ID A0A7K6K1G1_9PASE Unreviewed; 1336 AA.
AC A0A7K6K1G1;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE SubName: Full=COFA1 protein {ECO:0000313|EMBL:NWW06431.1};
DE Flags: Fragment;
GN Name=Col15a1_1 {ECO:0000313|EMBL:NWW06431.1};
GN ORFNames=OREARF_R13526 {ECO:0000313|EMBL:NWW06431.1};
OS Oreocharis arfaki (tit berrypecker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passeroidea; Paramythiidae; Oreocharis.
OX NCBI_TaxID=979223 {ECO:0000313|EMBL:NWW06431.1, ECO:0000313|Proteomes:UP000542358};
RN [1] {ECO:0000313|EMBL:NWW06431.1, ECO:0000313|Proteomes:UP000542358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-029-42 {ECO:0000313|EMBL:NWW06431.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NWW06431.1};
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:NWW06431.1}.
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DR EMBL; VZRR01005874; NWW06431.1; -; Genomic_DNA.
DR Proteomes; UP000542358; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 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:UP000542358};
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..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..569
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..615
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..675
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..738
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..781
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..798
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..864
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..890
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1054
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1073
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWW06431.1"
FT NON_TER 1336
FT /evidence="ECO:0000313|EMBL:NWW06431.1"
SQ SEQUENCE 1336 AA; 139273 MW; 01C3A0E05F3996B9 CRC64;
TERGSKGHLD LTVLIGVPLP PSVYFVTGYG GFPAYSFGPD SNIGRLTSAV IPSPFYRDFA
IVVTVKPNSD RGGALFAITD AFQKTIYLGL RISPVDDSTQ RIIMYYTEPG SPVSREAASF
KVPVMTNRWN RFTVTVEGND VALFMDCEEY QRLQFQRSAR TLVFESGSGI FVGNAGATGL
EKFTGSIQHL TIKSDPRATE DHCEDDDPYA SGDSSGNGSI QEHDVSEAQE ALGSSRLPIG
PEDTLAEPVE APPTILSYLE ENDFSGNHRS EETTEAAKFK EQGTASGFGV FWGGWGSAVM
ETGQGNSEST TVTQKMLREE EGSGAGVLPG VSREEVFNCY VSLTPFLSCS NSTASSPSSF
LLSFLCVPLL HPFLSHALSS CWDVPSQLLQ ITPIPGSVHH KLLIACTRIV CGEVLSGNAH
SNKPVAVTFC AHLSCCCVSV LCWSSTAWLL CFLSRCFVAA TLLEPEESGS GDTDRETEIL
RVSISHNKEL YFTHAMLQHW VLLSCCSFPW EHSGGFLGQG RDCLPSCSPS RTPCTAAPAS
CQPATSAMAK EGLPGPPGPP GLPGLPGKPA PDSGVGPPGS PGEDGTSGEP GPEVNLLSLQ
GPQGPPGRDG VVGPPGWKGE KGDQGLPGSA GPKGDTGVTG SIGPKGEAGP VGSPGKPGPP
GPPGPPGPPG PPGPPGLSYS LGFEVFCYSE ICYNYGYISS RVKAGPKGEK GDPGPRGEPG
QDGNSIVGPP GPPGPPGPVI AIPELLLNDT DGIFNFTEIK GLLGPPGPNG KPGLPGFPGP
RGPKGDAGSP GSQGPKGQQG EKGEPGAIIS ADGSLTELLG RKGEKGEAGV VGPAGPMGPI
GPPGPKGELG FPGRPGRPGL NGLRGVKGDR GEAFNGLPGL PGPPGPPGPP GRILYIKGTV
FPVPPRPHCK MPVNTPYPEN QDVLNDHGPK ANGDSWGLHS SVHLKGEKGD RGAPGPPGPP
LPPSYFSHFI NSIKGEKGDN GVTGVKGEKG EPNGGFFLTG PPGPPGRPGL IGPKGDSVVG
PRGPPGLPGL PGLPGYGKIG LPGPPGPPGP PGPPAIYGSA AAMPGPPGPP GEPGSPATRN
LVTTFQNIEG MLEKVHYVAE GTLIYLRETS EVFIRVRNGW RKLQLGELIP IPADSLPPPA
ISSHGFQSIP ALRPISNMNN GKPALHMVAL NFPLSGDMRA DFQCFRQAQL AGLTSTYRAF
LSSHLQDLAT VVRKTDRNHL PVVNLQGETL FSNWESIFDG NGGQFNIHVP IYSFDGRNVM
MDSSWPQKVI WHGSTANGIR LVSNYCEAWH TADMGAMGQA SPLNTGKLLD QKVYSCNNQF
IVLCIENSFV SDPQGK
//
