ID H3BGY3_LATCH Unreviewed; 1598 AA.
AC H3BGY3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Low-density lipoprotein receptor-related protein {ECO:0000256|PIRNR:PIRNR036314};
GN Name=LRP5 {ECO:0000313|Ensembl:ENSLACP00000021154.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000021154.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000021154.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers
CC beta-catenin signaling through inducing aggregation of receptor-ligand
CC complexes into ribosome-sized signalosomes.
CC {ECO:0000256|PIRNR:PIRNR036314}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Forms phosphorylated oligomer
CC aggregates on Wnt-signaling. {ECO:0000256|PIRNR:PIRNR036314}.
CC -!- SIMILARITY: Belongs to the LDLR family.
CC {ECO:0000256|PIRNR:PIRNR036314}.
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; AFYH01011051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01011052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01011053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01011054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01011055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01011056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01011057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005988070.1; XM_005988008.2.
DR STRING; 7897.ENSLACP00000021154; -.
DR Ensembl; ENSLACT00000021294.1; ENSLACP00000021154.1; ENSLACG00000018584.1.
DR GeneID; 102358016; -.
DR CTD; 4041; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000156574; -.
DR HOGENOM; CLU_002489_0_0_1; -.
DR InParanoid; H3BGY3; -.
DR OMA; HTPCEDN; -.
DR OrthoDB; 3107655at2759; -.
DR TreeFam; TF315253; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000018584; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0042813; F:Wnt receptor activity; IEA:InterPro.
DR GO; GO:0017147; F:Wnt-protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035676; P:anterior lateral line neuromast hair cell development; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0031101; P:fin regeneration; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR GO; GO:0032474; P:otolith morphogenesis; IEA:Ensembl.
DR GO; GO:0035677; P:posterior lateral line neuromast hair cell development; IEA:Ensembl.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0045124; P:regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR CDD; cd00112; LDLa; 3.
DR Gene3D; 2.10.25.10; Laminin; 1.
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 InterPro; IPR017049; LRP5/6.
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; 11.
DR PIRSF; PIRSF036314; LDL_recpt-rel_p5/6; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00135; LY; 20.
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; 13.
PE 3: Inferred from homology;
KW Developmental protein {ECO:0000256|PIRNR:PIRNR036314};
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR036314};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR036314};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|PIRNR:PIRNR036314};
KW Transmembrane {ECO:0000256|PIRNR:PIRNR036314};
KW Transmembrane helix {ECO:0000256|PIRNR:PIRNR036314};
KW Wnt signaling pathway {ECO:0000256|PIRNR:PIRNR036314}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|PIRNR:PIRNR036314"
FT CHAIN 20..1598
FT /note="Low-density lipoprotein receptor-related protein"
FT /evidence="ECO:0000256|PIRNR:PIRNR036314"
FT /id="PRO_5010897971"
FT TRANSMEM 1375..1396
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR036314"
FT REPEAT 63..106
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 107..149
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 150..193
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 194..236
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 285..324
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 372..414
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 415..457
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 458..501
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 502..544
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 591..628
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 674..716
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 717..759
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 760..802
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 892..929
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 1068..1112
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1113..1155
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1205..1243
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 1461..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1549..1581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1269..1284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1287..1299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1294..1312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1306..1321
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1325..1337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1332..1350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1344..1359
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1598 AA; 179194 MW; 93008BC91C98ED62 CRC64;
MEVSLFGLLL SCNFLFVAAS PVLLFANRRD VRVVDGGSVK PESSIVVSGL EDAAAVDFLY
SEGVIYWTDV SEEAIKQTYF NQSGNVQKVV ISGLVSPDGL ACDWLGKKLY WTDSETNRIE
VANLNGTLRK VLFWQDLDQP RAIALDPAHG YMYWTDWGET PRIERAGMDG RTRKIIVDSD
IYWPNGLTID LEEQKLYWAD AKLSFIHRSN LDGSFRQKVV EGTLTHPFAL TLSGDTLYWT
DWQTRSIHAC NKKTGGRKRE ILGGIYSPMD IQVLSRERQQ YSQTPCEDNN GGCSHLCLLS
PKDPFYSCAC PTGVQLREDR RTCKSGADKV LLLARRTDLR RISLDMPDFT DIVLQIDGIR
HAIAIDYDPV EGYIYWTDDE VRAIRRAYLD GSGAETLVTT EIQHPDGIAV DWVARNLYWT
DTGTDRIEVT RLNGTARKIL ISENLDEPRA IVLNPLTGYL YWTDWGENPK IERANLDGSD
RIILVNTSLG WPNGLALDLT EGKLYWGDAK TDKIEVINTD GTERKTLLED KLPHIFGFTL
LGDYIYWTDW QRRSIERVHK TRATREIIID QLPDLMGLKA AHVTQTFGTN PCAENNGGCS
HLCFYTPLGP RCFCPMGLEL LSDMKTCIIP EAFLMFTSRA AIHRISLETN NNDVAIPLTG
VKEASALDFD VSDNRIYWTD ISLKTISRAF MNGSSIDHVI EFGLDCPEGM AVDWMGKNLY
WADTGTNRIE VARLDGKYRQ VLVWKDLDNP RTLALDPAKG YMYWTEWGGK PRIVRAHMDG
ANSLTLVDKI GRANGLTIDY AERRLYWIDF DTCMIESSDM MGNDREIIAD DLPHPFGLTQ
YRDYIYWTDW NLHSIQRADK TNGQNRTMIQ GHLEFVMDIL IFHSSRQDGS NDCMQNSGYC
AHLCLAVPEG YKCGCASHYT LDANNKNCSS PTSFLLFSQK TAISRMVLDE QQSPDIILPI
HGLRNIKAID YDPLDKLIYW VDGRQNTVKR AKDDGTQPFI VACAPNQSSN PEKQPHDLSI
DIYSRTVYWT CETTNTINVH RLDGKSIGVV LRGDHDKPRA IVVNAERGYL YFTNFQERSP
KIERAALDGT EREVLFTTGL IGPVALVIDN KLGKLFWVDA DLKRIESSDL SGANRVTLED
SNILQPVGLT VLGDHLYWVD RQQQMIERVE KLNGFKRTRI QGRIPHLTDI HAVEEVNMKE
FASHPCSHDN GGCSHICIAK GDGTPRCSCP VHLVLLQNLL TCGEPPTCSP DQFTCATGEI
DCIPMAWRCD GFPECEDHSD EQNCPVCSAN QFECEKGQCI DARLRCNGEI DCQDKSDEAD
CDAICRPNQF RCGSGLCILM KQQCDSFPDC SDGSDELSCE TNKPPLDEPQ SHSSAIGPVI
GIILSLFVMG GMYFFCQRVV CQRPFPHEYI SGTPHVPLNF IAPGSSPHGT FTGISCGKSM
ISSMSLMGGS SGAPLYDRNH VTGASSSSSS STKGTFYPQI LNPPPSPATD RSLYNTEMFY
SSNSPSTTRS YRPYLMRGTV PHTTPYSTDV CDSDYTTSRW KTNKYYIDLN SDSDPYPPPP
TPRSQYMSAE ESCPPSPATE RSYFHLCPPP PSPCTDSS
//
