ID A0A093RI14_PHACA Unreviewed; 969 AA.
AC A0A093RI14;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 2 {ECO:0000313|EMBL:KFW95587.1};
DE Flags: Fragment;
GN ORFNames=N336_05788 {ECO:0000313|EMBL:KFW95587.1};
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW95587.1, ECO:0000313|Proteomes:UP000053238};
RN [1] {ECO:0000313|EMBL:KFW95587.1, ECO:0000313|Proteomes:UP000053238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW95587.1};
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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; KL446535; KFW95587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093RI14; -.
DR MEROPS; M12.301; -.
DR Proteomes; UP000053238; 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; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 4.
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; IPR013275; Pept_M12B_ADAM-TS2.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF141; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 2; 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; 3.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01859; ADAMTS2.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:KFW95587.1};
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:UP000053238};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 33..237
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 816..854
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 883..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 175
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 179
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 185
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 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 110..159
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 153..232
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 192..218
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 259..284
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 270..293
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 279..312
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 306..317
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 340..377
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 344..382
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 355..367
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW95587.1"
FT NON_TER 969
FT /evidence="ECO:0000313|EMBL:KFW95587.1"
SQ SEQUENCE 969 AA; 111026 MW; 9A4789F355391895 CRC64;
TNLDSLNSAL SFIEDRVHRS RQRYRRHATE DDYNIEVLLG VDDSVVQFHG KEHVQKYLLT
LMNIVNEIYH DESLGAHINV VLVRIILLSY GKSMSLIEIG NPSQSLENVC RWAYLQQKPD
TGHAEYHDHA IFLTRQDFGP SGMQGYAPVT GMCHPVRSCT LNHEDGFSSA FVVAHETGHV
LGMEHDGQGN RCGDEVRLGS IMAPLVQAAF HRFHWSRCSQ QELNRYLHSY DCLRDDPFEH
DWPSLPQLPG IHYSMNEQCR FDFGLGYMMC TAFRTFDPCK QLWCSHPENP YFCKTKKGPP
LDGTMCAPGK HCFKGHCIWL TPDILKQDGH WGAWSKFGSC SRTCGTGVKY RTRQCDNPHP
ANGGRTCVGP SYEFQLCNSQ DCPKDFEDFR EQQCRQWDPY FEYQNTKHHW LPYEHVDAKE
RCHLYCESKE TGDVVYMKRM VHDGTRCSYK DAYSICVRGD CLKVGCDRVI GSTKQEDKCG
VCGGDNSHCK VVKGTFSRVP KKPGHIKMFE IPVGARHLLI QETDATSHNL AIKNRETGKF
ILSEDNYVPD SKVFIDMGVE WEYRNDDDRE TVQTMGPLRN GIVILVKKTE RTNTKISLTY
KYMIHEDSLN VDNNNVLEED SVSHEWALKK WSQCSKPCGG GFQFTKYGCR RKTDHKMVHR
SYCELIQKPK PIRRVCNLQE CSQPIWVTGE WEPCSKSCGK TGYQVRSVRC IQPKYCNNDR
PEGRRPCNRE LCPAQWRIGP WSQCSVSCGN GTQDRPVLCR TRDNAIGLCK DSKPETVRIC
RLPPCPRNVS DPSKKTYMIQ WLSRPDPDYP IQKISSKDHC QGDKSMFCRM EVLSRYCSIP
GYNKLCCKSC NMYSNVTEDD NVTDSNVNKN NVIEEELLTT LSPPMGVSTT QSATSPPPVA
KTRAPPSNAT EEHPEINAVD VPYKIDGLDN EVSQHNIITR RRIPYERTRN QRIQELIAEK
RKKETLRKI
//
