ID A0A493TGA6_ANAPP Unreviewed; 1482 AA.
AC A0A493TGA6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSAPLP00000024931.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSAPLP00000024931.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000024931.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000024931.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000024931.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSAPLP00000024931.1}
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 STRING; 8840.ENSAPLP00000024931; -.
DR Ensembl; ENSAPLT00000019431.1; ENSAPLP00000024931.1; ENSAPLG00000019001.1.
DR GeneTree; ENSGT00940000158212; -.
DR OMA; VQDQHQN; -.
DR Proteomes; UP000016666; 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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0001525; P:angiogenesis; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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:SF1034; COLLAGEN ALPHA-1(XVIII) 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:UP000016666};
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_5019850761"
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..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..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 71..106
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 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 1009..1023
FT /note="Low complexity"
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; 150660 MW; 78810367E7AFD72E CRC64;
MAPHRLGLLL LLASCCFSSS EAQLLDWIWG SSKTTGTPAA PSTAATTSQL AEPSPTLGTA
AQRQDPATGD PTATTQQHQE QDPSTAAPTG QESAEGTEQW DRSSAGTAAP TSVAWTAAPP
SSTPPTQLPA GTGHPDATQP PRQPEGTGVS PQKLAAARPE NLSAEVSLLE LIGDPPPEEI
LKIYGPDNNP GYVFGPNANT GQVARYHLPS PFYRDFSLLF HIQPTTPRAG VLFAVTDSSQ
SIIYVGVKLS ELQAGKQRII FYYTEPGSPS SYTAATFTVP TLLNQWTRFA ISVEEDEVVL
YLDCEEYERV RFERSPDEME LEQGSGLFVA QAGGADPDKY QGVIADLKLR GDPRAAEHQC
EEEEDDAEAS GDFGSGAEDR RQPSGKDGGV PGLVDAVPVT SPPVAADGGS GRSLGSPQQA
ERTRAEERLR VPAGGPKGEK GEKGERGLKG DSGTGGVLGT GSTKGEKGQK GELGTKGSAG
FGYPGSKGQK GEPGEPGPPS RHSDGAVLEP VTGPPGPSGP PGLPGKEGPP GRDGEPGDPG
EDGKPGVMGP QGFPGTPGEP GMKGEKGDPG VGPRGPPGLP GPPGPPGPSS KQDRLTFIDM
EGSGFGGDLE TVRGPRGPPG PPGPPGVPGL PGEPGRFGMN STDLPGPPGL PGRDGVPGTP
GPEGPQGPPG KDGMPGPPGP KGERGDVGDL GLPGAPGPKG SKGDTGPAGA PGETGLAGLP
GPIGPRGPPG PPGPPGPPGP AYEAGFADME GSGLPLAAGS PGPRGPDGPQ GVPGLPGIKG
EVGSPGQPGV PGPKGDAGVP GVDGRPGLEG FPGPQGPKGD RGSPGEKGER GQDGVGLPGP
PGPPGPPGQV VYVSGEDRSL AAVPGPEGRP GHAGFPGPVG PKGDQGSPGL QGSPGLKGEK
GEPGVIISPD GTIIAANVKG EKGEPGLRGP MGPSGPHGRA GLKGEIGFPG RPGRPGMNGL
KGEKGDPADI SGMLGLRGPP GPPGPPGPPG PPGSIVYDSN NAFSDASRPA LPAFPGFPQF
PGQKGEKGDV GAPGPPGQFP YDLSHFGASL RGDKGEAGPK GEKGEPGGTS LYGPSVMGPP
GPQGYPGLPG PKGDSIVGPP GPPGPQGPPG IGYEGRQGPP GPPGPPGPPS FPGPHRPAIS
IPGPPGPPGP PGPPGSSGTS LGLRALPTYQ AMLSAAHELP EGGLVFVADR QELYVRLRGG
FRRVLLEEHT LVPSSALDNE VYDKPPSVHY GGSPHPLQPR GPLHPLRNHS PPPTARPWRG
DEVVANQHRL PQTPLLQQHE LLNSYYVQRR PEPAPVAAHV HQDFQPALHL VALNAPLSGG
MRGIRGADFQ CFQQARQVGL AGTFRAFLSS RLQDLYSIVR RADRATVPIV NLRDEVLFSN
WEALFTGSEA PLRADARILS FDGRDVLRDS AWPQKSVWHG SDAKGRRLPE SYCEAWRTEE
RGTSGQASSL SSGKLLEQAA SSCQHAFIVL CIENSFMTAA KK
//
