ID A0A2K6RUJ1_RHIRO Unreviewed; 836 AA.
AC A0A2K6RUJ1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ADAM metallopeptidase domain 15 {ECO:0000313|Ensembl:ENSRROP00000044686.1};
GN Name=ADAM15 {ECO:0000313|Ensembl:ENSRROP00000044686.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000044686.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000044686.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A2K6RUJ1; -.
DR Ensembl; ENSRROT00000069205.1; ENSRROP00000044686.1; ENSRROG00000045295.1.
DR GeneTree; ENSGT00940000159822; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF130; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 15; 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; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..836
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014381979"
FT TRANSMEM 692..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..412
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 419..506
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 651..683
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..798
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..836
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 478..498
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 655..665
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 673..682
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 836 AA; 89873 MW; 817106CBD01F54FE CRC64;
MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAMSEKAP RGPLEPQVLQ DDLPISLKKT
SLPEPLRIKL ELDGDSHILE LLQNRELVPG RPILVWYQPD GTRVVSEGHT LENCCYQGRV
QGYAGSWVSI CTCSGLRGLV VLSPERSYTL EQGPGDVQGP PIISRIQDLH LPGHTCVLSW
REPVHTQTPP KHPLGQRHIR RWRRDVVTET KTVELVIVAD HSEVQKYRDF QHLLNRTLEV
ALLLDTFFRP LNVRVALVGL EAWTQRDLVE ISPNPAVTLE NFLHWRRAHL LPRLPHDSAQ
LVTGTSFSGP MVGMAIQNSI CSPDFSGGVN MDHSTSILGV ASSIAHELGH SLGLDHDLPG
NSCPCPGPAP AKTCIMEAST DFLPGLNFSN CSRQALEKAL LDGMGSCLFE RLPSLPPMAA
FCGNMFVELG EQCDCGFPDD CADPCCDSST CQLRPGAQCA SDGPCCQNCQ LRPSGWQCRP
TRGDCDLPEF CPGDSSQCPP DISLGDGEPC AGGQAVCMHG RCASYAQQCQ SLWGPGAQPA
APLCLQTANT RGNAFGSCGR NPSGGYVSCT PRDAICGQLQ CQTGRTQPLL GSIQDLLWET
IDVNGTELNC SWVHLDLGSD VAQPLLTLPG TACGPGLVCI DHRCQRVDLL GAQECRSKCH
GHGVCDSNRH CYCEEGWAPP DCTTQLKATS SLTTGLLLSL LVLLVLVVLG ASYWYRARLH
QRLCQLKGPT CQYRAAQSGP PERPGPPQRA LLARGTKASA LGFPAPPSRP LPPDPVPKRL
QSQGPAKPPP PRKPLPADPQ GRCPSGDLPG PGAGIPPLAL PSRPAPPPPT VSSLYL
//
