ID A0A8C3B7G1_CAIMO Unreviewed; 1482 AA.
AC A0A8C3B7G1;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSCMMP00000001097.1};
OS Cairina moschata (Muscovy duck).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Cairina.
OX NCBI_TaxID=8855 {ECO:0000313|Ensembl:ENSCMMP00000001097.1, ECO:0000313|Proteomes:UP000694556};
RN [1] {ECO:0000313|Ensembl:ENSCMMP00000001097.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Vignal A., Thebault N., Warren W.C.;
RT "Common duck and Muscovy duck high density SNP chip.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCMMP00000001097.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCMMP00000001097.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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}.
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DR Ensembl; ENSCMMT00000001233.1; ENSCMMP00000001097.1; ENSCMMG00000000683.1.
DR Proteomes; UP000694556; Chromosome 7.
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 CDD; cd00110; LamG; 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:SF1060; COLLAGEN ALPHA-1(IV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 5.
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 Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000694556};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1482
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034133484"
FT DOMAIN 165..353
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 214..352
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 34..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..120
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..369
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..459
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..588
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..628
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..740
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..847
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1482 AA; 150579 MW; F7BF31C6D8B7CCC5 CRC64;
MAPHRLGLLL LLASCCFSSS EAQLLDWIWG SSKTTGPPAA PSTAATASRL AEPSPTPGTA
AQRRDPAAGD PTATTQQHQE QDPSTAAPTG RESAEGTEQW DGSSAGTAAP TSVAWTAAPP
SSTPPAQLPA GTGLPDATQP PRQPEGTGVS PQKPAAARPE NLSAEVSLLE LIGDPPPEEI
LKIYGPDNNP GYVFGPNANT GQVARYHLPS PFYRDFSLLF HIQPTTPRAG VLFAVTDSSQ
SIIYVGVKLS DLQAGKQRII FYYTEPGSPS SYAAATFTVP TLLNQWTRFA ISVEEDEVVL
YLDCEEYERV RFERSPDEME LEQGSGLFVA QAGGADPDKY QGVIADLKLR GDPRAAEHQC
EEEEDDAEAS GDFGSGAEDR RQPSGKDRGV PGLVDAVPVT SPPVAADGGS GSSSGSPQQA
ERTRAEERLR VPAGGPKGEK GEKGERGLKG DSGTGGVLGT GSTKGEKGQK GELGIKGSAG
FGYPGSKGQK GEPGEPGPPS RHSDGAVLEP VTGPPGPSGP PGLPGKEGAP GRDGEPGDPG
EDGKPGVMGP QGFPGTPGEP GMKGEKGDPG VGPRGPPGLP GPPGPPGPSS KQDRLTFIDM
EGSGFGGDLE TVRGPRGPPG PPGPPGVPGL PGEPGRFGMN STDLPGPPGL PGRDGVPGTP
GPEGPQGPPG KDGMPGPPGP KGERGDVGDL GLPGAPGPKG SKGDTGPAGA PGEMGLAGLP
GPIGPRGPPG PPGPPGPPGP AYEAGFADME GSGLPLAAGS PGPRGPDGPQ GVPGLPGIKG
EVGSPGQPGV PGPKGDAGVP GVDGRPGLEG FPGPQGPKGD RGSPGEKGER GQDGAGLPGP
PGPPGPPGQV IYISGEDRSL GAVPGPEGRP GHAGFPGPVG PKGDQGSPGL QGSPGLKGEK
GEPGVIISPD GTIIAANVKG EKGEPGLRGP MGPSGPHGRA GLKGEIGFPG RPGRPGMNGL
KGEKGDPADI SGMLGLRGPP GPPGPPGPPG PPGSIVYDSN NAFSDASRPA LPAFPGFHQF
PGQKGEKGDV GAPGPPGQFP YDLSHFSASL RGDKGEAGPK GEKGEPGGTA LYGPSVMGPP
GPQGYPGLPG PKGDSIVGPP GPPGPQGPPG IGYEGRQGPP GPPGPPGPPS FPGPHRPAIS
IPGPPGPPGP PGPPGSSGTS LGLRALPTYQ AMLSAAHELP EGGLVFLADR QELYVRLRGG
FRRVLLEEHT LVPSSALDNE VYDKPPSVHY GGSQHPLQPR GPLHPLRNHS PPPTARPWRG
DEVVANQHRL PQPPLLQQHE LLNSYYVQRR PEPAPVAAHV HQDFQPALHL VALNAPLSGG
MRGIRGADFQ CFQQARQVGL AGTFRAFLSS RLQDLYSIVR RADRATVPIV NLRDEVLFNN
WEALFTGSEA PLRADARILS FDGRDVLRDS AWPQKSVWHG SDAKGRRLPE SYCEAWRTEE
RGTSGQASSL SSGKLLEQAA SSCQHAFIVL CIENSFMTAA KK
//
