ID A0A091EZA4_CORBR Unreviewed; 676 AA.
AC A0A091EZA4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 31.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 8 {ECO:0000313|EMBL:KFO61614.1};
DE Flags: Fragment;
GN ORFNames=N302_11084 {ECO:0000313|EMBL:KFO61614.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO61614.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO61614.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO61614.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; KK719138; KFO61614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091EZA4; -.
DR STRING; 85066.A0A091EZA4; -.
DR MEROPS; M12.226; -.
DR Proteomes; UP000052976; Unassembled WGS sequence.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR013277; Pept_M12B_ADAM-TS8.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF41; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 8; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01861; ADAMTS8.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:KFO61614.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 1..189
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 124
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 55..107
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 84..89
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 101..184
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 139..168
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 212..237
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 223..246
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 232..267
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 261..272
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 297..334
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 301..339
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 312..324
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO61614.1"
FT NON_TER 676
FT /evidence="ECO:0000313|EMBL:KFO61614.1"
SQ SEQUENCE 676 AA; 74661 MW; 8F8C28BF5B37387F CRC64;
QNHVLTLMSM AARIYKHPSL RNSINLVVVK VLVVEEAAVG PEVSDNGGLT LRNFCSWQQR
FNPPSDRHPE HYDTAILLTR QDFCGHQSCD TLGVADIGTM CDRNKSCSVI EDEGLQAAYT
LAHELGHVLS MPHDDSKNCE RLFGPLGEHH VMAALFVHLN KTQPWSPCSA MYLTEFLDGG
HGDCLLDAPA QPISLPAELP GQRALYSLDQ QCQQIFGKDF QHCPNTTEED ICTQLWCRTS
SGEPLCHTKN GSLPWADGTP CKAEGLCWDG RCVQQDALKP QPAVNGGWGP WSAWGPCSRS
CGGGIQFSHR HCDSPKPRHG GSYCEGQRTK YQSCHTEECP LDGKSFREQQ CEKYNSYNFT
DLEGNHLEWV PKYAGVSPRD RCKLFCRARG RSEFKVFEAK VVDGTLCGPE TLSICVHGQC
IKAGCDHVIG SSKKLDKCGV CGGNGSTCRK ISGSLNRSKY GYNDIVTIPA GATNIDIKQR
SHRGIRPDGD YTALNGDFAT SAMEQDILIK GTILKYSGSM TTLERLQSFR QLPEPLTVQL
LTIASEVFPP KVKYTFFIPK DVPFSKQKGK EKKSVNVIRP MLTSQWVLGD WSECSKTCGS
GWQRRTVDCR DVEGQTSSAC NRSLKPEDIK PCGDMPCPLW RLGPWSPCSQ TCGEGVRTRN
ASCIDYAGKI TAPEKC
//
