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Database: UniProt
Entry: A0A674MVI7_TAKRU
LinkDB: A0A674MVI7_TAKRU
Original site: A0A674MVI7_TAKRU 
ID   A0A674MVI7_TAKRU        Unreviewed;      1601 AA.
AC   A0A674MVI7;
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:ENSTRUP00000064988.1};
GN   Name=LOC101069747 {ECO:0000313|Ensembl:ENSTRUP00000064988.1};
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:ENSTRUP00000064988.1, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000064988.1, 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:ENSTRUP00000064988.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSTRUP00000064988.1}
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_011604710.2; XM_011606408.2.
DR   Ensembl; ENSTRUT00000064355.1; ENSTRUP00000064988.1; ENSTRUG00000029019.1.
DR   GeneID; 101069747; -.
DR   KEGG; tru: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..1601
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025543543"
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..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1141..1250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1319..1423
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        832..845
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..930
FT                   /note="Basic and acidic 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        1028..1042
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1043..1064
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1093
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1189..1198
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1207..1218
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1330..1339
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1396..1409
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        186..232
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   1601 AA;  165005 MW;  9AE24BDF0E1EC0B6 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 AQGAPGRVGS PGQTGLAGLP GPMGPAGPPG
     PPGPPYRGGV GFGDQELEET TSLPGLAGPP GPQGPPGTAG FPGKPGFPGS NGEKGSEGPR
     GPPGIPGIDG FPGQLGEKGD RGEKGERGQP GRDSGLPGPP GPPGPPGQII YQSSNDYNDV
     YWSEGLQGGH GVPGRPGFPG PAGPKGERGD SGPPGYAPKG QKGEPGIIIG PDGSPQYHGG
     LAGLPGESGP PGPVGPPGPY GPPGQKGEIG LPGRPGRPGL NGAKGLKGDS GSGSGYAYPG
     PPGPPGPPGP PGASGPIDRI SGFEDIRRYL PDLKGEKGEQ GPPGRVEVSG SNFDINVLKN
     EMKGETGSPG LKGEKGEQGS GYYDPRYGGS GYPGQPGPPG PKGDSVIGPP GPQGPPGQPG
     RGYDGRPGPP GPPGPPGPAG GSYTGDSWDS RTVSVTGPPG PPGTPGLPGI SSGVSLFRTY
     DTMAATARRH PEGSLVYVID QTDLYLRVRE GVRQVYLGNY IALPGDENEV AAVEPPPVVL
     YSTDSNTPQP ESPVQPDPHP PIHHKPQDPH SQQPTHPDPH YHPDPRYPAP TDPRYPSYTE
     RINRPDGRSS HTTQERPTYP YHRYPVTTPR RPPVPETPVH RHASGPGLHL IALNAPQTGA
     MRGIRGVDYL CFTQAQAIGM KGTFRAFLSS RLQDLSSIVG KRDRDRLPII NLKDEVLFDS
     WDAIFNDGRI KDNVPIYSFD GRDILSDGAW PEKMLWHGST GAGQRHTEDL CDAWRSGDQA
     QNGMAAPLHA GSNPLQQRPG RCSSAYAVLC IENSYIGHAK R
//
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