ID A0A091Q7D5_LEPDC Unreviewed; 734 AA.
AC A0A091Q7D5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Cartilage oligomeric matrix protein {ECO:0000313|EMBL:KFQ15471.1};
DE Flags: Fragment;
GN ORFNames=N330_02270 {ECO:0000313|EMBL:KFQ15471.1};
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:KFQ15471.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ15471.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ15471.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thrombospondin family.
CC {ECO:0000256|ARBA:ARBA00009456}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KK688219; KFQ15471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091Q7D5; -.
DR PhylomeDB; A0A091Q7D5; -.
DR Proteomes; UP000053001; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd16077; TSP-5cc; 1.
DR Gene3D; 1.20.5.10; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR039081; TSP-5_cc.
DR InterPro; IPR024665; TSP/COMP_coiled-coil.
DR InterPro; IPR046970; TSP/COMP_coiled-coil_sf.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR10199:SF88; CARTILAGE OLIGOMERIC MATRIX PROTEIN; 1.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR Pfam; PF11598; COMP; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 5.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SUPFAM; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51234; TSP3; 3.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00634}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 60..99
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 100..137
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 199..241
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 275..310
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 334..369
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 471..506
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 510..724
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 356..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..453
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ15471.1"
FT NON_TER 734
FT /evidence="ECO:0000313|EMBL:KFQ15471.1"
SQ SEQUENCE 734 AA; 80417 MW; 170F1A014F9EBC87 CRC64;
GEVGPEMLEE MRETNRVLME VRDLLKQQIK EITFLKNTVM ECDACGMHTE ATGPVITVTQ
FNRCLPNPCF PGVACTETGT GFRCGPCPPG YSGNGSQCTD INECNANPCF PKVQCINTSP
GFRCDPCPPG FTGQTVEGVG LAYARANKQV CTDINECETG AARNCVPNSI CINTRGSYKC
GACKPGFVGD QVTGCKSQTL RRCPNGEISP CHEKAQCIVE RDGSLSCVCL VGWAGNGYVC
GKDTDIDGVP DEKQRCSDKK CRKDNCVTVP NSGQEDADRD GIGDACDDDA DGDGILNAED
NCVYTRNADQ RNADKDNFGD ACDNCRQVKN NDQRDIDGDG RGDECDDDMD GDGIKNAVDN
CKRVPNPDQK DGDGDGVGDV CDSCPTVSNP DQKDTDHDLV GDVCDTNQDS DGDGHQDSRD
NCPSVPNSSQ VDTDNDGLGD ECDDDDDDDG IPDEKPPGPD NCRLVPNPGQ EDSDGDGVGN
LCEDDFDRDM VIDRIDVCPE NAEVTLTDFR AFQTVVLDPE GDAQIDPNWI VLNQGMEIVQ
TMNSDPGLAV GYTAFNGVDF EGTFHVNTAT DDDYAGFIFG YQDSSSFYVV MWKQMEQTYW
QANPFRAVAE PGIQLKAVKS KTGPGEYLRN SLWHTGDTTD QVKLLWKDPR NSGWKDKTSY
RWFLQHRPQV GYIRARFYEG PEVVADTGVV LDTTMRGGRL GVFCFSQENI IWSNLRYRCN
DTIPEDYETF RVQQ
//
