ID A0A851JSI0_9PASS Unreviewed; 1311 AA.
AC A0A851JSI0;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE SubName: Full=COFA1 protein {ECO:0000313|EMBL:NXB81034.1};
DE Flags: Fragment;
GN Name=Col15a1_1 {ECO:0000313|EMBL:NXB81034.1};
GN ORFNames=DONATR_R09963 {ECO:0000313|EMBL:NXB81034.1};
OS Donacobius atricapilla.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Mimidae; Donacobius.
OX NCBI_TaxID=237420 {ECO:0000313|EMBL:NXB81034.1, ECO:0000313|Proteomes:UP000660704};
RN [1] {ECO:0000313|EMBL:NXB81034.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B10K-DU-001-63 {ECO:0000313|EMBL:NXB81034.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXB81034.1};
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:NXB81034.1}.
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DR EMBL; WBMY01016137; NXB81034.1; -; Genomic_DNA.
DR Proteomes; UP000660704; 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; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1118; LAMININ G DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000660704};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 425..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..196
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 57..195
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 193..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..568
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..586
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..646
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..703
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..713
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..756
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..773
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..864
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1029
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1048
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXB81034.1"
FT NON_TER 1311
FT /evidence="ECO:0000313|EMBL:NXB81034.1"
SQ SEQUENCE 1311 AA; 139021 MW; 7313983D1BBDE21E CRC64;
TERGSKGHLD LTELIGVPLP PSIYFVTGYG GFPAYSFGPD SNIGRLTSAI IPSPFYRDFA
VVVTVKPNSD HGGVLFAITD AFQKTIYLGL RISPVDDSTQ RIIMYYTEPG SHISREAASF
KVPVMTNRWN KFTVTVEGND IALFMDCEEY QRLQFQRSAQ TLVFESGSGI FVGNAGATGL
QKFTGSIQHL TIKSDPRATE DHCEDDDPYA SGDSSGNGSH QEYDAPEAQE ALAPSHLPIR
PEDTLAEPVE APPTILSYLE ENDFSGNHRP EETTEAAKFK EQGTASGFWD VAVMETGQGN
SESTTVTQKM FREEDGSGAG VLPGANRGEV APSVKLIIPF IFLTKQYRFH KFTIMTHINF
IYSDSFERIR NNFKGKIRLQ YRNQVMRLHG NPPSLCPVVM ERYVKQRVLI NCREVKACGA
VREHLWYILM GTLLLSSGTC LGYVNFIMQV LYMLNLQHPE RICRIFFQGQ KGVCAYKCGR
SMRQEVANKE ITARGLFKMR KWFLSDYEKT VNRREMGIID SQTHKKTLNG LPGPPGPPGL
PGLPGKPAPD SGVGPPGSPG EDGASGEPGP EGPQGPPGRD GVVGPPGWKG EKGDQGLPGS
AGAKGDTGVT GSIGPKGETG PIGSPGKPGP PGPPGPPGPP GPPGPPGLTY GLGFEQGRAH
FIISPFKSLM LIFFFNHLQG PKGEKGDPGP RGEPGPNGNS VVGPPGPPGP PGPIIAIPEL
LLNDTDGHFN FTEIKGLLGP PGPDGKPGLP GFPGPRGPKG DTGLPGSQGP KGQQGEKGEP
GAIISADGSL TELLGRKGEK GEAGVVGPVG PMGPRGPTGP KGELGFPGRP GRPGLNGLRG
VKGDRGEASN GLPGLPGPPG PPGPPGRILY IKGTVFPVPP RPHCKMPVNT PYPGNQELLS
DHGAKANRDS WGLHSSAHLK GEKGDRGAPG PPGPPLPPSY FSHFINSIKG EKGDSGVTGV
KGEKGEPNGG FFLTGPPGPP GRPGLIGPKG DSIVGPRGPP GLPGLPGLPG YGKIGPPGPP
GPPGPPGPPA IYGSAAAMPG PPGPPGEPGS PATRNLVTTF QNIEAMLEKV HYVAEGTLIY
LRETSEIFIR VQRGWRKLQL GELIPIPADS LPPPAISSHG FQSIPALRPL SNMNNGKPAL
HLVALNFPLS GDMRADFQCF RQAQLAGLTS TYRAFLSSHL QDLATVVRKT DRHHLPIVNL
QGETLFSNWE SIFDGNGGQF NIHVPIYSFD GKNVMTDSSW PQKIIWHGST ANGIRLVSNY
CEAWHTADMG AMGQASSLNT GKLLDQKVYS CNNLFIVLCI ENSFVSDPQG K
//
