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Disintegrin and metalloproteinase domain-containing protein 15 (ADAM 15) (EC 3.4.24.-) (CRII-7) (Metalloprotease RGD disintegrin protein) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15) (MDC-15) (Metargidin)

 ADA15_RAT               Reviewed;         864 AA.
Q9QYV0; Q6P779;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 2.
25-OCT-2017, entry version 141.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 15;
Short=ADAM 15;
EC=3.4.24.-;
AltName: Full=CRII-7;
AltName: Full=Metalloprotease RGD disintegrin protein;
AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15;
Short=MDC-15;
AltName: Full=Metargidin;
Flags: Precursor;
Name=Adam15; Synonyms=Mdc15;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Sciatic nerve;
PubMed=11102971;
DOI=10.1002/1098-1136(200012)32:3<313::AID-GLIA100>3.0.CO;2-G;
Bosse F., Petzold G., Greiner-Petter R., Pippirs U., Gillen C.,
Mueller H.-W.;
"Cellular localization of the disintegrin CRII-7/rMDC15 mRNA in rat
PNS and CNS and regulated expression in postnatal development and
after nerve injury.";
Glia 32:313-327(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: 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. 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 (By similarity). {ECO:0000250}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
Note=Binds 1 zinc ion per subunit. {ECO:0000305};
-!- SUBUNIT: Interacts with ITAGV-ITGB3 (vitronectin receptor).
Interacts with SH3GL2 and SNX9; this interaction occurs
preferentially with ADAM15 precursor, rather than the processed
form, suggesting it occurs in a secretory pathway compartment
prior to the medial Golgi (By similarity). Interacts with ITAG9-
ITGB1. Interacts specifically with Src family protein-tyrosine
kinases (PTKs). Interacts with SH3PXD2A. Interacts with ITAGV-
ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN, MAPK1, MAPK3,
NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Single-
pass type I membrane protein {ECO:0000250}. Cell junction,
adherens junction {ECO:0000250}. Cell projection, cilium,
flagellum {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle,
acrosome {ECO:0000250}. Note=The majority of the protein is
localized in a perinuclear compartment which may correspond to the
trans-Golgi network or the late endosome. The pro-protein is the
major detectable form on the cell surface, whereas the majority of
the protein in the cell is processed (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9QYV0-1; Sequence=Displayed;
Name=2;
IsoId=Q9QYV0-2; Sequence=VSP_039534;
-!- TISSUE SPECIFICITY: Predominantly expressed in brain, spinal cord,
sciatic nerve and lung. Expressed at lower levels in all other
tissues. In the peripheral nervous system, expressed predominantly
by Schwann cells. In the central nervous system, preferentially
expressed by neuronal cells.
-!- INDUCTION: In response to sciatic nerve injury.
-!- DOMAIN: The cytoplasmic domain is required for SH3GL2- and SNX9-
binding. {ECO:0000250}.
-!- DOMAIN: Disintegrin domain binds to integrin alphaV-beta3.
{ECO:0000250}.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- PTM: Phosphorylation increases association with PTKs.
{ECO:0000250}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AJ251198; CAB61762.1; -; mRNA.
EMBL; BC061796; AAH61796.1; -; mRNA.
RefSeq; NP_064704.1; NM_020308.1. [Q9QYV0-2]
RefSeq; XP_006232804.1; XM_006232742.3. [Q9QYV0-1]
UniGene; Rn.162607; -.
ProteinModelPortal; Q9QYV0; -.
SMR; Q9QYV0; -.
BioGrid; 248604; 1.
STRING; 10116.ENSRNOP00000039351; -.
MEROPS; M12.215; -.
PaxDb; Q9QYV0; -.
Ensembl; ENSRNOT00000027970; ENSRNOP00000027970; ENSRNOG00000020590. [Q9QYV0-2]
Ensembl; ENSRNOT00000050868; ENSRNOP00000039351; ENSRNOG00000020590. [Q9QYV0-1]
GeneID; 57025; -.
KEGG; rno:57025; -.
UCSC; RGD:620402; rat. [Q9QYV0-1]
CTD; 8751; -.
RGD; 620402; Adam15.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
GeneTree; ENSGT00760000118888; -.
HOGENOM; HOG000230884; -.
HOVERGEN; HBG006978; -.
InParanoid; Q9QYV0; -.
KO; K06836; -.
OMA; HGVCDSN; -.
OrthoDB; EOG091G01NX; -.
PhylomeDB; Q9QYV0; -.
TreeFam; TF314733; -.
Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
Reactome; R-RNO-8941237; Invadopodia formation.
PRO; PR:Q9QYV0; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000020590; -.
Genevisible; Q9QYV0; RN.
GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:RGD.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IEA:Ensembl.
GO; GO:0098609; P:cell-cell adhesion; TAS:RGD.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl.
GO; GO:1900121; P:negative regulation of receptor binding; IEA:Ensembl.
GO; GO:0070528; P:protein kinase C signaling; IEA:Ensembl.
GO; GO:0042246; P:tissue regeneration; IEP:RGD.
CDD; cd04269; ZnMc_adamalysin_II_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR033605; ADAM15.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR024079; MetalloPept_cat_dom.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR034027; Reprolysin_adamalysin.
PANTHER; PTHR11905:SF130; PTHR11905:SF130; 1.
Pfam; PF08516; ADAM_CR; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
SMART; SM00608; ACR; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
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.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 208 {ECO:0000250}.
/FTId=PRO_0000029086.
CHAIN 209 864 Disintegrin and metalloproteinase domain-
containing protein 15.
/FTId=PRO_0000029087.
TOPO_DOM 209 698 Extracellular. {ECO:0000255}.
TRANSMEM 699 719 Helical. {ECO:0000255}.
TOPO_DOM 720 864 Cytoplasmic. {ECO:0000255}.
DOMAIN 215 416 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 423 510 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
DOMAIN 659 687 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
MOTIF 178 185 Cysteine switch. {ECO:0000250}.
MOTIF 816 822 SH3-binding. {ECO:0000255}.
MOTIF 851 857 SH3-binding. {ECO:0000255}.
COMPBIAS 511 658 Cys-rich.
COMPBIAS 700 713 Poly-Leu.
ACT_SITE 351 351 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 180 180 Zinc; in inhibited form. {ECO:0000250}.
METAL 350 350 Zinc; catalytic. {ECO:0000255}.
METAL 354 354 Zinc; catalytic. {ECO:0000255}.
METAL 360 360 Zinc; catalytic. {ECO:0000255}.
MOD_RES 717 717 Phosphotyrosine; by HCK and LCK.
{ECO:0000250|UniProtKB:Q13444}.
MOD_RES 737 737 Phosphotyrosine; by HCK and LCK.
{ECO:0000250|UniProtKB:Q13444}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 391 391 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 394 394 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 608 608 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 613 613 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 325 411 {ECO:0000250}.
DISULFID 367 395 {ECO:0000250}.
DISULFID 369 378 {ECO:0000250}.
DISULFID 482 502 {ECO:0000250}.
DISULFID 659 669 {ECO:0000250}.
DISULFID 663 675 {ECO:0000250}.
DISULFID 677 686 {ECO:0000250}.
VAR_SEQ 762 809 Missing (in isoform 2).
{ECO:0000303|PubMed:11102971}.
/FTId=VSP_039534.
CONFLICT 202 202 H -> R (in Ref. 2; AAH61796).
{ECO:0000305}.
SEQUENCE 864 AA; 93308 MW; 5D46466922A89196 CRC64;
MRLALLWALG LLGAGSPRPS PPLPNIGGTE EEQQASPERT QSRSLENQVV QDSPPINLTE
VLQTGLPETL RIGLELDGEN HILELQQNRD LVPGRPTLVW YQPDGTRMVS EGHSLENCCY
RGRVQGRPSS WVSLCACSGI RGLVVLSPER SYTLELGPGD LQRPLIVSRI QDLLLPGHTC
APSWHAFVPT EAAPDLLLEQ HHLRRLKRDV VTETKIVELV IVADNSEVRK YPDFQQLLNR
TLEVALLLDT FFQPLNVRVA LVGLEAWTQR DLIEMSSNPA VLLDNFLRWR RTDLLPRLPH
DSAQLVTVTS FSGPMVGMAI QNSICSPDFS GGVNMDHSTS ILGVASSIAH ELGHSLGLDH
DSPGNSCPCP GPAPAKSCIM EASTDFLPGL NFSNCSRWAL EKALLDGMGS CLFEWPPSRA
PMSSLCGNMF VDPGEQCDCG FPDECTDPCC DYFTCQLRPG AQCASDGPCC QNCKLQPAGW
QCRLPTDDCD LPEFCLGDSS QCPPDIRLGD GEPCASGEAV CMHGRCASYT RQCQSLWGPG
AQPAAPLCLQ TANTRGNAFG SCGRSPSGSY MPCNLRDAIC GQLQCQWGRN QPLLGSVQDQ
LSEVLEANGT QLNCSWVDLD LGNDVAQPLL ALPGTACGPG LVCIGHRCQP VDLLGAQECR
SKCHGHGVCD SSRHCHCDEG WAPPDCMTQL RATSSLTTGL LLSLLLLLVL VLLGASYWYR
ARLHQRLCQL KGSSCQYRAA QSGPPERPGP PQRAQQMPGT KQANVSFPVP PSRPLPPNPV
PKKLQAELAD RSNPPTRPLP ADPVVWRPKP QGPTKPPPPR KPLPANPQGR PPLGDLPGPG
DGSLQLVVPS RPAPPPPAAS SLYL


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