ID A0A493SUW9_ANAPP Unreviewed; 1370 AA.
AC A0A493SUW9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSAPLP00000017362.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSAPLP00000017362.1};
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:ENSAPLP00000017362.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000017362.1, 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:ENSAPLP00000017362.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSAPLP00000017362.1}
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; ENSAPLT00000038542.1; ENSAPLP00000017362.1; ENSAPLG00000019001.1.
DR GeneTree; ENSGT00940000158212; -.
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: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; IPR001791; Laminin_G.
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; 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1370
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019776929"
FT DOMAIN 53..241
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 102..240
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 242..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..257
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..347
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..628
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..735
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..880
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..911
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..996
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1023
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1042
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1370 AA; 139847 MW; C3FD25AF6691AD5A CRC64;
MRPRCPPRWL PLLGLFVLLL PAASQEHGWA RAIGKRLPRD ERAGSQTENL SAEVSLLELI
GDPPPEEILK IYGPDNNPGY VFGPNANTGQ VARYHLPSPF YRDFSLLFHI QPTTPRAGVL
FAVTDSSQSI IYVGVKLSEL QAGKQRIIFY YTEPGSPSSY TAATFTVPTL LNQWTRFAIS
VEEDEVVLYL DCEEYERVRF ERSPDEMELE QGSGLFVAQA GGADPDKYQG VIADLKLRGD
PRAAEHQCEE EEDDAEASGD FGSGAEDRRQ PSGKDGGVPG LVDAVPVTSP PVAADGGSGR
SLGSPQQAER TRAEERLRVP AGGPKGEKGE KGERGLKGDS GTGGVLGTGS TKGEKGQKGE
LGTKGSAGFG YPGSKGQKGE PGEPGPPSRH SDGAVLEPVT GPPGPSGPPG LPGKEGPPGR
DGEPGDPGED GKPGVMGPQG FPGTPGEPGM KGEKGDPGVG PRGPPGLPGP PGPPGPSSKQ
DRLTFIDMEG SGFGGDLETV RGPRGPPGPP GPPGVPGLPG EPGRFGMNST DLPGPPGLPG
RDGVPGTPGP EGPQGPPGKD GMPGPPGPKG ERGDVGDLGL PGAPGPKGSK GDTGPAGAPG
ETGLAGLPGP IGPRGPPGPP GPPGPPGPAY EAGFADMEGS GLPLAAGSPG PRGPDGPQGV
PGLPGIKGEV GSPGQPGVPG PKGDAGVPGV DGRPGLEGFP GPQGPKGDRG SPGEKGERGQ
DGVGLPGPPG PPGPPGQVVY VSGEDRSLAA VPGPEGRPGH AGFPGPVGPK GDQGSPGLQG
SPGLKGEKGE PGVIISPDGT IIAANVKGEK GEPGLRGPMG PSGPHGRAGL KGEIGFPGRP
GRPGMNGLKG EKGDPADISG MLGLRGPPGP PGPPGPPGPP GSIVYDSNNA FSDASRPALP
AFPGFPQFPG QKGEKGDVGA PGPPGQFPYD LSHFGASLRG DKGEAGPKGE KGEPGGTSLY
GPSVMGPPGP QGYPGLPGPK GDSIVGPPGP PGPQGPPGIG YEGRQGPPGP PGPPGPPSFP
GPHRPAISIP GPPGPPGPPG PPGSSGTSLG LRALPTYQAM LSAAHELPEG GLVFVADRQE
LYVRLRGGFR RVLLEEHTLV PSSALDNEVY DKPPSVHYGG SPHPLQPRGP LHPLRNHSPP
PTARPWRGDE VVANQHRLPQ TPLLQQHELL NSYYVQRRPE PAPVAAHVHQ DFQPALHLVA
LNAPLSGGMR GIRGADFQCF QQARQVGLAG TFRAFLSSRL QDLYSIVRRA DRATVPIVNL
RDEVLFSNWE ALFTGSEAPL RADARILSFD GRDVLRDSAW PQKSVWHGSD AKGRRLPESY
CEAWRTEERG TSGQASSLSS GKLLEQAASS CQHAFIVLCI ENSFMTAAKK
//
