenomeNet

Database: UniProt
Entry: O88839
LinkDB: O88839
Original site: O88839 
ID   ADA15_MOUSE             Reviewed;         864 AA.
AC   O88839; A4ZYV2; Q3TDN7; Q3U7C2; Q3UE21; Q8C7Z0; Q91VS9; Q9QYL2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2003, sequence version 2.
DT   13-FEB-2019, entry version 192.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 15;
DE            Short=ADAM 15;
DE            EC=3.4.24.-;
DE   AltName: Full=AD56;
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND PROTEOLYTIC PROCESSING.
RC   TISSUE=Lung;
RX   PubMed=9748307; DOI=10.1074/jbc.273.40.26236;
RA   Lum L., Reid M.S., Blobel C.P.;
RT   "Intracellular maturation of the mouse metalloprotease disintegrin
RT   MDC15.";
RL   J. Biol. Chem. 273:26236-26247(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Myeloid, and Myeloma;
RX   PubMed=13679040; DOI=10.1016/j.bbrc.2003.08.070;
RA   Shimizu E., Yasui A., Matsuura K., Hijiya N., Higuchi Y., Yamamoto S.;
RT   "Structure and expression of the murine ADAM 15 gene and its splice
RT   variants, and difference of interaction between their cytoplasmic
RT   domains and Src family proteins.";
RL   Biochem. Biophys. Res. Commun. 309:779-785(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow macrophage, Cerebellum, and Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Mammary gland;
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 207-694 (ISOFORMS 1/2/3), FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=18390692; DOI=10.1530/REP-07-0300;
RA   Pasten-Hidalgo K., Hernandez-Rivas R., Roa-Espitia A.L.,
RA   Sanchez-Gutierrez M., Martinez-Perez F., Monrroy A.O.,
RA   Hernandez-Gonzalez E.O., Mujica A.;
RT   "Presence, processing, and localization of mouse ADAM15 during sperm
RT   maturation and the role of its disintegrin domain during sperm-egg
RT   binding.";
RL   Reproduction 136:41-51(2008).
RN   [6]
RP   INTERACTION WITH ENDOPHILIN I 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
RT   two SH3 domain-containing proteins, endophilin I and SH3PX1.";
RL   J. Biol. Chem. 274:31693-31699(1999).
RN   [7]
RP   FUNCTION, INTERACTION WITH INTEGRIN ALPHAV-BETA3 AND ALPHA9-BETA1, AND
RP   MUTAGENESIS OF ARG-482; ASP-489; LEU-490; PRO-491; GLU-492 AND
RP   PHE-493.
RX   PubMed=11882657; DOI=10.1074/jbc.M200086200;
RA   Eto K., Huet C., Tarui T., Kupriyanov S., Liu H.Z.,
RA   Puzon-McLaughlin W., Zhang X.P., Sheppard D., Engvall E., Takada Y.;
RT   "Functional classification of ADAMs based on a conserved motif for
RT   binding to integrin alpha 9beta 1: implications for sperm-egg binding
RT   and other cell interactions.";
RL   J. Biol. Chem. 277:17804-17810(2002).
RN   [8]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=12897135; DOI=10.1128/MCB.23.16.5614-5624.2003;
RA   Horiuchi K., Weskamp G., Lum L., Hammes H.P., Cai H., Brodie T.A.,
RA   Ludwig T., Chiusaroli R., Baron R., Preissner K.T., Manova K.,
RA   Blobel C.P.;
RT   "Potential role for ADAM15 in pathological neovascularization in
RT   mice.";
RL   Mol. Cell. Biol. 23:5614-5624(2003).
RN   [9]
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   [10]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=18381816; DOI=10.1096/fj.07-099283;
RA   Xie B., Shen J., Dong A., Swaim M., Hackett S.F., Wyder L.,
RA   Worpenberg S., Barbieri S., Campochiaro P.A.;
RT   "An Adam15 amplification loop promotes vascular endothelial growth
RT   factor-induced ocular neovascularization.";
RL   FASEB J. 22:2775-2783(2008).
CC   -!- FUNCTION: Active metalloproteinase with gelatinolytic and
CC       collagenolytic activity. Plays a role in the wound healing
CC       process. Mediates both heterotypic intraepithelial cell/T-cell
CC       interactions and homotypic T-cell aggregation. Inhibits beta-1
CC       integrin-mediated cell adhesion and migration of airway smooth
CC       muscle cells. Suppresses cell motility on or towards fibronectin
CC       possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell
CC       surface expression via ERK1/2 inactivation. Cleaves E-cadherin in
CC       response to growth factor deprivation. Plays a role in glomerular
CC       cell migration (By similarity). Plays a role in pathological
CC       neovascularization. May play a role in cartilage remodeling. May
CC       be proteolytically processed, during sperm epididymal maturation
CC       and the acrosome reaction. May play a role in sperm-egg binding
CC       through its disintegrin domain. Interactions with egg membrane
CC       could be mediated via binding between the disintegrin-like domain
CC       to one or more integrin receptors on the egg. {ECO:0000250,
CC       ECO:0000269|PubMed:11882657, ECO:0000269|PubMed:12897135,
CC       ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:18390692}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SUBUNIT: Interacts specifically with Src family protein-tyrosine
CC       kinases (PTKs) (By similarity). Interacts with ITAGV-ITGB3
CC       (vitronectin receptor). Interacts with SH3GL2 and SNX9; this
CC       interaction occurs preferentially with ADAM15 precursor, rather
CC       than the processed form, suggesting it occurs in a secretory
CC       pathway compartment prior to the medial Golgi. Interacts with
CC       ITAG9-ITGB1. Interacts with SH3PXD2A (By similarity). Interacts
CC       with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN,
CC       MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000269|PubMed:18390692}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:18390692}. Cell junction, adherens junction
CC       {ECO:0000250}. Cell projection, cilium, flagellum
CC       {ECO:0000269|PubMed:18390692}. Cytoplasmic vesicle, secretory
CC       vesicle, acrosome {ECO:0000269|PubMed:18390692}. Note=The majority
CC       of the protein is localized in a perinuclear compartment which may
CC       correspond to the trans-Golgi network or the late endosome. The
CC       pro-protein is the major detectable form on the cell surface,
CC       whereas the majority of the protein in the cell is processed.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=ADAM15v2;
CC         IsoId=O88839-1; Sequence=Displayed;
CC       Name=2; Synonyms=ADAM15v1;
CC         IsoId=O88839-2; Sequence=VSP_008880;
CC       Name=3; Synonyms=ADAM15;
CC         IsoId=O88839-3; Sequence=VSP_008881;
CC       Name=4;
CC         IsoId=O88839-4; Sequence=VSP_008879;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed moderately in pericytes of retina.
CC       Expressed in testis and in spermatozoa from the caput, corpus, and
CC       cauda epididymis, as well as in non-capacitated and acrosome-
CC       reacted sperm (at protein level). Highly expressed in heart,
CC       brain, lung, and kidney. Expressed at lower levels in spleen,
CC       liver, testis and muscle. {ECO:0000269|PubMed:18381816,
CC       ECO:0000269|PubMed:18390692}.
CC   -!- DEVELOPMENTAL STAGE: At 13.5 dpc, strongly expressed in the
CC       developing vasculature of the endocardium. At P17, expressed
CC       throughout the retina (at protein level). At 9.5 dpc and
CC       thereafter, prominently expressed in the vasculature, including in
CC       ventral and dorsal aorta and the caudal artery. In developing
CC       heart, detected in endocardium and blood vessels of the ventricle,
CC       bulbus arteriosus, and atrium. Also highly expressed in
CC       hypertrophic cells of the developing bone. In adult, expressed
CC       prominently in brain, including in hippocampus, cerebellum, pons,
CC       thalamus, cortex, and olfactory bulb.
CC       {ECO:0000269|PubMed:12897135, ECO:0000269|PubMed:18381816}.
CC   -!- INDUCTION: By hypoxic stimulus in retina (at protein level). Up-
CC       regulated by VEGF in retina. {ECO:0000269|PubMed:12897135,
CC       ECO:0000269|PubMed:18381816}.
CC   -!- DOMAIN: The cytoplasmic domain is required for SH3GL2- and SNX9-
CC       binding.
CC   -!- DOMAIN: Disintegrin domain binds to integrin alphaV-beta3.
CC       {ECO:0000250}.
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. An
CC       additional membrane proximal site of cleavage affects a small
CC       percentage of the proteins and results in disulfide-linked
CC       fragments. The prodomain is apparently cleaved in several
CC       positions that are N-terminal of the furin cleavage site.
CC       {ECO:0000269|PubMed:9748307}.
CC   -!- PTM: May be partially sialylated.
CC   -!- PTM: Phosphorylation increases association with PTKs.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Mice targeted for deletion of the first 27 amino
CC       acids of the ADAM15 N-terminal sequence are viable and fertile,
CC       showing no major developmental defects and displaying normal
CC       mortality or morbidity. These mutant mice, however, exhibit
CC       significantly reduced ischemia-induced retinal neovascularization,
CC       choroidal neovascularization at rupture sites in Bruch's membrane,
CC       and VEGF-induced subretinal neovascularization, and develop
CC       significantly smaller tumors following implantation of B16F0
CC       melanoma cells. Aging mutant mice exhibit accelerated development
CC       of osteoarthritic lesions in knee joints.
DR   EMBL; AF006196; AAC61896.1; -; mRNA.
DR   EMBL; AB022089; BAA88903.1; -; Genomic_DNA.
DR   EMBL; AK048901; BAC33485.1; -; mRNA.
DR   EMBL; AK149796; BAE29090.1; -; mRNA.
DR   EMBL; AK151804; BAE30703.1; -; mRNA.
DR   EMBL; AK152725; BAE31447.1; -; mRNA.
DR   EMBL; AK170101; BAE41564.1; -; mRNA.
DR   EMBL; BC009132; AAH09132.1; -; mRNA.
DR   EMBL; EF506571; ABP73662.1; -; mRNA.
DR   CCDS; CCDS17502.1; -. [O88839-1]
DR   CCDS; CCDS17503.1; -. [O88839-3]
DR   RefSeq; NP_001032811.2; NM_001037722.3. [O88839-1]
DR   RefSeq; NP_033744.1; NM_009614.3. [O88839-3]
DR   RefSeq; XP_006500981.1; XM_006500918.1. [O88839-2]
DR   UniGene; Mm.274049; -.
DR   UniGene; Mm.470104; -.
DR   ProteinModelPortal; O88839; -.
DR   SMR; O88839; -.
DR   IntAct; O88839; 3.
DR   MINT; O88839; -.
DR   STRING; 10090.ENSMUSP00000029676; -.
DR   MEROPS; M12.215; -.
DR   iPTMnet; O88839; -.
DR   PhosphoSitePlus; O88839; -.
DR   SwissPalm; O88839; -.
DR   MaxQB; O88839; -.
DR   PaxDb; O88839; -.
DR   PeptideAtlas; O88839; -.
DR   PRIDE; O88839; -.
DR   Ensembl; ENSMUST00000029676; ENSMUSP00000029676; ENSMUSG00000028041. [O88839-1]
DR   Ensembl; ENSMUST00000074582; ENSMUSP00000074167; ENSMUSG00000028041. [O88839-3]
DR   Ensembl; ENSMUST00000107446; ENSMUSP00000103070; ENSMUSG00000028041. [O88839-4]
DR   Ensembl; ENSMUST00000107448; ENSMUSP00000103072; ENSMUSG00000028041. [O88839-2]
DR   Ensembl; ENSMUST00000184651; ENSMUSP00000139147; ENSMUSG00000028041. [O88839-1]
DR   GeneID; 11490; -.
DR   KEGG; mmu:11490; -.
DR   UCSC; uc008pyv.1; mouse. [O88839-1]
DR   UCSC; uc008pyw.1; mouse. [O88839-3]
DR   CTD; 8751; -.
DR   MGI; MGI:1333882; Adam15.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000159822; -.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; O88839; -.
DR   KO; K06836; -.
DR   OMA; ADHQEFL; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; O88839; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-MMU-8941237; Invadopodia formation.
DR   PRO; PR:O88839; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000028041; Expressed in 240 organ(s), highest expression level in bone marrow macrophage.
DR   Genevisible; O88839; MM.
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; ISO:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
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:0005178; F:integrin binding; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; ISO:MGI.
DR   GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0002418; P:immune response to tumor cell; ISO:MGI.
DR   GO; GO:0045087; P:innate immune response; ISO:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
DR   GO; GO:1900121; P:negative regulation of receptor binding; ISO:MGI.
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; IPR013032; EGF-like_CS.
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; Complete proteome; Cytoplasmic vesicle;
KW   Disulfide bond; EGF-like domain; Flagellum; Glycoprotein; Hydrolase;
KW   Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW   Reference proteome; SH3-binding; Signal; Transmembrane;
KW   Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   PROPEP       18    207       {ECO:0000305}.
FT                                /FTId=PRO_0000029084.
FT   CHAIN       208    864       Disintegrin and metalloproteinase domain-
FT                                containing protein 15.
FT                                /FTId=PRO_0000029085.
FT   TOPO_DOM    208    696       Extracellular. {ECO:0000255}.
FT   TRANSMEM    697    717       Helical. {ECO:0000255}.
FT   TOPO_DOM    718    864       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      214    415       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      422    509       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      658    686       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   MOTIF       177    184       Cysteine switch. {ECO:0000250}.
FT   MOTIF       816    822       SH3-binding. {ECO:0000255}.
FT   MOTIF       851    857       SH3-binding. {ECO:0000255}.
FT   COMPBIAS    510    657       Cys-rich.
FT   COMPBIAS    699    712       Poly-Leu.
FT   ACT_SITE    350    350       {ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       179    179       Zinc; in inhibited form. {ECO:0000250}.
FT   METAL       349    349       Zinc; catalytic. {ECO:0000255}.
FT   METAL       353    353       Zinc; catalytic. {ECO:0000255}.
FT   METAL       359    359       Zinc; catalytic. {ECO:0000255}.
FT   SITE        289    290       Cleavage; by furin. {ECO:0000255}.
FT   MOD_RES     716    716       Phosphotyrosine; by HCK and LCK.
FT                                {ECO:0000250|UniProtKB:Q13444}.
FT   MOD_RES     736    736       Phosphotyrosine; by HCK and LCK.
FT                                {ECO:0000250|UniProtKB:Q13444}.
FT   CARBOHYD    238    238       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    390    390       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    393    393       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    607    607       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    612    612       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    324    410       {ECO:0000250}.
FT   DISULFID    366    394       {ECO:0000250}.
FT   DISULFID    368    377       {ECO:0000250}.
FT   DISULFID    481    501       {ECO:0000250}.
FT   DISULFID    658    668       {ECO:0000250}.
FT   DISULFID    662    674       {ECO:0000250}.
FT   DISULFID    676    685       {ECO:0000250}.
FT   VAR_SEQ     415    830       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_008879.
FT   VAR_SEQ     761    809       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072,
FT                                ECO:0000303|PubMed:9748307}.
FT                                /FTId=VSP_008881.
FT   VAR_SEQ     761    785       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_008880.
FT   MUTAGEN     482    482       R->A: Reduced binding to CHO cells
FT                                expressing ITAG9-ITGB1.
FT                                {ECO:0000269|PubMed:11882657}.
FT   MUTAGEN     489    489       D->A: Reduced binding to CHO cells
FT                                expressing ITAG9-ITGB1.
FT                                {ECO:0000269|PubMed:11882657}.
FT   MUTAGEN     490    490       L->A: Reduced binding to CHO cells
FT                                expressing ITAG9-ITGB1.
FT                                {ECO:0000269|PubMed:11882657}.
FT   MUTAGEN     491    491       P->A: Reduced binding to CHO cells
FT                                expressing ITAG9-ITGB1.
FT                                {ECO:0000269|PubMed:11882657}.
FT   MUTAGEN     492    492       E->A: Reduced binding to CHO cells
FT                                expressing ITAG9-ITGB1.
FT                                {ECO:0000269|PubMed:11882657}.
FT   MUTAGEN     493    493       F->A: Reduced binding to CHO cells
FT                                expressing ITAG9-ITGB1.
FT                                {ECO:0000269|PubMed:11882657}.
FT   CONFLICT     21     22       PP -> RR (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
FT   CONFLICT     51     51       Q -> H (in Ref. 3; BAE29090).
FT                                {ECO:0000305}.
FT   CONFLICT     73     73       S -> P (in Ref. 3; BAE41564).
FT                                {ECO:0000305}.
FT   CONFLICT    443    443       E -> Q (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
FT   CONFLICT    459    459       G -> E (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
FT   CONFLICT    564    565       SP -> T (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
FT   CONFLICT    654    654       G -> E (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
FT   CONFLICT    660    660       R -> S (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
FT   CONFLICT    703    703       L -> R (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
FT   CONFLICT    712    712       L -> R (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
FT   CONFLICT    729    729       L -> R (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
FT   CONFLICT    830    830       Q -> R (in Ref. 3; BAE41564).
FT                                {ECO:0000305}.
FT   CONFLICT    846    846       L -> S (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
FT   CONFLICT    852    854       PAP -> AAS (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
FT   CONFLICT    859    859       A -> P (in Ref. 2; BAA88903).
FT                                {ECO:0000305}.
SQ   SEQUENCE   864 AA;  92664 MW;  B1CBEB923463BB15 CRC64;
     MRLALLWALG LLGAGSPRPS PPLPNIGGTE EEQQASPERT LSGSMESRVV QDSPPMSLAD
     VLQTGLPEAL RISLELDSES HVLELLQNRD LIPGRPTLVW YQPDGTRMVS EGYSLENCCY
     RGRVQGHPSS WVSLCACSGI RGLIVLSPER GYTLELGPGD LQRPVISRIQ DHLLLGHTCA
     PSWHASVPTR AGPDLLLEQH HAHRLKRDVV TETKIVELVI VADNSEVRKY PDFQQLLNRT
     LEAALLLDTF FQPLNVRVAL VGLEAWTQHN LIEMSSNPAV LLDNFLRWRR TDLLPRLPHD
     SAQLVTVTSF SGPMVGMAIQ NSICSPDFSG GVNMDHSTSI LGVASSIAHE LGHSLGLDHD
     SPGHSCPCPG PAPAKSCIME ASTDFLPGLN FSNCSRQALE KALLEGMGSC LFERQPSLAP
     MSSLCGNMFV DPGEQCDCGF PDECTDPCCD HFTCQLRPGA QCASDGPCCQ NCKLHPAGWL
     CRPPTDDCDL PEFCPGDSSQ CPSDIRLGDG EPCASGEAVC MHGRCASYAR QCQSLWGPGA
     QPAAPLCLQT ANTRGNAFGS CGRSPGGSYM PCAPRDVMCG QLQCQWGRSQ PLLGSVQDRL
     SEVLEANGTQ LNCSWVDLDL GNDVAQPLLA LPGTACGPGL VCIGHRCQPV DLLGAQECRR
     KCHGHGVCDS SGHCRCEEGW APPDCMTQLK ATSSLTTGLL LSLLLLLVLV LLGASYWHRA
     RLHQRLCQLK GSSCQYRAPQ SCPPERPGPP QRAQQMTGTK QASVVSFPVP PSRPLPPNPV
     PKKLQAALAD RSNPPTRPLP ADPVVRRPKS QGPTKPPPPR KPLPANPQGQ HPPGDLPGPG
     DGSLPLVVPS RPAPPPPAAS SLYL
//
DBGET integrated database retrieval system