ID A0A8X7WYR2_POLSE Unreviewed; 1287 AA.
AC A0A8X7WYR2;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE SubName: Full=COFA1 protein {ECO:0000313|EMBL:KAG2458303.1};
DE Flags: Fragment;
GN Name=Col15a1 {ECO:0000313|EMBL:KAG2458303.1};
GN ORFNames=GTO96_0018239 {ECO:0000313|EMBL:KAG2458303.1};
OS Polypterus senegalus (Senegal bichir).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Polypteriformes; Polypteridae; Polypterus.
OX NCBI_TaxID=55291 {ECO:0000313|EMBL:KAG2458303.1, ECO:0000313|Proteomes:UP000886611};
RN [1] {ECO:0000313|EMBL:KAG2458303.1, ECO:0000313|Proteomes:UP000886611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bchr_013 {ECO:0000313|EMBL:KAG2458303.1};
RX PubMed=33545088;
RA Bi X., Wang K., Yang L., Pan H., Jiang H., Wei Q., Fang M., Yu H., Zhu C.,
RA Cai Y., He Y., Gan X., Zeng H., Yu D., Zhu Y., Jiang H., Qiu Q., Yang H.,
RA Zhang Y.E., Wang W., Zhu M., He S., Zhang G.;
RT "Tracing the genetic footprints of vertebrate landing in non-teleost ray-
RT finned fishes.";
RL Cell 0:0-0(2021).
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:KAG2458303.1}.
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DR EMBL; JAATIS010007298; KAG2458303.1; -; Genomic_DNA.
DR Proteomes; UP000886611; 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; 5.
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:UP000886611};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1287
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036474764"
FT DOMAIN 36..224
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 224..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..251
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..382
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..395
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..499
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..531
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..590
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..603
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..850
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..998
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1021
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAG2458303.1"
FT NON_TER 1287
FT /evidence="ECO:0000313|EMBL:KAG2458303.1"
SQ SEQUENCE 1287 AA; 132618 MW; 5EC87445E36BC767 CRC64;
MALGDCRGPL ALLLILWSCH LSEAAQVLEE RGSRGHLDLT ELIGVPLPPS VSFITGYEGF
PAYSFGQDAN IGRLTKTFIP QPFYRDFAVI VTIKPTTNRG GVLFAITDAF QKIIYLGIEL
TPVEDDTQRI IMYYTESSTS KSQQVASFKV QEMTNKWNRF TLAVQDNKIT LFMDCEEYHR
ILFERTSQQL QFESSSGIFV GNAGGTGRPK FIGSIQQLLI KPDPRAAEEQ CEDDDPYASG
DESGDSPQEE INVDEAKKNV EEVEYFPSPS ELEHSVPVPA PPTEVSIIKE TDEFSGGLST
PTEQLLISSA IPEHTDEVGL ESSVSQKEVP RERGHGVDAS HGEKTESSSF RFGPKGEKGD
PGPPGPPGPS GQPGQSNGVT PLAGPPGPAG PPGQPGTPGR DGQPGLSGKD GLPGEKGPQG
FPGLPGESGI KGEKGDPGVG LPGPPGPPGA PGRAFSYRLM NENDAEGSGL RDIDSDAEIM
RGPPGPPGPP GKPGPPGPSN PGGSLNDAVT GPPGPPGIPG KDGAPGKPGL PGFHGPPGRN
GSIGPKGEHG DKGDIGPQGL PGEKGDPGMP GEAGPPGLSG TQGQTGLPGP QGLPGPPGPP
GPPGRGYNFG LEDLEGSTAF GGLSEPGPRG PPGIAGLPGP VGSKGEQGDI GPPGATGQKG
EPGLTGVDGL PGIAGQPGPV GQKGEMGDKG QRGERGLDGV SITGPPGPPG PPGPVISLQD
FMLNDTDGIF NFTGIQGPPG PPGPRGPKGD HGFPGVQGPP GVKGEKGEPG VVIAADGSMM
TGVIGPKGMK GDRGMSGPHG PMGPSGAKGE FGFPGRPGRP GMTGKKGEKG EVLNIQGPPG
PPGPPGPPGP CLSIKGTVFP VPPRLHCKTP VNGNEETDRT LSFSVIKGQK GSLGTNGRKG
EKGANGTPGK PGPADSLLPD DFKGDKGDAG YKGDKGEKGE AGLPGPPGLP GRSGLVGPKG
EAVIGPRGPP GFPGLPGPPG FGRPGPPGPP GPPGPPGPSS MFGSSIPLPG PPGPPGQPGP
PGIGTSNAVI TYRNLEGLLR DSYRTAEGTL IYITDKSELY IRVRQGWRKV QLGDLIPITG
DSPPLPGSPV LEMQSFLPGH SLLSHTVHTH PGLHLVALNA PLSGDMMGIR GADNQCFQQA
RAMGLVATYR AFLSSQLQDL ATIVKKADRF NTPIVNLKGE ILFNNWMEIF ATNGQFNPQI
PIYSFDGRNV LTDPSWPQKM IWHGSSPGGI RLMSSYCEAW RAGDMAVTGQ ASFLQRGRLL
EQHTRSCSNN FIVLCIENSY LQDHRRK
//
