ID A0A3P8WPN2_CYNSE Unreviewed; 1437 AA.
AC A0A3P8WPN2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE SubName: Full=Collagen type XVIII alpha 1 chain a {ECO:0000313|Ensembl:ENSCSEP00000026635.1};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000026635.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000026635.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278; DOI=10.1038/ng.2890;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000026635.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCSEP00000026635.1}
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR Ensembl; ENSCSET00000026988.1; ENSCSEP00000026635.1; ENSCSEG00000017010.1.
DR GeneTree; ENSGT00940000158212; -.
DR InParanoid; A0A3P8WPN2; -.
DR OMA; NQWKGER; -.
DR Proteomes; UP000265120; Chromosome 16.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
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; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
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; 1.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; 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:UP000265120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 247..374
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..34
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..218
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..368
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..764
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..833
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..850
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..946
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1082
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 262..308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 299..337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1437 AA; 152651 MW; A2BD3D669D05CB72 CRC64;
MGVGSADFNP LRFSGLEADR GSGLWSGSGE SSRSGFEEEA KADWFSGSDT HEFLEVNDRE
AVLTTDGVTL PDNYRNESNK SHLIIHRAEK VNASDESSQN LRSLLEIPVN NSVNYSPENS
TSVDLLIPLN DTVSNLDSRG RQLTPVTDLP VTTQEPVVYQ SVPTSQASTV SQRFQTAITA
AQREDSTSTL ATSHTAATST AAAQREESTS TLATSHTLAA RPSLATSSQQ LTTVSKDVKT
GGDRAVTESQ RCVLLSEPLP FCSFTKGEKI LVPNFVNQTS VEEVRALLTE WAWLLGSNCH
HGVQWFFCLL LVPKCDPAGA LPLLPCRSFC EVLRDSCWML LDEGRLPVEC HTLPDDDDDG
DDGDDDDGYQ CLSPSNQKED SGVSLLQLIG DPPPSEITQV YGPDNSPGYV FGPDANTGQL
ARAHLPSPFY RHFSLIFNVK PTSDRGGVLF SVTDVPQQIM YVGVKLSAVQ GNHQNVILYY
TEPGSERSYE AASFRVHSMR DTWTRFAIAV RDDKVMFYLN CDTDPQVSRI ERSPDEMELD
AGAGVFVGQA GGADPDKFLG VIGELRVVGD PRAAERHCEE DEDDSDMPVL INTSSPLMIM
KDTCLHTAPL RSLMVTTLYY QGSAGFGYQG TKGDRGLPGP PGLPGPPGPT PDYLLTNDGT
VVPAGPRGPP GPPGPQGPVG ADGEPVSDEK KLLMSSVTSI YKYICAVNVS VMSVIIRSCT
VGSNRLHLLH PCRTFVDMEA SGFPDLESVR GLPGPPGPPG PPGLPGISTA STVLSSGAFG
PPGKDGAPGQ PGLPGLPGTD GSPGVPGAKG EKGSRGDPGL SGPSGQSGLA GLPGPMGPVG
PPGPPGPPGP SYRVGFVSTV DVPSSRSEDF TLCFCPPAPQ GKPGFPGLPG QKGSEGPVGK
DGQPGLDGFP GPQVKDNVLE GWSGQTGEPG RDGSGFPGPP GPPGPPGQVV YSTSGNVCLF
VCVQGEKGEP GLVIAPDGNL LEGLRGAKVS PGLFGPVGDT GPSGPGHYGP PGIKGEIGMP
GRPVSVFISC PENIYILTGT GPKGDYVIGP PGPQGPPGTP GVGYDGRPGA PGPPGPPGPP
GSYPGAYRPN HGECRFKPGP SVTVLKSYDT MIATARRQTE GSLIYIIDKA DLYLRVRDGL
RQVMVRTWTP KYDHNEVAEV QPPPVILYPQ SQDQSHNNGA GHYSQSSPVI RPLEPPLHLP
EDPKPPPHYD PRFPDPRHTG HTDQTLVTQR VESRYPVTPQ RRPSPPLWSP GSSSNKPPSP
PQLHLIALNA PQSGNMRGIR GADFLCFQQA RAVGLKGTFR AFLSSKLQDL YTIVRGSDRD
HLPILNLKDQ VLFSSWSSVF GDRADRMREN VPIYSFDGRD IIRDSAWPEK MVWHGSDVHG
QRQTDHYCET WRAGDRAVTG LASSLQSGLL LQQTSSSCSG SYVVLCIENA LISQSKK
//
