ADA15_MOUSE
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 03-AUG-2022, entry version 209.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 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 domains
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT 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 two
RT 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 PHE-493.
RX PubMed=11882657; DOI=10.1074/jbc.m200086200;
RA Eto K., Huet C., Tarui T., Kupriyanov S., Liu H.Z., Puzon-McLaughlin W.,
RA Zhang X.P., Sheppard D., Engvall E., Takada Y.;
RT "Functional classification of ADAMs based on a conserved motif for binding
RT to integrin alpha 9beta 1: implications for sperm-egg binding and other
RT 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., Blobel C.P.;
RT "Potential role for ADAM15 in pathological neovascularization in 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., Worpenberg S.,
RA Barbieri S., Campochiaro P.A.;
RT "An Adam15 amplification loop promotes vascular endothelial growth factor-
RT 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 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 (By similarity). Plays a role in
CC pathological neovascularization. May play a role in cartilage
CC remodeling. May be proteolytically processed, during sperm epididymal
CC maturation and the acrosome reaction. May play a role in sperm-egg
CC binding through its disintegrin domain. Interactions with egg membrane
CC could be mediated via binding between the disintegrin-like domain to
CC 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 (vitronectin
CC receptor). Interacts with SH3GL2 and SNX9; this interaction occurs
CC preferentially with ADAM15 precursor, rather than the processed form,
CC suggesting it occurs in a secretory pathway compartment prior to the
CC medial Golgi. Interacts with ITAG9-ITGB1. Interacts with SH3PXD2A (By
CC similarity). Interacts with ITAGV-ITGB1. Interacts with GRB2, HCK,
CC ITSN1, ITSN2, LYN, MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33,
CC LCK and SRC (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 vesicle,
CC acrosome {ECO:0000269|PubMed:18390692}. Note=The majority of the
CC protein is localized in a perinuclear compartment which may correspond
CC to the trans-Golgi network or the late endosome. The pro-protein is the
CC major detectable form on the cell surface, whereas the majority of the
CC 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 -!- 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-reacted
CC sperm (at protein level). Highly expressed in heart, brain, lung, and
CC kidney. Expressed at lower levels in spleen, liver, testis and muscle.
CC {ECO:0000269|PubMed:18381816, ECO:0000269|PubMed:18390692}.
CC -!- DEVELOPMENTAL STAGE: At 13.5 dpc, strongly expressed in the developing
CC vasculature of the endocardium. At P17, expressed throughout the retina
CC (at protein level). At 9.5 dpc and thereafter, prominently expressed in
CC the vasculature, including in ventral and dorsal aorta and the caudal
CC artery. In developing heart, detected in endocardium and blood vessels
CC of the ventricle, bulbus arteriosus, and atrium. Also highly expressed
CC in hypertrophic cells of the developing bone. In adult, expressed
CC prominently in brain, including in hippocampus, cerebellum, pons,
CC thalamus, cortex, and olfactory bulb. {ECO:0000269|PubMed:12897135,
CC 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 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. An additional
CC membrane proximal site of cleavage affects a small percentage of the
CC proteins and results in disulfide-linked fragments. The prodomain is
CC apparently cleaved in several positions that are N-terminal of the
CC furin cleavage site. {ECO:0000269|PubMed:9748307}.
CC -!- PTM: May be partially sialylated.
CC -!- PTM: Phosphorylation increases association with PTKs. {ECO:0000250}.
CC -!- MISCELLANEOUS: Mice targeted for deletion of the first 27 amino acids
CC of the ADAM15 N-terminal sequence are viable and fertile, showing no
CC major developmental defects and displaying normal mortality or
CC morbidity. These mutant mice, however, exhibit significantly reduced
CC ischemia-induced retinal neovascularization, choroidal
CC neovascularization at rupture sites in Bruch's membrane, and VEGF-
CC induced subretinal neovascularization, and develop significantly
CC smaller tumors following implantation of B16F0 melanoma cells. Aging
CC mutant mice exhibit accelerated development of osteoarthritic lesions
CC in knee joints.
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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 AlphaFoldDB; O88839; -.
DR SMR; O88839; -.
DR IntAct; O88839; 2.
DR STRING; 10090.ENSMUSP00000029676; -.
DR MEROPS; M12.215; -.
DR GlyGen; O88839; 5 sites.
DR iPTMnet; O88839; -.
DR PhosphoSitePlus; O88839; -.
DR SwissPalm; O88839; -.
DR MaxQB; O88839; -.
DR PaxDb; O88839; -.
DR PeptideAtlas; O88839; -.
DR PRIDE; O88839; -.
DR ProteomicsDB; 285603; -. [O88839-1]
DR ProteomicsDB; 285604; -. [O88839-2]
DR ProteomicsDB; 285605; -. [O88839-3]
DR ProteomicsDB; 285606; -. [O88839-4]
DR Antibodypedia; 2491; 447 antibodies from 37 providers.
DR DNASU; 11490; -.
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 VEuPathDB; HostDB:ENSMUSG00000028041; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000159822; -.
DR HOGENOM; CLU_012714_7_2_1; -.
DR InParanoid; O88839; -.
DR OMA; SNRKCHC; -.
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 BioGRID-ORCS; 11490; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Adam15; mouse.
DR PRO; PR:O88839; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O88839; protein.
DR Bgee; ENSMUSG00000028041; Expressed in granulocyte and 217 other tissues.
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: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..207
FT /evidence="ECO:0000305"
FT /id="PRO_0000029084"
FT CHAIN 208..864
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 15"
FT /id="PRO_0000029085"
FT TOPO_DOM 208..696
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..864
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 214..415
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 422..509
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 658..686
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 18..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 177..184
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT MOTIF 816..822
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 851..857
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 27..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..834
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..864
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
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 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT SITE 289..290
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000255"
FT MOD_RES 716
FT /note="Phosphotyrosine; by HCK and LCK"
FT /evidence="ECO:0000250|UniProtKB:Q13444"
FT MOD_RES 736
FT /note="Phosphotyrosine; by HCK and LCK"
FT /evidence="ECO:0000250|UniProtKB:Q13444"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 324..410
FT /evidence="ECO:0000250"
FT DISULFID 366..394
FT /evidence="ECO:0000250"
FT DISULFID 368..377
FT /evidence="ECO:0000250"
FT DISULFID 481..501
FT /evidence="ECO:0000250"
FT DISULFID 658..668
FT /evidence="ECO:0000250"
FT DISULFID 662..674
FT /evidence="ECO:0000250"
FT DISULFID 676..685
FT /evidence="ECO:0000250"
FT VAR_SEQ 415..830
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008879"
FT VAR_SEQ 761..809
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9748307"
FT /id="VSP_008881"
FT VAR_SEQ 761..785
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_008880"
FT MUTAGEN 482
FT /note="R->A: Reduced binding to CHO cells expressing ITAG9-
FT ITGB1."
FT /evidence="ECO:0000269|PubMed:11882657"
FT MUTAGEN 489
FT /note="D->A: Reduced binding to CHO cells expressing ITAG9-
FT ITGB1."
FT /evidence="ECO:0000269|PubMed:11882657"
FT MUTAGEN 490
FT /note="L->A: Reduced binding to CHO cells expressing ITAG9-
FT ITGB1."
FT /evidence="ECO:0000269|PubMed:11882657"
FT MUTAGEN 491
FT /note="P->A: Reduced binding to CHO cells expressing ITAG9-
FT ITGB1."
FT /evidence="ECO:0000269|PubMed:11882657"
FT MUTAGEN 492
FT /note="E->A: Reduced binding to CHO cells expressing ITAG9-
FT ITGB1."
FT /evidence="ECO:0000269|PubMed:11882657"
FT MUTAGEN 493
FT /note="F->A: Reduced binding to CHO cells expressing ITAG9-
FT ITGB1."
FT /evidence="ECO:0000269|PubMed:11882657"
FT CONFLICT 21..22
FT /note="PP -> RR (in Ref. 2; BAA88903)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="Q -> H (in Ref. 3; BAE29090)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="S -> P (in Ref. 3; BAE41564)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="E -> Q (in Ref. 2; BAA88903)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="G -> E (in Ref. 2; BAA88903)"
FT /evidence="ECO:0000305"
FT CONFLICT 564..565
FT /note="SP -> T (in Ref. 2; BAA88903)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="G -> E (in Ref. 2; BAA88903)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="R -> S (in Ref. 2; BAA88903)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="L -> R (in Ref. 2; BAA88903)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="L -> R (in Ref. 2; BAA88903)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="L -> R (in Ref. 2; BAA88903)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="Q -> R (in Ref. 3; BAE41564)"
FT /evidence="ECO:0000305"
FT CONFLICT 846
FT /note="L -> S (in Ref. 2; BAA88903)"
FT /evidence="ECO:0000305"
FT CONFLICT 852..854
FT /note="PAP -> AAS (in Ref. 2; BAA88903)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="A -> P (in Ref. 2; BAA88903)"
FT /evidence="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
