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Q91VN0 (LRP5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low-density lipoprotein receptor-related protein 5

Short name=LRP-5
Alternative name(s):
Low-density lipoprotein receptor-related protein 7
Short name=LRP-7
Lr3
Gene names
Name:Lrp5
Synonyms:Lrp7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1614 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin By similarity. Appears be required for postnatal control of vascular regression in the eye. Required for posterior patterning of the epiblast during gastrulation. Ref.5 Ref.7

Subunit structure

Homodimer; disulfide-linked. Forms phosphorylated oligomer aggregates on Wnt-signaling. Component of a WNT-signaling complex that contains a WNT protein, a FZD protein and LRP5 or LRP6. Interacts with FZD8; the interaction is formed on WNT-binding and signaling. Interacts (via the phosphorylated PPPSP motif domains) with AXIN1; the interaction prevents inhibition of beta-catenin phosphorylation and signaling and is enhanced in the presence of GSK3B and WNT1 or WNT3A. Interacts (via beta-propeller regions 3 and 4) with DKK1; the interaction, enhanced by MESD and/or KREMEN, inhibits beta-catenin signaling by preventing GSK3-mediated phosphorylation of the PPPSP motifs and subsequent, AXIN1 binding. Interacts with CSNK1E. Interacts with SOST; the interaction antagonizes canonical Wnt signaling. Interacts with APCDD1 By similarity. Interacts with MESD; the interaction prevents the formation of LRP5 aggregates, targets LRP5 to the plasma membrane and, when complexed with KREMEN2, increases DKK1 binding. Ref.6

Subcellular location

Membrane; Single-pass type I membrane protein. Endoplasmic reticulum. Note: Chaperoned to the plasma membrane by MESD By similarity. Ref.6

Tissue specificity

Widely expressed, with the highest expression levels in liver, heart, and lung and the lowest levels in brain and spleen. Expressed in early embryo with strongest expression in visceral endoderm overlying the extraembryonic ectoderm. Not present in the mesoderm nor in endoderm emerging from the primitive streak. Ref.7

Developmental stage

Expressed before or on embryonic day 7.

Post-translational modification

Phosphorylation of cytoplasmic PPPSP motifs regulates the signal transduction of the Wnt signaling pathway through acting as a docking site for AXIN1 By similarity.

Disruption phenotype

Mice exhibit decreased osteoblast proliferation, developing low bone mass postnatally. Also display persistent embryonic eye vascularization due to a failure of macrophage-induced endothelial cell apoptosis. Mutant animals exhibit a loss of middle phalanx ossification at 18.5 dpc. LRP5 and LRP6 double null mutants are more severely affected. Embryos arrest prior to mid-gestation. Ref.5 Ref.7

Sequence similarities

Belongs to the LDLR family.

Contains 4 EGF-like domains.

Contains 3 LDL-receptor class A domains.

Contains 20 LDL-receptor class B repeats.

Ontologies

Keywords
   Biological processEndocytosis
Wnt signaling pathway
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from direct assay Ref.5. Source: MGI

Wnt signaling pathway involved in dorsal/ventral axis specification

Inferred from Biological aspect of Ancestor. Source: RefGenome

adipose tissue development

Inferred from Biological aspect of Ancestor. Source: RefGenome

anatomical structure regression

Inferred from mutant phenotype PubMed 16163358. Source: MGI

anterior/posterior pattern specification

Inferred from genetic interaction Ref.7. Source: MGI

apoptotic process involved in patterning of blood vessels

Inferred from mutant phenotype PubMed 16163358. Source: MGI

bone development

Inferred from mutant phenotype PubMed 17700537. Source: BHF-UCL

bone marrow development

Inferred from Biological aspect of Ancestor. Source: RefGenome

bone morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

bone remodeling

Inferred from mutant phenotype Ref.5PubMed 15207752PubMed 16790443PubMed 17147489PubMed 17627087. Source: MGI

branching involved in mammary gland duct morphogenesis

Inferred from mutant phenotype PubMed 16973609. Source: MGI

canonical Wnt signaling pathway

Inferred from direct assay PubMed 15035989. Source: BHF-UCL

cell migration involved in gastrulation

Inferred from genetic interaction Ref.7. Source: MGI

cell-cell signaling involved in mammary gland development

Inferred from mutant phenotype PubMed 16973609. Source: MGI

cholesterol homeostasis

Inferred from Biological aspect of Ancestor. Source: RefGenome

cholesterol metabolic process

Inferred from mutant phenotype PubMed 12509515. Source: MGI

embryonic camera-type eye morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic digit morphogenesis

Inferred from genetic interaction Ref.7. Source: MGI

embryonic retina morphogenesis in camera-type eye

Inferred from Biological aspect of Ancestor. Source: RefGenome

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix-cell signaling

Inferred from direct assay PubMed 15035989. Source: BHF-UCL

gastrulation with mouth forming second

Inferred from genetic interaction Ref.7. Source: MGI

glucose catabolic process

Inferred from electronic annotation. Source: Ensembl

limb morphogenesis

Inferred from genetic interaction PubMed 15537447. Source: MGI

mammary gland duct morphogenesis

Inferred from genetic interaction PubMed 19503830. Source: MGI

negative regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

osteoblast development

Inferred from mutant phenotype PubMed 17700537. Source: BHF-UCL

positive regulation of fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mesenchymal cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast proliferation

Inferred from mutant phenotype Ref.5. Source: MGI

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15035989. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15035989. Source: BHF-UCL

regulation of apoptotic process

Inferred from mutant phenotype Ref.5. Source: MGI

regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

regulation of bone remodeling

Inferred from mutant phenotype PubMed 12817748. Source: MGI

regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of fat cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from mutant phenotype PubMed 12509515. Source: MGI

regulation of ossification

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

retina vasculature morphogenesis in camera-type eye

Inferred from mutant phenotype Ref.5PubMed 18263894. Source: MGI

retinal blood vessel morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

somatic stem cell maintenance

Inferred from mutant phenotype PubMed 19672307. Source: MGI

vasculature development

Inferred from mutant phenotype PubMed 16163358. Source: MGI

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

receptor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionWnt-activated receptor activity

Inferred from direct assay Ref.5. Source: MGI

Wnt-protein binding

Inferred from physical interaction Ref.5. Source: MGI

coreceptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 18632848PubMed 19075000. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced.
Isoform 1 (identifier: Q91VN0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 16141584Low-density lipoprotein receptor-related protein 5
PRO_0000017329

Regions

Topological domain31 – 13831353Extracellular Potential
Transmembrane1384 – 140623Helical; Potential
Topological domain1407 – 1614208Cytoplasmic Potential
Repeat74 – 11845LDL-receptor class B 1
Repeat119 – 16143LDL-receptor class B 2
Repeat162 – 20544LDL-receptor class B 3
Repeat206 – 24641LDL-receptor class B 4
Repeat247 – 28943LDL-receptor class B 5
Domain294 – 33643EGF-like 1
Repeat384 – 42643LDL-receptor class B 6
Repeat427 – 46943LDL-receptor class B 7
Repeat470 – 51344LDL-receptor class B 8
Repeat514 – 55643LDL-receptor class B 9
Repeat557 – 59943LDL-receptor class B 10
Domain600 – 64041EGF-like 2
Repeat686 – 72843LDL-receptor class B 11
Repeat729 – 77143LDL-receptor class B 12
Repeat772 – 81443LDL-receptor class B 13
Repeat815 – 85440LDL-receptor class B 14
Repeat855 – 89743LDL-receptor class B 15
Domain901 – 94141EGF-like 3
Repeat988 – 103447LDL-receptor class B 16
Repeat1035 – 107743LDL-receptor class B 17
Repeat1078 – 112245LDL-receptor class B 18
Repeat1123 – 116442LDL-receptor class B 19
Repeat1165 – 120642LDL-receptor class B 20
Domain1212 – 125342EGF-like 4
Domain1257 – 129539LDL-receptor class A 1
Domain1296 – 133237LDL-receptor class A 2
Domain1334 – 137037LDL-receptor class A 3
Region31 – 287257Beta-propeller 1
Region340 – 601262Beta-propeller 2
Region643 – 902260Beta-propeller 3
Region944 – 1211268Beta-propeller 4
Motif1499 – 15057PPPSP motif A
Motif1537 – 15448PPPSP motif B
Motif1573 – 15808PPPSP motif C
Motif1590 – 15956PPPSP motif D
Motif1604 – 16118PPPSP motif E

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation4981N-linked (GlcNAc...) Potential
Glycosylation7041N-linked (GlcNAc...) Potential
Glycosylation8771N-linked (GlcNAc...) Potential
Disulfide bond298 ↔ 309 By similarity
Disulfide bond305 ↔ 320 By similarity
Disulfide bond322 ↔ 335 By similarity
Disulfide bond604 ↔ 615 By similarity
Disulfide bond611 ↔ 624 By similarity
Disulfide bond626 ↔ 639 By similarity
Disulfide bond905 ↔ 916 By similarity
Disulfide bond912 ↔ 925 By similarity
Disulfide bond927 ↔ 940 By similarity
Disulfide bond1216 ↔ 1227 By similarity
Disulfide bond1223 ↔ 1237 By similarity
Disulfide bond1239 ↔ 1252 By similarity
Disulfide bond1258 ↔ 1272 By similarity
Disulfide bond1265 ↔ 1285 By similarity
Disulfide bond1279 ↔ 1294 By similarity
Disulfide bond1297 ↔ 1309 By similarity
Disulfide bond1304 ↔ 1322 By similarity
Disulfide bond1316 ↔ 1331 By similarity
Disulfide bond1335 ↔ 1347 By similarity
Disulfide bond1342 ↔ 1360 By similarity
Disulfide bond1354 ↔ 1369 By similarity

Experimental info

Sequence conflict2201R → H in AAC70183. Ref.2
Sequence conflict15201I → S in AAH11374. Ref.4
Sequence conflict15531T → I in AAC36468. Ref.1
Sequence conflict15531T → I in AAC70183. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 80FF4288470A4FC5

FASTA1,614178,885
        10         20         30         40         50         60 
METAPTRAPP PPPPPLLLLV LYCSLVPAAA SPLLLFANRR DVRLVDAGGV KLESTIVASG 

        70         80         90        100        110        120 
LEDAAAVDFQ FSKGAVYWTD VSEEAIKQTY LNQTGAAAQN IVISGLVSPD GLACDWVGKK 

       130        140        150        160        170        180 
LYWTDSETNR IEVANLNGTS RKVLFWQDLD QPRAIALDPA HGYMYWTDWG EAPRIERAGM 

       190        200        210        220        230        240 
DGSTRKIIVD SDIYWPNGLT IDLEEQKLYW ADAKLSFIHR ANLDGSFRQK VVEGSLTHPF 

       250        260        270        280        290        300 
ALTLSGDTLY WTDWQTRSIH ACNKWTGEQR KEILSALYSP MDIQVLSQER QPPFHTPCEE 

       310        320        330        340        350        360 
DNGGCSHLCL LSPREPFYSC ACPTGVQLQD NGKTCKTGAE EVLLLARRTD LRRISLDTPD 

       370        380        390        400        410        420 
FTDIVLQVGD IRHAIAIDYD PLEGYVYWTD DEVRAIRRAY LDGSGAQTLV NTEINDPDGI 

       430        440        450        460        470        480 
AVDWVARNLY WTDTGTDRIE VTRLNGTSRK ILVSEDLDEP RAIVLHPVMG LMYWTDWGEN 

       490        500        510        520        530        540 
PKIECANLDG RDRHVLVNTS LGWPNGLALD LQEGKLYWGD AKTDKIEVIN IDGTKRKTLL 

       550        560        570        580        590        600 
EDKLPHIFGF TLLGDFIYWT DWQRRSIERV HKVKASRDVI IDQLPDLMGL KAVNVAKVVG 

       610        620        630        640        650        660 
TNPCADGNGG CSHLCFFTPR ATKCGCPIGL ELLSDMKTCI IPEAFLVFTS RATIHRISLE 

       670        680        690        700        710        720 
TNNNDVAIPL TGVKEASALD FDVSNNHIYW TDVSLKTISR AFMNGSSVEH VIEFGLDYPE 

       730        740        750        760        770        780 
GMAVDWMGKN LYWADTGTNR IEVARLDGQF RQVLVWRDLD NPRSLALDPT KGYIYWTEWG 

       790        800        810        820        830        840 
GKPRIVRAFM DGTNCMTLVD KVGRANDLTI DYADQRLYWT DLDTNMIESS NMLGQERMVI 

       850        860        870        880        890        900 
ADDLPYPFGL TQYSDYIYWT DWNLHSIERA DKTSGRNRTL IQGHLDFVMD ILVFHSSRQD 

       910        920        930        940        950        960 
GLNDCVHSNG QCGQLCLAIP GGHRCGCASH YTLDPSSRNC SPPSTFLLFS QKFAISRMIP 

       970        980        990       1000       1010       1020 
DDQLSPDLVL PLHGLRNVKA INYDPLDKFI YWVDGRQNIK RAKDDGTQPS MLTSPSQSLS 

      1030       1040       1050       1060       1070       1080 
PDRQPHDLSI DIYSRTLFWT CEATNTINVH RLDGDAMGVV LRGDRDKPRA IAVNAERGYM 

      1090       1100       1110       1120       1130       1140 
YFTNMQDHAA KIERASLDGT EREVLFTTGL IRPVALVVDN ALGKLFWVDA DLKRIESCDL 

      1150       1160       1170       1180       1190       1200 
SGANRLTLED ANIVQPVGLT VLGRHLYWID RQQQMIERVE KTTGDKRTRV QGRVTHLTGI 

      1210       1220       1230       1240       1250       1260 
HAVEEVSLEE FSAHPCARDN GGCSHICIAK GDGTPRCSCP VHLVLLQNLL TCGEPPTCSP 

      1270       1280       1290       1300       1310       1320 
DQFACTTGEI DCIPGAWRCD GFPECADQSD EEGCPVCSAS QFPCARGQCV DLRLRCDGEA 

      1330       1340       1350       1360       1370       1380 
DCQDRSDEAN CDAVCLPNQF RCTSGQCVLI KQQCDSFPDC ADGSDELMCE INKPPSDDIP 

      1390       1400       1410       1420       1430       1440 
AHSSAIGPVI GIILSLFVMG GVYFVCQRVM CQRYTGASGP FPHEYVGGAP HVPLNFIAPG 

      1450       1460       1470       1480       1490       1500 
GSQHGPFPGI PCSKSVMSSM SLVGGRGSVP LYDRNHVTGA SSSSSSSTKA TLYPPILNPP 

      1510       1520       1530       1540       1550       1560 
PSPATDPSLY NVDVFYSSGI PATARPYRPY VIRGMAPPTT PCSTDVCDSD YSTSRWKSSK 

      1570       1580       1590       1600       1610 
YYLDLNSDSD PYPPPPTPHS QYLSAEDSCP PSPGTERSYC HLFPPPPSPC TDSS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a novel member of the low-density lipoprotein receptor family."
Hey P.J., Twells R.C.J., Phillips M.S., Nakagawa Y., Brown S.D., Kawaguchi Y., Cox R., Xie G., Dugan V., Hammond H., Metzker M.L., Todd J.A., Hess J.F.
Gene 216:103-111(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]"Molecular cloning of mouse Lrp7(Lr3) cDNA and chromosomal mapping of orthologous genes in mouse and human."
Chen D., Lathrop W., Dong Y.
Genomics 55:314-321(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
Tissue: Liver.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Mammary tumor.
[5]"Cbfa1-independent decrease in osteoblast proliferation, osteopenia, and persistent embryonic eye vascularization in mice deficient in Lrp5, a Wnt coreceptor."
Kato M., Patel M.S., Levasseur R., Lobov I., Chang B.H., Glass D.A. II, Hartmann C., Li L., Hwang T.H., Brayton C.F., Lang R.A., Karsenty G., Chan L.
J. Cell Biol. 157:303-314(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[6]"Mesd encodes an LRP5/6 chaperone essential for specification of mouse embryonic polarity."
Hsieh J.-C., Lee L., Zhang L., Wefer S., Brown K., DeRossi C., Wines M.E., Rosenquist T., Holdener B.C.
Cell 112:355-367(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MESD, OLIGOMERIZATION, SUBCELLULAR LOCATION.
[7]"The Wnt co-receptors Lrp5 and Lrp6 are essential for gastrulation in mice."
Kelly O.G., Pinson K.I., Skarnes W.C.
Development 131:2803-2815(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF064984 mRNA. Translation: AAC36468.1.
AF077847 mRNA. Translation: AAC70183.1.
AC112990 Genomic DNA. No translation available.
AC117797 Genomic DNA. No translation available.
BC011374 mRNA. Translation: AAH11374.1.
CCDSCCDS37881.1. [Q91VN0-1]
RefSeqNP_032539.2. NM_008513.3. [Q91VN0-1]
UniGeneMm.274581.

3D structure databases

ProteinModelPortalQ91VN0.
SMRQ91VN0. Positions 31-1255.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201202. 7 interactions.
IntActQ91VN0. 2 interactions.
MINTMINT-8293473.

PTM databases

PhosphoSiteQ91VN0.

Proteomic databases

PaxDbQ91VN0.
PRIDEQ91VN0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025856; ENSMUSP00000025856; ENSMUSG00000024913. [Q91VN0-1]
GeneID16973.
KEGGmmu:16973.
UCSCuc008fwq.2. mouse. [Q91VN0-1]

Organism-specific databases

CTD4041.
MGIMGI:1278315. Lrp5.

Phylogenomic databases

eggNOGNOG121718.
GeneTreeENSGT00750000117273.
HOVERGENHBG049167.
InParanoidQ91VN0.
KOK03068.
OMALFWTCEA.
OrthoDBEOG75XGK3.
TreeFamTF315253.

Gene expression databases

ArrayExpressQ91VN0.
BgeeQ91VN0.
GenevestigatorQ91VN0.

Family and domain databases

Gene3D2.120.10.30. 4 hits.
4.10.400.10. 3 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR000742. EG-like_dom.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR017049. Low_density_Lipo_rcpt-rel_p5/6.
[Graphical view]
PfamPF00057. Ldl_recept_a. 3 hits.
PF00058. Ldl_recept_b. 14 hits.
[Graphical view]
PIRSFPIRSF036314. LDL_recpt-rel_p5/6. 1 hit.
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00181. EGF. 4 hits.
SM00192. LDLa. 3 hits.
SM00135. LY. 20 hits.
[Graphical view]
SUPFAMSSF57424. SSF57424. 3 hits.
PROSITEPS01209. LDLRA_1. 3 hits.
PS50068. LDLRA_2. 3 hits.
PS51120. LDLRB. 20 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio291030.
PROQ91VN0.
SOURCESearch...

Entry information

Entry nameLRP5_MOUSE
AccessionPrimary (citable) accession number: Q91VN0
Secondary accession number(s): E9QQ75, O88883, Q9R208
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot