ID A0A1S3WEF3_ERIEU Unreviewed; 860 AA.
AC A0A1S3WEF3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 15 isoform X1 {ECO:0000313|RefSeq:XP_016044715.1};
GN Name=ADAM15 {ECO:0000313|RefSeq:XP_016044715.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016044715.1};
RN [1] {ECO:0000313|RefSeq:XP_016044715.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_016044715.1; XM_016189229.1.
DR AlphaFoldDB; A0A1S3WEF3; -.
DR GeneID; 103115619; -.
DR CTD; 8751; -.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; A0A1S3WEF3; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000079721; 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:UP000079721};
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..860
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010383807"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..414
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 421..508
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 653..685
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 179..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..860
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 480..500
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 657..667
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 675..684
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 860 AA; 91896 MW; FF0255DDA606718C CRC64;
MRLALLWALG LLGAGSPLPS RPLPNIGGKE EAQAQQQKPV SVLSEPQAFQ INPAFHLTEG
LQTSLPGALQ IGVDLDGQRH VLELMPYRDL IPGHPKLVWH QPDGTQVVSE GHTLENCCYQ
GRVQGHKGSW VSVCTCSGLR GLVSLSSERS YSLDLGPRGL QGPPAISRIQ DFLPPGQACA
QGQRTSVPTQ VSPQHPVERH QSRRRRHTMT ETKTVELVIV ADHSEVQRYP DPQRLLNRTL
ELALLLDTFF RPLNVRVALV GLEAWAQRDL VEVNRDPGVT LHNFLRWRQE DLLPRLPHDS
AQLVTATEFS GPHVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLTHEA
PGNSCPCPGP APAKSCIMEA STDFLPGLNF SNCSRRALED GLLDGMGSCL LARATGLPSL
ASYCGNGLLE PGEQCDCGFP DDCTDPCCDS FTCQLSPGAQ CASAELCCHN CQLRPAGWQC
RSARGDCDLP ESCPGDSAQC PPDLSVGDGE PCANGQAVCM QGRCASYAHQ CQALWGPGTQ
PTSLLCLQVA NTRGDAFGSC GRAPNGSYVP CEARDAICGQ LQCQRGTAQP LLGMAQDLRW
ERLEANGTWL NCSWVHLDLG SDVAQPLLVL PGTSCGPGLV CLNRQCQPVG LLGAQECRSR
CHGHGVCDSN RHCHCDEGWA PPDCATQARA TSSLTTGLLL SLLVLLVLVL LGASYWYRAR
LHQRLCQLKG PTCQYRAAQP APPERPGLPQ RAQLVPGTKA SALGFPAPPS RPLPPDPVPK
RLQAELAGRP SPPTRPLPAD PVVRHLQGPT KPPLPRKPLP VDPHGRRPSG NLPNPGAASP
PLVVPSRPAP PPPAASSPYL
//
