ID A0A452S0N1_URSAM Unreviewed; 1606 AA.
AC A0A452S0N1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Low-density lipoprotein receptor-related protein {ECO:0000256|PIRNR:PIRNR036314};
GN Name=LRP5 {ECO:0000313|Ensembl:ENSUAMP00000025455.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000025455.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000025455.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 9643.ENSUAMP00000025455; -.
DR Ensembl; ENSUAMT00000028420.1; ENSUAMP00000025455.1; ENSUAMG00000019028.1.
DR GeneTree; ENSGT00940000156574; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
DR GO; GO:0042813; F:Wnt receptor activity; IEA:Ensembl.
DR GO; GO:0017147; F:Wnt-protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0048539; P:bone marrow development; IEA:Ensembl.
DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006007; P:glucose catabolic process; IEA:Ensembl.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0110135; P:Norrin signaling pathway; IEA:Ensembl.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0061304; P:retinal blood vessel morphogenesis; 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; 3.
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; 12.
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:UP000291022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|PIRNR:PIRNR036314};
KW Transmembrane helix {ECO:0000256|PIRNR:PIRNR036314};
KW Wnt signaling pathway {ECO:0000256|PIRNR:PIRNR036314}.
FT TRANSMEM 1377..1398
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR036314"
FT REPEAT 116..158
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 159..202
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 203..245
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 293..334
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 382..424
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 425..467
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 468..511
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 512..554
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 601..638
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 723..765
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 766..808
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 809..850
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 898..935
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 1072..1116
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1117..1159
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1209..1253
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1559..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1273..1288
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1291..1303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1298..1316
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1327..1339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1334..1352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1346..1361
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1606 AA; 178139 MW; B03D9EDA8A9701A3 CRC64;
MGAGVRLGGA GSTWGPRSSP FASTPAASPL LLFANRRDVR LVDAGGVKLE STVVVSGLED
AAAVDFQFSK GAVYWTDVSE EAIKQTYLNQ TGVAVQNVVI SGLVSPDGLA CDWVGKKLYW
TDSETNRIEV ANLNGTSRKV LFWQDLDQPR AIALDPAHGY MYWTDWGETP RIERAGMDGS
TRKIIVDSDI YWPNGLTIDL EEQKLYWADA KLSFIHRANL DGSFRQKVVE GSLTHPFALT
LSGDTLYWTD WQTRSIHACN KRTGEKRKEI LSALYSPMDI QVLSSERQPY CKTCRLKEDN
GGCSHLCLLS PREPFYTCAC PTGVQLQDNG KTCKAGAEEV LLLARRTDLR RISLDTPDFT
DIVLQVDDIR HAIAIDYDPL EGYVYWTDDE VRAIRRAYLD GSGAQTLVNT EINDPDGIAV
DWVARNLYWT DTGTDRIEVT RLNGTSRKIL VSEDLDEPRA IVLHPVMGLM YWTDWGENPK
IECAHLDGQE RHILVNTSLG WPNGLALDLQ EGKLYWGDAK TDKIEVINVD GTKRRTLLED
KLPHIFGFTL LGDFIYWTDW QRRSIERVHK VKASRDVIID QLPDLMGLKA VNVAKVVGTN
PCADRNGGCS HLCFFTPHAT KCGCPIGLEL LSDLKTCIVP EAFLVFTSRA AIHRISLETN
NNDVAIPLTG VKEASALDFD VSNNHIYWTD TISRAFMNGS SVEHVIEFGL DYPEGMAVDW
VGKNLYWADT GTNRIEVARL DGQFRQVLVW RDLDNPRSLA LDPTKGYIYW TEWGGKPRIV
RAFMDGTNCM TLVDKVGRAN DLTIDYADQR LYWTDLDTNM IESSDMLGQE RVVIADDLPH
PFGLTQYSDY IYWTDWNLHS IERADKTSGR NRTLIQGHLD FVMDILVFHS SRQDGLNDCM
HNNGQCGQLC LAIPGGHRCG CASHYTLDPS SRNCSPPTAF LLFSQKCAIS RMIPDDQHSP
DLILPLHGLR NVKAIDYDPL DKFIYWVDGR QNIKRAKDDG TQPFVLTSPS QSQNPDRQPH
DLSIDIYSRT LFWTCEATNT INVHRLNGDA MGVVLRGDRD KPRAIVVNAE RGYLYFTNMQ
DRAAKIERAA LDGTEREVLF TTGLIRPVAL VVDNRLGKLF WVDADLKRIE SCDLSGANRL
TLEDANIVQP VGLTVLGKHL YWIDRQQQMI ERVEKTTGDK RTRVQGRVAH LTGIHAVEDV
SLEEFSAHPC ARDNGGCSHI CIAKGDGTPR CSCPVHLVLL QNLLACGEPP TCSPDQFACA
TGEIDCIPGA WRCDGFPECD DQSDEEGCPV CSAAQFPCAR GQCVDLRLRC DGEADCQDRS
DEADSVCLPN QFRCASGQCV LIKQQCDSFP DCIDGSDELM CEITKPPSDD SPAHSSAIGP
VIGIILSLFV MGGVYFVCQR VVCQRYAGAN GPFPHEYVSG TPHVPLNFIA PGSSQHGPFT
GISCGKSMMS SVSLMGGRGG VPLYDRNHVT GASSSSSSST KATLYPPILN PPPSPATDPS
LYNADTFYSS NIPSTTRPYR PYIIRGMAPP TTPCSTDVCD SDYSANRWKA SKYYLDLNSD
SDPYPPPPTP HSQYLSAEDS CPPSPATERS YFHLFPPPPS PCTDSS
//
