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Database: UniProt
Entry: A0A674NV85_TAKRU
LinkDB: A0A674NV85_TAKRU
Original site: A0A674NV85_TAKRU 
ID   A0A674NV85_TAKRU        Unreviewed;      1605 AA.
AC   A0A674NV85;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   SubName: Full=Collagen alpha-1(XVIII) chain-like {ECO:0000313|Ensembl:ENSTRUP00000077389.1};
GN   Name=LOC101069747 {ECO:0000313|Ensembl:ENSTRUP00000077389.1};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000077389.1, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000077389.1, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000077389.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSTRUP00000077389.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR   RefSeq; XP_029696004.1; XM_029840144.1.
DR   Ensembl; ENSTRUT00000073449.1; ENSTRUP00000077389.1; ENSTRUG00000029019.1.
DR   GeneID; 101069747; -.
DR   GeneTree; ENSGT00940000165423; -.
DR   Proteomes; UP000005226; Chromosome 8.
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   CDD; cd00247; Endostatin-like; 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; 1.10.2000.10; 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; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR   Pfam; PF01391; Collagen; 3.
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   4: Predicted;
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   Reference proteome {ECO:0000313|Proteomes:UP000005226};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1605
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025625775"
FT   DOMAIN          171..289
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   REGION          42..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..1103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1145..1254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1323..1427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..58
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..128
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..138
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..626
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..669
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..719
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..761
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..800
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        932..945
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        952..961
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1032..1046
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1047..1068
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1083..1097
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1193..1202
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1211..1222
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1334..1343
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1400..1413
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        186..232
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   1605 AA;  165042 MW;  486AA0E6AC517E4C CRC64;
     MSRIQTLAIF LVLCTGTCES WFWSSNQEEK TTESPTEVLI TNASTTPAGP TSAAVTPTNA
     TKEEEDDDLS GIGEELLDMA SGIRKFVEAW NATARNTHEV TEKVDPNRTG NANTSRGEGG
     PEGSGSGSGP AADAGSSEES LMIVPNSTSV VGAAQRLSNY TKAPDGGRAD ASRPPCLPVP
     SDWPICSAKR PQSLTLPNVF NHTSVDQVGA VLKEWAWLAR KGCHPSAEWF LCLLLAPRCS
     APAPLPCRSF CQTLRDSCWA SLDNGRLPVE CHLLPDVAPG RSHPTCLSVS NWKAESGVSL
     LQLIGDLPSG LNRSYGPRGQ VSFSFNAKAT AGQLALAHVP NPFYRHFSLI FNVRPSSPAA
     AVLFSITDGP QKLVYVGVKL SGERAGRQKV QFFYTEPDSE ASYEAASFEV PSLANSWTRF
     SLSIYEDQVT FYHGCESEPQ MVRFERSPDP MELDPEAKIF VGQAGNADAD RFRGDMSELK
     VVGDPQAAER LCDDEDDSDT ASGDFGSGDG GVVKQTESTL KTTPPSFQPL PAPPVTASQR
     LTGTIGEKGQ KGDRGERGSK GDLGLVGPKG EPGLGTRLSS ESGGPNGEKG SKGDKGQKGS
     LGAGYAGKKG EPGVPGPPGL PGPPGPAATV VQRGNGSVVQ HEPGPIGPPG LPGLIGPVGP
     PGSDGLPGDP GEDGKDGPPG PQGVPGTPGN PGSKGQKGDP GEGQPGPRGP PGLPGPPGPG
     AGDRQTSTFF DMEGSGFSDM EKLRGAQGPP GPPGLPGPPG IPGTSVALGP NGAIGFGPPG
     PPGLDGTPGL PGPPGPPGPR GQPGLVGVKG DSGNLGLPGI PGEKGAQGAP GRVGSPGQTG
     LAGLPGPMGP AGPPGPPGPP YRGGVGFGDQ ELEETTSLPG LAGPPGPQGP PGTAGFPGKP
     GFPGSNGEKG SEGPRGPPGI PGIDGFPGQL GEKGDRGEKG ERGQPGRDSG LPGPPGPPGP
     PGQIIYQSSN DGGHGVPGRP GFPGPAGPKG ERGDSGPPGY APKGQKGEPG IIIGPDGSPQ
     YHGGLAGLPG ESGPPGPVGP PGPYGPPGQK GEIGLPGRPG RPGLNGAKGL KGDSGSGSGY
     AYPGPPGPPG PPGPPGASGP IDRISGFEDI RRYLPDLKGE KGEQGPPGRV EVSGSNFDIN
     VLKNEMKGET GSPGLKGEKG EQGSGYYDPR YGGSGYPGQP GPPGPKGDSV IGPPGPQGPP
     GQPGRGYDGR PGPPGPPGPP GPAGGSYTGD SWDSRTVSVT GPPGPPGTPG LPGISSGVSL
     FRTYDTMAAT ARRHPEGSLV YVIDQTDLYL RVREGVRQVY LGNYIALPGD ENEVAAVEPP
     PVVLYSTDSN TPQPESPVQP DPHPPIHHKP QDPHSQQPTH PDPHYHPDPR YPAPTDPRYP
     SYTERINRPD GRSSHTTQER PTYPYHRYPV TTPRRPPVPE TPVHRHASGP GLHLIALNAP
     QTGAMRGIRG VDYLCFTQAQ AIGMKGTFRA FLSSRLQDLS SIVGKRDRDR LPIINLKDEV
     LFDSWDAIFN DGRIKDNVPI YSFDGRDILS DGAWPEKMLW HGSTGAGQRH TEDLCDAWRS
     GDQAQNGMAA PLHAGSNPLQ QRPGRCSSAY AVLCIENSYI GHAKR
//
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