| Tag | Content |
|---|
| CPLM ID | CPLM-001411 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Disintegrin and metalloproteinase domain-containing protein 15 |
Protein Synonyms/Alias | ADAM 15; AD56; Metalloprotease RGD disintegrin protein; Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15; MDC-15; Metargidin |
Gene Name | Adam15 |
Gene Synonyms/Alias | Mdc15 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 730 | HQRLCQLKGSSCQYR | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration (By similarity). Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. Interactions with egg membrane could be mediated via binding between the disintegrin-like domain to one or more integrin receptors on the egg. |
Sequence Annotation | DOMAIN 214 415 Peptidase M12B.
DOMAIN 422 509 Disintegrin.
DOMAIN 658 686 EGF-like.
MOTIF 177 184 Cysteine switch (By similarity).
MOTIF 816 822 SH3-binding (Potential).
MOTIF 851 857 SH3-binding (Potential).
ACT_SITE 350 350 Potential.
METAL 179 179 Zinc; in inhibited form (By similarity).
METAL 349 349 Zinc; catalytic (Potential).
METAL 353 353 Zinc; catalytic (Potential).
METAL 359 359 Zinc; catalytic (Potential).
MOD_RES 716 716 Phosphotyrosine; by HCK and LCK (By
MOD_RES 736 736 Phosphotyrosine; by HCK and LCK (By
CARBOHYD 238 238 N-linked (GlcNAc...) (Potential).
CARBOHYD 390 390 N-linked (GlcNAc...) (Potential).
CARBOHYD 393 393 N-linked (GlcNAc...) (Potential).
CARBOHYD 607 607 N-linked (GlcNAc...) (Potential).
CARBOHYD 612 612 N-linked (GlcNAc...) (Potential).
DISULFID 324 410 By similarity.
DISULFID 366 394 By similarity.
DISULFID 368 377 By similarity.
DISULFID 481 501 By similarity.
DISULFID 658 668 By similarity.
DISULFID 662 674 By similarity.
DISULFID 676 685 By similarity. |
Keyword | Alternative splicing; Angiogenesis; Cell adhesion; Cell junction; Cell projection; Cleavage on pair of basic residues; Collagen degradation; Complete proteome; Cytoplasmic vesicle; Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Reference proteome; SH3-binding; Signal; Transmembrane; Transmembrane helix; Zinc; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 864 AA |
Protein Sequence | MRLALLWALG LLGAGSPRPS PPLPNIGGTE EEQQASPERT LSGSMESRVV QDSPPMSLAD 60
VLQTGLPEAL RISLELDSES HVLELLQNRD LIPGRPTLVW YQPDGTRMVS EGYSLENCCY 120
RGRVQGHPSS WVSLCACSGI RGLIVLSPER GYTLELGPGD LQRPVISRIQ DHLLLGHTCA 180
PSWHASVPTR AGPDLLLEQH HAHRLKRDVV TETKIVELVI VADNSEVRKY PDFQQLLNRT 240
LEAALLLDTF FQPLNVRVAL VGLEAWTQHN LIEMSSNPAV LLDNFLRWRR TDLLPRLPHD 300
SAQLVTVTSF SGPMVGMAIQ NSICSPDFSG GVNMDHSTSI LGVASSIAHE LGHSLGLDHD 360
SPGHSCPCPG PAPAKSCIME ASTDFLPGLN FSNCSRQALE KALLEGMGSC LFERQPSLAP 420
MSSLCGNMFV DPGEQCDCGF PDECTDPCCD HFTCQLRPGA QCASDGPCCQ NCKLHPAGWL 480
CRPPTDDCDL PEFCPGDSSQ CPSDIRLGDG EPCASGEAVC MHGRCASYAR QCQSLWGPGA 540
QPAAPLCLQT ANTRGNAFGS CGRSPGGSYM PCAPRDVMCG QLQCQWGRSQ PLLGSVQDRL 600
SEVLEANGTQ LNCSWVDLDL GNDVAQPLLA LPGTACGPGL VCIGHRCQPV DLLGAQECRR 660
KCHGHGVCDS SGHCRCEEGW APPDCMTQLK ATSSLTTGLL LSLLLLLVLV LLGASYWHRA 720
RLHQRLCQLK GSSCQYRAPQ SCPPERPGPP QRAQQMTGTK QASVVSFPVP PSRPLPPNPV 780
PKKLQAALAD RSNPPTRPLP ADPVVRRPKS QGPTKPPPPR KPLPANPQGQ HPPGDLPGPG 840
DGSLPLVVPS RPAPPPPAAS SLYL 864 |
Gene Ontology | GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell. GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell. GO:0042995; C:cell projection; IEA:UniProtKB-KW. GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:MGI. GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. GO:0042246; P:tissue regeneration; IEA:Compara. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |