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Database: UniProt
Entry: D0EWS1_DANRE
LinkDB: D0EWS1_DANRE
Original site: D0EWS1_DANRE 
ID   D0EWS1_DANRE            Unreviewed;      1430 AA.
AC   D0EWS1;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Low density lipoprotein-related protein 6 {ECO:0000313|EMBL:ACX46988.1};
DE   SubName: Full=Low-density lipoprotein receptor-related protein 5 {ECO:0000313|RefSeq:NP_001170929.1};
GN   Name=lrp5 {ECO:0000313|RefSeq:NP_001170929.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-050518-2};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:ACX46988.1};
RN   [1] {ECO:0000313|RefSeq:NP_001170929.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16237125;
RA   Dixon R.J., Eperon I.C., Hall L., Samani N.J.;
RT   "A genome-wide survey demonstrates widespread non-linear mRNA in expressed
RT   sequences from multiple species.";
RL   Nucleic Acids Res. 33:5904-5913(2005).
RN   [2] {ECO:0000313|EMBL:ACX46988.1, ECO:0000313|RefSeq:NP_001170929.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19801552; DOI=10.1074/jbc.M109.047456;
RA   Chen M., Philipp M., Wang J., Premont R.T., Garrison T.R., Caron M.G.,
RA   Lefkowitz R.J., Chen W.;
RT   "G Protein-coupled receptor kinases phosphorylate LRP6 in the Wnt
RT   pathway.";
RL   J. Biol. Chem. 284:35040-35048(2009).
RN   [3] {ECO:0000313|RefSeq:NP_001170929.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21911394;
RA   Ramachandran R., Zhao X.F., Goldman D.;
RT   "Ascl1a/Dkk/beta-catenin signaling pathway is necessary and glycogen
RT   synthase kinase-3beta inhibition is sufficient for zebrafish retina
RT   regeneration.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:15858-15863(2011).
RN   [4] {ECO:0000313|RefSeq:NP_001170929.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23484855;
RA   Lu H., Ma J., Yang Y., Shi W., Luo L.;
RT   "EpCAM is an endoderm-specific Wnt derepressor that licenses hepatic
RT   development.";
RL   Dev. Cell 24:543-553(2013).
RN   [5] {ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [6] {ECO:0000313|RefSeq:NP_001170929.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24485658;
RA   Wehner D., Cizelsky W., Vasudevaro M.D., Ozhan G., Haase C.,
RA   Kagermeier-Schenk B., Roder A., Dorsky R.I., Moro E., Argenton F., Kuhl M.,
RA   Weidinger G.;
RT   "Wnt/beta-catenin signaling defines organizing centers that orchestrate
RT   growth and differentiation of the regenerating zebrafish caudal fin.";
RL   Cell Rep. 6:467-481(2014).
RN   [7] {ECO:0000313|RefSeq:NP_001170929.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=27189481;
RA   Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA   Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA   Bobe J.;
RT   "Gene evolution and gene expression after whole genome duplication in fish:
RT   the PhyloFish database.";
RL   BMC Genomics 17:368-368(2016).
RN   [8] {ECO:0000313|RefSeq:NP_001170929.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=27193966;
RA   Cui Y., Lv S., Liu J., Nie S., Chen J., Dong Q., Huang C., Yang D.;
RT   "Chronic perfluorooctanesulfonic acid exposure disrupts lipid metabolism in
RT   zebrafish.";
RL   Hum Exp Toxicol 36:207-217(2017).
RN   [9] {ECO:0000313|RefSeq:NP_001170929.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28677207;
RA   Xia W., Hu J., Liu F., Ma J., Sun S., Zhang J., Jin K., Huang J., Jiang N.,
RA   Wang X., Li W., Ma Z., Ma D.;
RT   "New role of LRP5, associated with nonsyndromic autosomal-recessive
RT   hereditary hearing loss.";
RL   Hum. Mutat. 38:1421-1431(2017).
RN   [10] {ECO:0000313|RefSeq:NP_001170929.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29266316;
RA   So J., Khaliq M., Evason K., Ninov N., Martin B.L., Stainier D.Y.R.,
RA   Shin D.;
RT   "Wnt/beta-catenin signaling controls intrahepatic biliary network formation
RT   in zebrafish by regulating notch activity.";
RL   Hepatology 67:2352-2366(2018).
RN   [11] {ECO:0000313|RefSeq:NP_001170929.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29511374; DOI=10.7150/ijms.23054;
RA   Du Z., Ma H.L., Zhang Z.Y., Zheng J.W., Wang Y.A.;
RT   "Transgenic Expression of A Venous Malformation Related Mutation, TIE2-
RT   R849W, Significantly Induces Multiple Malformations of Zebrafish.";
RL   Int. J. Med. Sci. 15:385-394(2018).
RN   [12] {ECO:0000313|RefSeq:NP_001170929.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR   EMBL; GQ903573; ACX46988.1; -; mRNA.
DR   RefSeq; NP_001170929.1; NM_001177458.1.
DR   GeneID; 568518; -.
DR   KEGG; dre:568518; -.
DR   AGR; ZFIN:ZDB-GENE-050518-2; -.
DR   CTD; 4041; -.
DR   ZFIN; ZDB-GENE-050518-2; lrp5.
DR   OrthoDB; 3107655at2759; -.
DR   PhylomeDB; D0EWS1; -.
DR   Proteomes; UP000000437; Chromosome 25.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042813; F:Wnt receptor activity; IBA:GO_Central.
DR   GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR   GO; GO:0035676; P:anterior lateral line neuromast hair cell development; IMP:ZFIN.
DR   GO; GO:0030282; P:bone mineralization; IMP:ZFIN.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:ZFIN.
DR   GO; GO:0051216; P:cartilage development; IMP:ZFIN.
DR   GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:ZFIN.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR   GO; GO:0001889; P:liver development; IMP:ZFIN.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:ZFIN.
DR   GO; GO:0032474; P:otolith morphogenesis; IMP:ZFIN.
DR   GO; GO:0035677; P:posterior lateral line neuromast hair cell development; IMP:ZFIN.
DR   GO; GO:0030500; P:regulation of bone mineralization; IMP:ZFIN.
DR   GO; GO:0045124; P:regulation of bone resorption; IMP:ZFIN.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; IMP:ZFIN.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:ZFIN.
DR   CDD; cd00112; LDLa; 3.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   PANTHER; PTHR46513:SF16; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 5; 1.
DR   PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR   Pfam; PF14670; FXa_inhibition; 4.
DR   Pfam; PF00057; Ldl_recept_a; 3.
DR   Pfam; PF00058; Ldl_recept_b; 8.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00192; LDLa; 3.
DR   SMART; SM00135; LY; 17.
DR   SUPFAM; SSF57196; EGF/Laminin; 4.
DR   SUPFAM; SSF57424; LDL receptor-like module; 3.
DR   SUPFAM; SSF63825; YWTD domain; 4.
DR   PROSITE; PS01209; LDLRA_1; 2.
DR   PROSITE; PS50068; LDLRA_2; 3.
DR   PROSITE; PS51120; LDLRB; 11.
PE   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipoprotein {ECO:0000313|EMBL:ACX46988.1,
KW   ECO:0000313|RefSeq:NP_001170929.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:D0EWS1};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:NP_001170929.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1203..1223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          27..69
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          118..157
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   REPEAT          205..247
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          248..290
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          291..334
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          335..377
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          424..461
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   REPEAT          507..549
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          550..592
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          593..635
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          676..718
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          725..762
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   REPEAT          896..940
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          941..983
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          1033..1077
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   DOMAIN          1114..1150
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   REGION          822..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1288..1321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1380..1430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1288..1309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1397..1411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1416..1430
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1097..1112
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1115..1127
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1122..1140
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1134..1149
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1153..1165
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1160..1178
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1172..1187
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   1430 AA;  160013 MW;  FD1FF5E16991B700 CRC64;
     MDGSNRQIIV QKQIYWPNGL TIDLDEQKLY WADAKLSFIH RANLDGTSRE AVVEGSLTHP
     FALTLYDETL YWTDWQTRSI HACNKHSGEK HREILNGIYS PMDIQVLGQE RQPNIQTPCS
     ERNGGCSHLC LLSPIPPFYS CACPTGVKLK EDGKTCRPGA EQVLLLARRT DLRRISLDLP
     DFTDIVLQVN DIRHAIAIDY DPVEGYVYWT DDELRAIRRA RIDGSDAQTL ITNEINHPDG
     IAVDWVARNL YWTDTGTDRI EVTRLNGTSR RVLISENLDE PRAIVLDPIN GYMYWTDWGE
     LPKIERANLD GTDRVVLLNT SLGWPNGLAI DYIAGKLYWG DAKTDKIEVI NVDGTNRMTI
     LEDKLPHIFG FTLLGEYIYW TDWQRRSIER VHIANSTREV IVEQLPDLMG LKATKVMEAE
     GTNGCAENNG GCSHLCFHRP QGLSCACPMG LELLSDLRTC VVPEAFLLFT NRADIRSISL
     GTNSNDVPIP LTGVKEASAL DFDVLENRIY WTDVSTKTIS RAFMNGSSVE PVIEFGLDYP
     EGMAVDWMGR NLYWADTGTN RIEVARLDGQ YRQVLVCKDL DNPRSLALDP ANGYMYWTEW
     GGRPRIARAH MDGSNIVTLV DKVGRANGLT IDYIDQRLYW TDLDTCMIES TNMQSLQREI
     VADDLPHPFG LTQYRDYIYW TDWNLRSIER ADKRSGLNRT VVQGHLEYVM DILVFHSSRQ
     DGANDCSQNN GQCAHLCLAS PSGAQCRCAS HYTLEANGRN CSSPSSFLLF SQKSSISRMV
     LGEQSPDMIL PIHVMKNLRA ISFDPLERLV YWVDGRQNIR RSRDDGTQAS TVMTPNSDHP
     KQPHDLSLDP YSRTVYWTCE TTNTINIHRM DGHVIGEVLK DDVDKPRAIV VNAEKGYMYF
     TTVQERSAKI EGASLDGTER ESLFTTSLIR PVALALDNKL GKLFWVDADL KRIESSDLSG
     ANRIVLQDSN ILQPVGLTVL GDHLYWIDKQ QQMIERVDKL TGEKRTRIQG RLQYLTGIHA
     VQYMETDEFA THPCSRDNGG CSHICIAKGD GTPRCSCPMH LVLLQNLLSC GEPPTCSSEQ
     FTCATGEIDC IPMAWRCDGI AECADNSDEM NCPICSKLQF QCDKGQCVDI QVRCNGEPDC
     ADGSDEQDCE TICLSNQFRC GNSQCILKKQ QCDSFPDCTD ESDERFCDFP PPPNDLPRHT
     STIGPVIGII LSVFVMGGMC FVCQRVVCRH YKGPNGGFPH EYISGTPHVP LNFIAPTNSQ
     HGKGISCGKS MMSSVSLMGS SSSGAPLYDR NHVTGASSSS SSSTKGAFYP QMLNPPPSPA
     TDRSLYNAEV FYSSNSPSTT RSYRPYLMRG VAPPTTPCST DVCDSDYTTS RWKSNKYYMD
     LNSDSDPYPP PPTPRSQYMS AEESCPPSPS TERSYFHLCP PPPSPCTDSS
//
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