ID A0A452RGV8_URSAM Unreviewed; 811 AA.
AC A0A452RGV8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=ADAM metallopeptidase domain 15 {ECO:0000313|Ensembl:ENSUAMP00000018176.1};
GN Name=ADAM15 {ECO:0000313|Ensembl:ENSUAMP00000018176.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000018176.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000018176.1}
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:PRU00276}.
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DR AlphaFoldDB; A0A452RGV8; -.
DR Ensembl; ENSUAMT00000020347.1; ENSUAMP00000018176.1; ENSUAMG00000014398.1.
DR GeneTree; ENSGT00940000159822; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
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 InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
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; 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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00068}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
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 TRANSMEM 670..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..386
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 393..480
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..811
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 321
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 452..472
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 811 AA; 86817 MW; A01B743682C8F8CC CRC64;
PAGGTEEERA RPERARGGPS EPQILQDIPT LSLAEVFQVS VSPLKEAMVT ALLFLPRELV
PGHPSLMWYQ PDGTRVVSVG HTLENCCYQG AVQGHAGSWV SVCTCSGLRG VVILSPERSY
TLDLGPGDLQ APPNISRTQD LVLPGRTCAL SWPASLHTQA RLERPRGRRH SPSHRRRRDV
VTETKTIELV IVADHSEVQR YPDSQHLLNR MLRVTLLLDT FFRPLNVRVV LVGLEAWTQR
DLVEVSQDPG LTLDKFLRWR RRDLLSRLPH DSAQLVTATS FSGPTVGMAI QNSICSPDFS
GGVNMDHSTS VLGLASSIAH ELGHSLGLAH DLPGNSCPCP GPAPAKSCIM EASTDFLPGL
NFSNCSQQAL EKALLEGMGS CLFERLPSLP SLATVCGNMF VEPGEQCDCG FPDDCTDPCC
DYFTCQLRPG AQCASDGLCC QNCQLRPTSW QCRPSRGDCD LPEFCSGDSP QCPPDVSLGD
GEPCAGGQAV CMQGRCASYA QQCQALWGPG AQPASPLCLL AANTRGDAFG SCGRNPNGSY
VSCAPKDAIC GQLQCQGGQA QPLLGSARDL RWEMLEANGT QLRPNCSWVH LDLGDDVAQP
LLTLPGTACG PDLGCLDEQC AGLSVPQCRH RLSGGPMRVC DSAGHCHCEE GWAPPDCTQR
VRATSSLTTG LPLSLLLVVV LMLLGASYWH RARLRQRLCQ LKGPSCQYRA AQSGPPERPG
PPQRVLLMPG AKAELADRPN PPTRPLPADP VVRRPKVTGP AKPPPPRKPL PANPQGRRPS
GDLPGPGDGI PPLAVPARPA PPPPAASSLY L
//
