ID A0A851QQV3_TYCCO Unreviewed; 1341 AA.
AC A0A851QQV3;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE SubName: Full=COFA1 protein {ECO:0000313|EMBL:NXC80739.1};
DE Flags: Fragment;
GN Name=Col15a1_0 {ECO:0000313|EMBL:NXC80739.1};
GN ORFNames=CERCOR_R02258 {ECO:0000313|EMBL:NXC80739.1};
OS Tychaedon coryphoeus (Karoo scrub-robin) (Erythropygia coryphaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Muscicapidae; Cercotrichas.
OX NCBI_TaxID=614051 {ECO:0000313|EMBL:NXC80739.1, ECO:0000313|Proteomes:UP000631545};
RN [1] {ECO:0000313|EMBL:NXC80739.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OUT-0024 {ECO:0000313|EMBL:NXC80739.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXC80739.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXC80739.1}.
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DR EMBL; WBND01000065; NXC80739.1; -; Genomic_DNA.
DR Proteomes; UP000631545; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000631545};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 8..196
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 193..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..581
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..602
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..620
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..680
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..743
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..786
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..803
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..968
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1078
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXC80739.1"
FT NON_TER 1341
FT /evidence="ECO:0000313|EMBL:NXC80739.1"
SQ SEQUENCE 1341 AA; 140431 MW; E5D2E4F4FB161795 CRC64;
PERGSKGHLD LTELIGVPLP PSVYFVTGYG GFPAYSFGPD SNIGRLASAM VPSPFYRDFA
VVVTAKPNRD RGGVLFAITD AFQKTIYLGL RIAPVDDSTQ RIIMYYTEPG SHISREAASF
KVPVMTNRWN KFTVAVEGND VALFMDCEEY QRLHFQRSAR ALVFESGSGI FVGNAGATGL
EKFTGSIQHL TIKSDPRATE DHCEDDDPYA SGDSSGNDSI QDHDVSEAQE ALAPSRLPIR
PEDVLAEPVE APPTILSYLE ENDFSGNHRS EETSEAAKFK EQGTASDSAV METGQGNSES
SPVTQKMLRE EDGSGAGVLP GASREKVCQE VEDGSTEPLG GSGIEDVENK DQGPPGSPGK
PGQLGQPVSI FSLLKEILCF RKGDGDPSHM HGELELHSLA HQLHFHETGF SPAAQEDPAC
PAQVSGTGAL WVTPTRRQRQ TAAVPTYKCS QSSNSNSLGS TAAPSQLPGL SVCKGAEPTF
CLVFCCTAAA FKRPVRQPQI SRTRCSRPTA LPKGHFYKYS REHQVLHCLY FPVLCDSKFQ
SLLFCSEVEE VSVHPRNASL TPRHLKWPPG PPGLPGLPGM PAPDSGVGPP GSPGEDGASG
EPGPEGPQGP PGQDGVVGPP GWKGEKGDQG LRGSAGPKGD TGVTGSIGPK GEAGPIGSPG
KPGPPGPPGP PGPPGPPGPP GQSYGLGFEV FCYSELCCNY GYTSSRGRTG PKGEKGDPGP
RGEPGQDGNS VVGPPGPPGP PGPVIAIPEF LLNDTDGIFN FTESKGLLGP PGPDGKPGLP
GFPGPRGPKG DTGLPGLQGP KGQQGEKGEP GAIISADGSL TELLGRKGEK GEAGVVGPAG
PMGPIGPTGP KGELGFPGRP GRPGLNGLRG VKGDRGEAVY GPPGLPGPPG PPGPPGRILY
IKGTVFPVPP RPHCKMPVNT PYPGNQEVLN DHGARANRDS WGLHSSAHLK GEKGDRGAPG
PPGPPLPPSY FSHFINSIKG EKGDNGVTGV KGEKGEPNGG FFLTGPPGPP GRPGLIGPKG
DSVVGPRGPP GLPGLPGLPG YGKIGPPGPP GPPGPPGPPA IYGSAAAMPG PPGPPGEPGS
PATRNLVTTF QNIEGMLEKV HYVAEGTLIY LRETSEVFIR VRKGWRKLQL GELIPIPADS
LPPPAISSHG FQSIPALRPI SNMNNGKPAL HLVALNFPLS GDMRADFQCF RQAQLAGLTS
TYRAFLSSHL QDLATVVRKT DRQHLPIVNL QGETLFNNWE SIFDGNGGQF NIHVPIYSFD
GRNVMTDSSW PQKIIWHGST ANGIRLVSNY CEAWHTADMG AMGQASPLNT GKLLDQKVYS
CNNLFIVLCI ENSFVSDLQR K
//
