ID A0A087VE55_BALRE Unreviewed; 1047 AA.
AC A0A087VE55;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 10 {ECO:0000313|EMBL:KFO10897.1};
DE Flags: Fragment;
GN ORFNames=N312_02707 {ECO:0000313|EMBL:KFO10897.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO10897.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO10897.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO10897.1};
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; KL489884; KFO10897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087VE55; -.
DR Proteomes; UP000053309; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; 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: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 Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 2.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
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; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF26; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 10; 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; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 5.
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:ARBA00022801};
KW Integrin {ECO:0000313|EMBL:KFO10897.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053309};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT DOMAIN 226..438
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 390..417
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 460..482
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 471..489
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 477..512
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 502..517
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 540..577
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 544..582
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 555..567
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO10897.1"
FT NON_TER 1047
FT /evidence="ECO:0000313|EMBL:KFO10897.1"
SQ SEQUENCE 1047 AA; 116643 MW; 3019EB55AAF18396 CRC64;
SSCVCFPSSE EFLSSLDHYE IAFPIQVDQN GDFLTFDVRS QLKQRPRRSL GSLPYEPSEQ
QVFYKVSAHR TQFLLNLTLH SNLLAEHFTV EYWKRDGMDW QHDFHEDCHY AGHLQDRYLN
SKVAISNCNG LHGVIVADEE EYFIEPLSPG ANVSTGSEGK GSPHVVYKRS SLQYPHMDAA
CGVLDEKPWK RRHWWLRTLK PSPLKPSGNH SQRGQLPLKR SVSTERYVET LVVADKMMVG
YHGRRDIEQY ILAIMNIVAK LFQDSSLGNI VNILVTRLIL LTEDQPTLEI NHHAGKSLDS
FCKWQKSIVN RNGNGNAIPE NGIANHDTAV LITRNTLHLT HHVLSACFFP ALIPMGPPGC
VESAAADHLS IDLAMLSRFG MNHDGVGNSC GSRGQETAKL MAAHITMKTN PFVWSTCSRD
YITSFLDSGM GLCLNNAPPK QDFIYPTVAP GQAYDADEQC RFQYGVKSRQ CKYGEVCSEL
WCLSKSNRCI TNSIPAAEGT ICQTNTIEKG WCYKRECVPF GTRPEGVDGA WGAWSSWGEC
SRTCGGGVSS SIRHCDSPRP TIGGKYCLGE RKRYRSCNTD DCPPGSQDFR ELQCAEFDNV
PFRGKYYTWK TYRGGGVKAC SLNCLAEGFN FYTERAAAVV DGTPCRQDSN DICVNGECKH
VGCDRVLGSD SKEDKCRVCG GDGSSCETVE GIFNQSLPEG GYEEVIQIPK GSVHIDIREL
NLSINYLALR GESGEYYING KLSIDPPRRF DIAGTTFHYR RSPEEPESLE ALGPTNVTLF
VMVLVRTELQ GIRYKFNAPI GRDASNQYSW HYTPWTKCSV LCAGGSQIQS VVCKKLADGS
TVFNHFCSPE TKMPERQRPC NTEPCPPAWV IGNWSECSRS CNEGVRTRSV FCKRKISATE
EKTLDDASCT HPRPKMLEPC NNQTCPPEWV ALDWSECTPS CGPGFRHRIV LCKSGDHSTT
LPTSQCYEGS KPPTSMRCNL RRCPPPRWVT GEWGECSAQC GLGQQRRSVQ CLAHTGQLSS
DCVETLQPPG MQQCETKCES GPTDNPD
//
