ID A0A8C8SJX7_9SAUR Unreviewed; 1579 AA.
AC A0A8C8SJX7;
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:ENSPCEP00000020004.1};
OS Pelusios castaneus (West African mud turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Pleurodira; Pelomedusidae;
OC Pelusios.
OX NCBI_TaxID=367368 {ECO:0000313|Ensembl:ENSPCEP00000020004.1, ECO:0000313|Proteomes:UP000694393};
RN [1] {ECO:0000313|Ensembl:ENSPCEP00000020004.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSPCEP00000020004.1}
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; ENSPCET00000020674.1; ENSPCEP00000020004.1; ENSPCEG00000015472.1.
DR Proteomes; UP000694393; Unplaced.
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; IPR010363; DUF959_COL18_N.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
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:UP000694393};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1579
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034745390"
FT DOMAIN 227..415
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 37..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..430
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..611
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..647
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..672
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..715
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..749
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..759
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..830
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..883
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..937
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1075
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1219
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1579 AA; 161225 MW; 9F484FC0FD4261BB CRC64;
MAPAEQCLFL LLLLTCCCSF AEAQLFGWLW GSQKSPKVTT LSPTGSPATE GQTAESLNSG
VAPSTQAALP ATAQQGDQVW SMPSVTTQEP ATGATRPAWA PPAVPPGKEE NIAGVGAEIL
YVAEGIRSLV QRWDERTIQR PGNTGEPLAA APLTTTHASL AAPSTATGPV GLRNTTANST
GHDHSLPGTR QPDASLPVPT GPPPAWNRTR VLLQKPAAAP PENFSTEVSL LQLIGDPPPQ
QITQVDGPDN SLGYVFSQDA NAGQVARYHL PSPFYRDFSL LFHIQPTTNK AGMLFAITDA
LQTVIYVGVK LSDVKDRKQQ IIFYYTEPGS ERSYVAATFS IPSLVNEWTR FAISVVEDEV
VLYLNCEQFR RVRFERSPDE MELDVGSGLF VAQAGGADPD KYQGVIADLK VTGDSQAAEL
QCEEEEEDTD VASGDFGSGV EDRPHLSGRE QGTPVISWLP KPPPVTAPPT AGETEQAVKN
VSTGSHLQTE QVTVEGPQQV SSGARVGPKG EKGDQGEKGE RGPKGDSGSG GVLATGGTRG
QKGEKGDLGV KGSAGFGYPG SKGQKGEPGA QGSPGPAGPP GPPGTMVQHS DGSMVEQVSG
PPGPTGSPGP PGKDGRPGKD GEPGDPGEDG KPGDTGPQGF PGTPGEPGLK GEKGEPGAGA
RGPPGPPGPP GAPGLSSKQD KLTFIDMEGS GFGGDLDSFR GPPGPPGPPG PPGVPGLPGQ
PGRFGMNSTE LPGPPGLPGL PGRDGIPGPQ GTPGPPGPPG KDGSTGQPGL RGERGDPGDL
GLPGAPGPKG SKGEMGLTGA PGETGLAGLP GPMGPRGLPG PPGPAGPPGP GYEVGFGDME
GSGMPFPSAA PGERGPEGPQ GPPGVPGLKG DSGSPGLPGL PGQKGDHGSP GVDGRPGLEG
FPGPQGPKGD KGSRGTKGER GQDGMGSPGP PGPPGPPGQV IDALSDKKVF GGLPGPEGRE
GHAGFPGPVG PKGDPGSPGF QGAPGPKGEK GEPGVVISPD GTVGAAATRG DKGEQGLVGP
VGATGPHGRP GQKGEIGYPG RPGRPGMNGL KGEKGDTGGL GLQGPPGPPG LPGPPGSIVS
VYDNNAFSES GPPGPPGLPG YQGPPGQKGE RGERGAPGPP GQFPYALSEF GSTFRGDKGD
RGDPGLKGAK GEPGEGGLYG PSISGPPGPQ GYPGPPGPKG ESIRGPPGPP GAQGPPGIGY
EGRPGPPGPP GPPSFPGPHR PTVNIPGPPG PPGPPGPPGT SESSASSGLR ILPTYQAMLS
AAQEVPEGGL IFLPDREELY IRVRSGFRRV QLEERTLISS RGLENEVYDR PPSDPYSQGG
TASSGSHQHG PLHPHREHNP YPTSRPWRGD DSIANHHRLP DQPSIHHSHH GAQPQREPLD
GLSPDRREES VPSAVHMHHD FQPALHLVAL NTPLSGSMRG IRGADFQCFQ QARAVGLTGT
FRAFLSSRLQ DLYSIVRRAD RGGVPIVNLR DEMLFNDWEA LFSGTEAQFR AGGRILSFDG
RDVLRDSAWP QKSVWHGSDA KGRRLTESYC ETWRTDDSVV TGQASPLGGG KLLEQRASSC
QNAFIVLCIE NSFMTSSKK
//
