ID A0A493T9T8_ANAPP Unreviewed; 1350 AA.
AC A0A493T9T8;
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:ENSAPLP00000022415.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSAPLP00000022415.1};
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:ENSAPLP00000022415.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000022415.1, 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:ENSAPLP00000022415.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSAPLP00000022415.1}
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; ENSAPLT00000038777.1; ENSAPLP00000022415.1; 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..1350
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019836241"
FT DOMAIN 33..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 82..220
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 222..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..327
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..391
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..496
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..608
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..715
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..860
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..891
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..976
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1003
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1022
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1350 AA; 137640 MW; 9089D88CB5418615 CRC64;
MRPRCPPRWL PLLGLFVLLL PAASQEHENL 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
//
