ID A0A091Q937_LEPDC Unreviewed; 968 AA.
AC A0A091Q937;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 17 {ECO:0000313|EMBL:KFQ16480.1};
DE Flags: Fragment;
GN ORFNames=N330_11775 {ECO:0000313|EMBL:KFQ16480.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ16480.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ16480.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ16480.1};
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; KK690656; KFQ16480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091Q937; -.
DR MEROPS; M12.027; -.
DR PhylomeDB; A0A091Q937; -.
DR Proteomes; UP000053001; 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 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; 5.
DR InterPro; IPR006586; ADAM_Cys-rich.
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; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13723:SF151; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 17; 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; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00608; ACR; 1.
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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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:KFQ16480.1};
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:UP000053001};
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}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 81..301
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 921..960
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 239
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 238
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 242
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 248
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 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 157..222
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 197..204
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 216..296
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 255..280
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 325..349
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 336..357
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 344..376
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 370..381
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 404..441
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 408..446
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 419..431
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ16480.1"
FT NON_TER 968
FT /evidence="ECO:0000313|EMBL:KFQ16480.1"
SQ SEQUENCE 968 AA; 108468 MW; 5528A3A91C6350AD CRC64;
VGYIQIGSEH MLIQPVNTSE TSFSGKEHFI RRRRSAKSNH PMKPVPDEHC KVVAEKKRQK
KMKSTSDWRE RRNAIRLNNE YTVETLVVAD ADMVQYHGAE AAQRFILTVM NMVYNMFQHQ
SLGIKVSIRV TKLVLLHNRP AKLSIGHHGE RSLESFCQWQ NEEYGGAKYL GNNQVPGARD
DTPPVDAAVF VTRTDFCVHK DEPCDTVGIA YLGGVCSAKR KCVLAEDNGL NLAFTIAHEL
GHNMGMSHDD DHQPCAGRSH IMSGEWVKGR NPSDLSWSSC SRDDLENFLK SKVSTCLLVT
DPRSQYAVRL PHKLPGMHYS ADEQCQILFG TNATFCKNME HLMCAGLWCL VEGDTSCKTK
LDPPLDGTEC GADKWCRAGE CVSKTPIPEH VDGDWSMWSQ WSMCSRTCGT GVRFRQRKCD
NPPPGPGGKN CRGASVEHTV CENLPCPKGV PGFRDQQCQA HDRYTNKKKS VLTAVIVDDK
PCELFCSPLG KDSPVLVADR VLDGTPCGPY ETDLCVHGKC QKIGCDGIIG SAAKEDRCGI
CSGDGKTCKV VKGDFNHTKG MGYIEAAVIP AGARRIRVVE DKPAHSFLAL KDSSKRSINS
DWKIELPGEF QIAGTTVRYV RRGLWEKISA KGPTKIPLHL MVLLFHDQNY GIHYEYTIPV
NYTAENRSEP EKQQDSLYIW THSGWEGCSV QCGGGERKTI VSCTRIINKT MTLVNDSDCQ
RVNRPEPQVR KCNTHPCQSR WVTGHWSPCS ATCEKGVQHR EVTCVYQLQN GTYVNTRDLY
CLGNKPTTVQ SCEGRDCLSI WEASEWSKCS ADCGKGIQKR TVTCTNSQGK CDAATRPRDE
EECEDHTGCY EWKTGDWSKC SSTCGKGLQS RVVQCMHKVT GRHGNECPVL SKPAAYRQCH
QEVCNEKINV NTITSPRLAA LTYKCTGDQW TVYCRVIREK NLCQDMRWYQ RCCQTCRDFY
ANKMQQKS
//
