ID A0A7L1WCW6_9PASS Unreviewed; 1313 AA.
AC A0A7L1WCW6;
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=COIA1 protein {ECO:0000313|EMBL:NXO95439.1};
DE Flags: Fragment;
GN Name=Col18a1 {ECO:0000313|EMBL:NXO95439.1};
GN ORFNames=CERBRA_R09962 {ECO:0000313|EMBL:NXO95439.1};
OS Certhia brachydactyla (short-toed tree-creeper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Certhiidae; Certhiinae; Certhia.
OX NCBI_TaxID=73330 {ECO:0000313|EMBL:NXO95439.1, ECO:0000313|Proteomes:UP000536092};
RN [1] {ECO:0000313|EMBL:NXO95439.1, ECO:0000313|Proteomes:UP000536092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-20 {ECO:0000313|EMBL:NXO95439.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXO95439.1};
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:NXO95439.1}.
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DR EMBL; VXBV01004210; NXO95439.1; -; Genomic_DNA.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000536092; 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: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; 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:UP000536092};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 6..194
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 193..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..302
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..496
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..560
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..616
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..684
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..826
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..910
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..942
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..965
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..988
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXO95439.1"
FT NON_TER 1313
FT /evidence="ECO:0000313|EMBL:NXO95439.1"
SQ SEQUENCE 1313 AA; 134194 MW; B60ED01FDCE19441 CRC64;
ESLSAEVSLL ELIGDPPTEE IHRIYGPDNN PGYVFGPNAN TGQVARYHLP SPFYRDFSLL
FHIQPTTPRA GVLFAITDSS QNIIYVGVKL SELRAGQQQI IFYYTEPGSP SSYPAATFTV
PTLLNQWTRF AISVEEEEVV LYLDCEEHER VRFERSPDEM ELEEGSGLFV AQAGGADPDK
YQGVIADLKL RGDPRAAERQ CEEEEDDAEV SGDFGSGMEG GQQPSGKVEG VPGLVNAVPV
TSPPVAGGSG PRSGGRSTQQ AERTRAEETL RVSTGGTGRK GEKGEKGERG LKGDSGTGGI
IGPGSVKGQK GEKGDLGIKG SAGFGYPGSK GQKGEPGDPG PPGSLSRHTD GSVVEQVTGP
PGPPGKDGAP GRDGEPGDPG EDGKSGEMGP PGFPGMPGEP GLKGEKGDPG IGPRGPPGPP
GPPGPPGPSS KNDKLTFIDM EGSGFGSDLE TLRGPRGPPG PPGPPGVPGL PGEPGRFGMN
RTDLLGPPGL PGRDGIPGPP GPVGPQGPPG RDGESGQPGP KGEQGDVGDL GLPGLPGPKG
NKGEMGPAGP PGEMGLAGLP GPIGPRGQPG PPGPPGPPGP GYEAGFGDME GSGLSFTPGP
PGPEGPQGVP GLPGVKGEVG SPGQPGLPGP KGDAGMPGVD GRPGLEGFPG PQGPKGDKGS
TGEKGERGQD GVGLPGPPGP PGPPGQVITV SSEDKSLVAF PGPEGRPGHI GLPGPVGPKG
DQGSTGPQGA PGLKGEKGEP GVIISPDGTV VTAKVKGEKG EPGLRGPMGP LGPPGRAGMK
GEIGFPGRPG RPGMNGLKGE KGDPADVLGS RGPPGPPGPP GPPGPPGSIV YNNGNTFSDS
SHPAFPGFHQ FPGQKGEKGD TGPPGPPGQF PYDASHFGTS LRGDKGDAGP KGEKGEPGST
PLYGPGVSGL PGPPGPQGYP GLPGPKGDSI VGPPGPPGPQ GPPGIGYEGR QGPPGPPGPP
GPSSFPGPHR QAVSIPGPPG PPGPPGPPGT SGMSLGLQAL PTYQAMLSTA HELPEGSLIF
LTDRQELYVR LHGGFRRVLL EEHNLIPSSA LDNEVYDKPP TLHYAGPQPR GPLHPLRNHV
PPATARPWRG DEVVANQHRL PEQPLLHHQH ELINGYYIHR RPDPAPVAAH VHQDFQPALH
LVALNTPLSG SMRGIRGADF QCFQQARQVG LAGTFRAFLS SRLQDLYSIV RRADRTTVPI
VNLRDEVLFS NWEALFTGSG APLRTGTHIL SFDGRDVLRD AGWPQKSVWH GSDAKGRRLP
ESYCETWRTE ERAVTGQASS LASGKLLEQA ASSCQHAFIV LCIENSFMTA AKK
//
