ID A0A6P6BWM7_PTEVA Unreviewed; 1250 AA.
AC A0A6P6BWM7;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|RefSeq:XP_023379523.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_023379523.1};
OS Pteropus vampyrus (Large flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Pteropodinae; Pteropus.
OX NCBI_TaxID=132908 {ECO:0000313|Proteomes:UP000515202, ECO:0000313|RefSeq:XP_023379523.1};
RN [1] {ECO:0000313|RefSeq:XP_023379523.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_023379523.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR RefSeq; XP_023379523.1; XM_023523755.1.
DR AlphaFoldDB; A0A6P6BWM7; -.
DR GeneID; 105305970; -.
DR KEGG; pvp:105305970; -.
DR CTD; 80781; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000515202; 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 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 InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000313|RefSeq:XP_023379523.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Reference proteome {ECO:0000313|Proteomes:UP000515202};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 166..350
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 362..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..395
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..634
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..710
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..740
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..982
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1006
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1057
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1081
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 125837 MW; A9CA46599E036BB0 CRC64;
MTPLLCVPAS VPFLCPRPQR MALRLAQHRA RCRAVGLVSG AALPQETGGG GPRVCTARGP
VCAGPSAGSQ HSRCRDPVTP WSAFPGRTRV VLVGSRRLWQ DCLCVWTSAD ETPAVAGGRR
ALDADPGPQS GRGRGRGLAL TLLRTQLPYL LTDLRSARVT KSVGAEVGLL QLLGEPPPQH
VTQVDDPDVG PAYVFGPDAS SGQAARAHLP SPFFRDFSLL FYVRPATEGA GVLFAITDAA
QAVVSVGVKL SSVRDGHQHV QLLYTEPGTA QTRTAASFRL PAFTGQWTRL ALSVDGDTVA
LFVDCEELQR VPLARSPQRL QLEPGAGLFV AQAGAADPDS FQERKLVVPV FSARCWYRRA
RMGPAHQRRS ATSGGVLGSS PEVDLAPRAA AAGGASPPPA GRAPRHCSPL VSVTPQASGD
FGSGLQESPE LAGEEVGMSS QPGLPEAPPA TSPPLAGGSN SEDSRTEEIE EETTASSLGA
QTLPGSHTVA TGDGNIWSPG DSLEEDPAGP VVRGPDARLV PGPQGPPGPP GKDGAPGRDG
EPGDPGKDGR PGDTGPQGFP GTPGDVGPKG EKGDPGVGPR GPPGPQGPPG PPGPSFRQDK
LTFIDMEGSG FGGDLESLRG PRGFPGPPGP PGVPGLPGQP GRFGVNSSAT PGPAGLPGVP
GRDGHPGLPG PPGPPGSPGR DGRPGETGQK GSLGAEGAPG PKGSKGDPGP IGAPGVNGLT
GAPGPAGPPG PPGPPGPPGP GLAAGFDDME GSGGPFWPTA RGADGLQGPP GQPGAKGDPR
RRPPGAASLL ARGRLSQKTE GRGARSRPPS GFRRWPVGLA VGTRRGGTAV VTWPFFLSAA
PRALPLPRWE KMVAGAHGAK GQPGFAGFPG PAGPKGNLGS RGQQGPPGVK GEKGEPGMVY
GPDGRGLAPA HKGAKGEPGP RGPPGPYGRP GHKGEIGFPG RPGRPGMNGF KGEKGEPGDA
SVGFGVQGPP GPPGPPGPPG LPGTPVYDSN AFMESGPPGP PGPPGHQGPS GPKGDKGEVG
SPGAPGQFPL DLFQLGSEMK GEKGDRGHTG QKGERGEPGA GGFFGSSIPG PPGPPGYPGI
PGPKGESTPG QPGPPGPRGP PGVGYEGRQG PPGPPGPPGP PGPPSFPGPY RQTISVPGPP
GPPGPPGPPG TMGTASGVRI WPTYQTMLDR VPELPEGWLV FVAEGEELYV RVRDGFRKVL
LGARTPLPRG TVSPHLPTPA GFGTHVPAFQ MAGAHVVCDS GRLHCLMVLE
//
