ID A0A093H2G9_STRCA Unreviewed; 704 AA.
AC A0A093H2G9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 14 {ECO:0000313|EMBL:KFV73257.1};
DE Flags: Fragment;
GN ORFNames=N308_03707 {ECO:0000313|EMBL:KFV73257.1};
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:KFV73257.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV73257.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV73257.1};
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; KL205708; KFV73257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093H2G9; -.
DR STRING; 441894.ENSSCUP00000000955; -.
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; 1.
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; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF24; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 14; 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; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 1.
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:KFV73257.1};
KW Metal-binding {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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2}.
FT DOMAIN 89..280
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 167..215
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 210..288
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 250..276
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 315..340
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 326..349
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 335..368
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 362..373
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 397..434
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 401..439
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 412..424
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV73257.1"
FT NON_TER 704
FT /evidence="ECO:0000313|EMBL:KFV73257.1"
SQ SEQUENCE 704 AA; 79114 MW; 468A44352EB97530 CRC64;
CGLQAGLIRT DSNEFFIEPL ERGQQEKEAH GRAHVVYRRS AIRQDGAQPR EDLHPRAPRF
RVGELPNSLE LVEERLGDAG RRRAKRDDYN IEVLLAVDDS VVRFHGKEHV QNYVLTLMNI
VRLSRLFFFF FGGGRDCLPR AQLEGCWWEQ VSLIERGNPS RSLEQVCRWA HSQQRSDPEH
AEYHDHAVFL TRQDFGPAGM QGTVFISISC SVLACGLRIK PSLPKRAASG QQTGFSNRLG
MEHDGQGNRC ADETSMGSIM APLVQAAFHR YHWSRCSKQE SYIHSYDCLL DDPFEHQWPK
LPELPGINYS MDEQCRFDFG VGYKTCTAFR TFDPCKQLWC SHPDNPYFCK TKKGPPLDGT
ECSSGKWCFK GHCIWKTSEQ PYSQDGSWSS WSKFGSCSRT CGGGVRSRSR SCSNPPPAYG
GRHCPGATYE YQVCNPEECP GPYEDFRAQQ CSKRNSYYTH QSAKHTWLPY EHHDDAQKCE
LICQSEGTGD VVFMNQVVHD GTRCSYRDPY SICVRGECVH VGCDKEVGSL KQDDKCGVCG
GDNSHCRTVK GTLAKTPKQL ACSFLPSLLS LPLSLSVGIH VQIEEMEPAS HSIAVKNQAT
GDFILNAKGK EAKSKVFIGM GLEWEYAVEN GKESLKTSGP LHEAISVLVV PQEEEAKSSL
MYRYIIHEDL LPMIGNNNVL LEEMDSYEWA LKSWSQCSKA CGGG
//
