ID A0A093HCS1_STRCA Unreviewed; 1079 AA.
AC A0A093HCS1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 10 {ECO:0000313|EMBL:KFV77230.1};
DE Flags: Fragment;
GN ORFNames=N308_08039 {ECO:0000313|EMBL:KFV77230.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV77230.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV77230.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV77230.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL205931; KFV77230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HCS1; -.
DR STRING; 441894.ENSSCUP00000007771; -.
DR Proteomes; UP000053584; 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); 1.
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; IPR010909; PLAC.
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; PF08686; PLAC; 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; PS50900; PLAC; 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:KFV77230.1};
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:UP000053584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 DOMAIN 1041..1079
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
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 302..360
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
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:KFV77230.1"
FT NON_TER 1079
FT /evidence="ECO:0000313|EMBL:KFV77230.1"
SQ SEQUENCE 1079 AA; 120446 MW; 790280BB4729DAF7 CRC64;
SSCVCFSSPE EFLSSLDHYE IAFPIQVDQN GDFLTFDMRS QLKQRPRRSL GSLPYEPSEQ
QVFYKVSAHR TQFLLNLTLH SNLLAEHFTV EYWKRDGVDW QHDFHEDCHY AGHLQDQYLN
SKVAISNCNG LHGVIVADEE EYFIEPLSPG ANVSTGNEGK GSPHVVYKRS SLQYPHMDAA
CGVLDEKPWK GRHWWLRTLK PSPLKPSGNH SQRGQLPLKR SVSTERYVET LVVADKMMVG
YHGRRDIEQY ILAIMNIVAK LFQDSSLGNI VNILVTRLIL LTEDQPTLEI NHHAGKSLDS
FCKWQKSIVN RNGNGNAIPE NGIANHDTAV LITRLSLGDW PVTSILFSGF SAHPHQCKKC
VKNAAVDHVS IAMMMFSRFG MNHDGVGNSC GSRGQETAKL MAAHITMKTN PFVWSTCSRD
YITSFLDSGM GLCLNNAPPK QDFIYPTVAP GQAYDADEQC RFQYGVKSRQ CKYGEVCSEL
WCLSKSNRCI TNSIPAAEGT ICQTNTIDKG WCYKRECVPF GTRPEGVDGA WGAWSSWGEC
SRTCGGGVSS SIRHCDSPRP TIGGKYCLGE RKRYRSCNTD DCPPGSQDFR ELQCAEFDNV
PFRGKYYTWK TYRGGGVKAC SLNCLAEGFN FYTERAAAVV DGTPCRQDSN DICVNGECKH
VGCDRVLGSD SKEDKCRVCG GDGSTCETIE GVFNQSLPEG GYEEVIQIPK GSVHIDIREL
NLSVNYLALR GENGEYYING KLSIDPPRRF DIAGTTFHYR RSPDEPESLE ALGPTNITLV
VMVELQGIRY KFNAPISRDA SNQYSWHYAP WTKCSALCAG GSQIQSVICK KLSDSSTVFS
HFCSPETKMP ERQRPCNTEP CPPAWVIGNW SECSRSCNEG VRTRSVFCKR KISTTEEKTL
DDASCPQPRP KMLEPCNNQT CPPEWVALDW SECTPSCGPG FRHRIVLCKS GDHSTTLPTS
QCPEGSKPPT SMRCNLRRCP PPRWVTGEWG ECSAQCGLGQ QRRSVQCLAH TGQPSSDCVE
TLQPPGMQQC ETKCESGPTD NPEECKDVNK VAYCPLVLKF KFCSRTYFRQ MCCKTCQGH
//
