ID A0A7K8MA63_9CORV Unreviewed; 1335 AA.
AC A0A7K8MA63;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE SubName: Full=COFA1 protein {ECO:0000313|EMBL:NXE38162.1};
DE Flags: Fragment;
GN Name=Col15a1_0 {ECO:0000313|EMBL:NXE38162.1};
GN ORFNames=PTILEU_R10905 {ECO:0000313|EMBL:NXE38162.1};
OS Ptilorrhoa leucosticta.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Corvoidea; Cinclosomatidae; Ptilorrhoa.
OX NCBI_TaxID=449384 {ECO:0000313|EMBL:NXE38162.1, ECO:0000313|Proteomes:UP000547721};
RN [1] {ECO:0000313|EMBL:NXE38162.1, ECO:0000313|Proteomes:UP000547721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-CU-031-17 {ECO:0000313|EMBL:NXE38162.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXE38162.1};
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:NXE38162.1}.
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DR EMBL; VWYY01000439; NXE38162.1; -; Genomic_DNA.
DR Proteomes; UP000547721; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 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:UP000547721};
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..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..596
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..614
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..653
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..673
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..797
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..863
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..889
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..962
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1053
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1072
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXE38162.1"
FT NON_TER 1335
FT /evidence="ECO:0000313|EMBL:NXE38162.1"
SQ SEQUENCE 1335 AA; 140055 MW; 791AAB1708FE8448 CRC64;
TERGPKGHLD LTELIGVPLP PSVYFVTGYG GFPAYNFGPD SNIGRLTSAI VPSPFYRDFA
IVATVKPNSD RGGVLFAITD AFQKTIYLGL RISPVDDSTQ RIIMYYTEPG SHISREAASF
KVPVMTNRWN KFTVTVEGNN AALFMDCEEY QRLQFQRSAR TFVFESGSGI FVGNAGATGL
EKFTGSIQHL TIKSDPRATE DHCEDDDPYA SGDSSGNGSI QEHDISEAQE ALGSSRLPIG
PEDMLAEPVE APPTILSYLE ENDFSGNHRS EETSEAAKFK EQGTASGFGV SWGVGPYSAV
METGQGNSES TTVTQKMLRE EDGSGAGVLP GVSREKVLLL LPRCRIWHLF CLMLLITAQC
SNLSRSLCKA SCPSGESTAP PNLKSSANLV MVHSTPASRS LINILTRTNP RIDPQGTPLM
TDHQPDVTLF TAILELCPSA MNHHTWMKSW NCTALHTLTI YTSTRWVLAQ QLRSILPALH
MDQWLHRGLV SDSRQKAKAN SCRANVQMVS GKQFHQLPGQ SCSTLPAVRF ESVQRCRTDR
PPSVASLYPG CFTLQILGLP GPPGPPGLPG LPGKPAPDSG VGPPGSPGED GASGEPGPEG
PQGPPGRDGV VGPPGWKGEK GDQGLPGSAG PKGDTGVTGS IGPKGESGPI GSPGKPGPPG
PPGPPGPPGP PGLPGLSYSL GFEVICYSEV CCNYGYISSR GKTGPKGEKG DPGPRGEPGQ
DGNSIVGPPG PPGPPGPVIA IPEFLLNDTD GIFSFTEIKG LLGPPGPDGK SGLPGFPGPR
GPKGDTGLPG SQGPKGQQGE KGEPGAIISA DGSLTELLGR KGEKGEAGMV GPAGPMGPRG
PTGPKGELGF PGRPGRPGLN GLRGVKGDRG EAFNGLPGLP GPPGPPGPPG RILYIKGAVF
PVPPRPHCKM PVNTPYPGNQ KVLSDHDAKA NRDSWELHSS AHLKGEKGDR GAPGPPGPPL
PPSYFSHFIN SIKGEKGDNG VTGVKGEKGE PNGGFFLTGP PGPPGRPGLI GPKGDSVVGP
RGPPGLPGLP GLPGYGKIGP PGPPGPPGPP GPPAIYGSAA AMPGPPGPPG EPGSPATRNL
VTTFQNIEGM LEKVHYVAEG TLIYLRETSE VFIRVRNGWR KLQLGELIPI PTDSLPPPAI
SSHGFQSIPA LRPISNTNNG KPALHLVALN FPLPGDMRAD FQCFQQAQLA GLTSTYRAFL
SSHLQDLATV VRKADRHHLP VVNLQGETLF SNWESIFDGN GGQFNIHVPI YSFDGRNIMT
DSSWPQKVIW HGSTANGIRL VSNYCEAWHT ADMGAMGQAS PLNTGKLLDQ KVYSCNNQFI
VLCIENSFVS DPQGK
//
