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O75197 (LRP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=LRP-5
Gene names
Name:LRP5
Synonyms:LR3, LRP7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1615 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. Appears be required for postnatal control of vascular regression in the eye. Required for posterior patterning of the epiblast during gastrulation. Ref.8 Ref.9 Ref.10 Ref.12 Ref.25

Subunit structure

Homodimer; disulfide-linked. Forms phosphorylated oligomer aggregates on Wnt-signaling By similarity. 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 MESD; the interaction prevents the formation of LRP5 aggregates, targets LRP5 to the plasma membrane and, when complexed with KREMEN2, increases DKK1 binding. Interacts with CSNK1E. Interacts with SOST; the interaction antagonizes canonical Wnt signaling. Interacts with APCDD1. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Subcellular location

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

Tissue specificity

Widely expressed, with the highest level of expression in the liver and in aorta. Ref.1

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.

Polymorphism

Genetic variations in LRP5 define the bone mineral density quantitative trait locus 1 (BMND1) [MIM:601884]. Variance in bone mineral density influences bone mass and contributes to size determination in the general population.

Involvement in disease

Vitreoretinopathy, exudative 4 (EVR4) [MIM:601813]: A disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.24 Ref.26 Ref.27 Ref.32 Ref.36 Ref.37

Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.25 Ref.28 Ref.30

Osteoporosis-pseudoglioma syndrome (OPPG) [MIM:259770]: A disease characterized by congenital or infancy-onset blindness and severe juvenile-onset osteoporosis and spontaneous fractures. Additional clinical manifestations may include microphthalmos, abnormalities of the iris, lens or vitreous, cataracts, short stature, microcephaly, ligamental laxity, mental retardation and hypotonia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.26 Ref.31 Ref.33 Ref.34

High bone mass trait (HBM) [MIM:601884]: Rare phenotype characterized by exceptionally dense bones. HBM individuals show otherwise a completely normal skeletal structure and no other unusual clinical findings.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.19 Ref.20 Ref.29

Endosteal hyperostosis, Worth type (WENHY) [MIM:144750]: An autosomal dominant sclerosing bone dysplasia clinically characterized by elongation of the mandible, increased gonial angle, flattened forehead, and the presence of a slowly enlarging osseous prominence of the hard palate (torus palatinus). Serum calcium, phosphorus and alkaline phosphatase levels are normal. Radiologically, it is characterized by early thickening of the endosteum of long bones, the skull and of the mandible. With advancing age, the trabeculae of the metaphysis become thickened. WENHY becomes clinically and radiologically evident by adolescence, does not cause deformity except in the skull and mandible, and is not associated with bone pain or fracture. Affected patients have normal height, proportion, intelligence and longevity.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

Osteopetrosis, autosomal dominant 1 (OPTA1) [MIM:607634]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. OPTA1 is an autosomal dominant form characterized by generalized osteosclerosis most pronounced in the cranial vault. Patients are often asymptomatic, but some suffer from pain and hearing loss. It appears to be the only type of osteopetrosis not associated with an increased fracture rate.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

Van Buchem disease 2 (VBCH2) [MIM:607636]: VBCH2 is an autosomal dominant sclerosing bone dysplasia characterized by cranial osteosclerosis, thickened calvaria and cortices of long bones, enlarged mandible and normal serum alkaline phosphatase levels.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

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 diversityPolymorphism
   DiseaseDisease mutation
Osteogenesis imperfecta
Osteopetrosis
   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 PubMed 17955262. Source: BHF-UCL

Wnt signaling pathway involved in dorsal/ventral axis specification

Inferred from direct assay PubMed 11029007. Source: BHF-UCL

adipose tissue development

Inferred from mutant phenotype PubMed 17680723. Source: BHF-UCL

anterior/posterior pattern specification

Inferred from Biological aspect of Ancestor. Source: RefGenome

bone marrow development

Inferred from mutant phenotype PubMed 17680723. Source: BHF-UCL

bone morphogenesis

Inferred from mutant phenotype PubMed 19673927PubMed 20146170PubMed 20630166. Source: BHF-UCL

bone remodeling

Inferred from Biological aspect of Ancestor. Source: RefGenome

branching involved in mammary gland duct morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

canonical Wnt signaling pathway

Inferred from direct assay PubMed 12121999PubMed 12857724PubMed 15035989. Source: BHF-UCL

cholesterol homeostasis

Inferred from mutant phenotype PubMed 18721193PubMed 20146170. Source: BHF-UCL

embryonic camera-type eye morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic limb morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic retina morphogenesis in camera-type eye

Inferred from Biological aspect of Ancestor. Source: RefGenome

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

gastrulation with mouth forming second

Inferred from Biological aspect of Ancestor. Source: RefGenome

glucose catabolic process

Inferred from mutant phenotype PubMed 19673927. Source: BHF-UCL

negative regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 17680723. Source: BHF-UCL

negative regulation of protein serine/threonine kinase activity

Inferred from mutant phenotype PubMed 19107203. Source: BHF-UCL

osteoblast development

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of cell proliferation

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of fat cell differentiation

Inferred from mutant phenotype PubMed 17680723. Source: BHF-UCL

positive regulation of mesenchymal cell proliferation

Inferred from mutant phenotype PubMed 17680723. Source: BHF-UCL

positive regulation of mitosis

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12857724. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15035989PubMed 17955262. Source: BHF-UCL

regulation of blood pressure

Inferred from mutant phenotype PubMed 18721193. Source: BHF-UCL

regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 18044981. Source: BHF-UCL

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from Biological aspect of Ancestor. Source: RefGenome

retina morphogenesis in camera-type eye

Inferred from mutant phenotype Ref.24. Source: BHF-UCL

retinal blood vessel morphogenesis

Inferred from mutant phenotype Ref.22Ref.24. Source: BHF-UCL

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 17680723. Source: BHF-UCL

receptor complex

Inferred from direct assay PubMed 18762581. Source: BHF-UCL

   Molecular_functionWnt-activated receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt-protein binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

coreceptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CAPRIN2Q6IMN63EBI-2466421,EBI-6918449

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 16151584Low-density lipoprotein receptor-related protein 5
PRO_0000017328

Regions

Topological domain32 – 13841353Extracellular Potential
Transmembrane1385 – 140723Helical; Potential
Topological domain1408 – 1615208Cytoplasmic Potential
Repeat75 – 11945LDL-receptor class B 1
Repeat78 – 814YWTD 1
Repeat120 – 16243LDL-receptor class B 2
Repeat123 – 1264YWTD 2
Repeat163 – 20644LDL-receptor class B 3
Repeat166 – 1694YWTD 3
Repeat207 – 24741LDL-receptor class B 4
Repeat248 – 29043LDL-receptor class B 5
Repeat251 – 2544YWTD 4
Domain295 – 33743EGF-like 1
Repeat385 – 42743LDL-receptor class B 6
Repeat388 – 3914YWTD 5
Repeat428 – 47043LDL-receptor class B 7
Repeat431 – 4344YWTD 6
Repeat471 – 51444LDL-receptor class B 8
Repeat474 – 4774YWTD 7
Repeat515 – 55743LDL-receptor class B 9
Repeat558 – 60043LDL-receptor class B 10
Repeat559 – 5624YWTD 8
Domain601 – 64141EGF-like 2
Repeat687 – 72943LDL-receptor class B 11
Repeat690 – 6934YWTD 9
Repeat730 – 77243LDL-receptor class B 12
Repeat773 – 81543LDL-receptor class B 13
Repeat816 – 85540LDL-receptor class B 14
Repeat819 – 8224YWTD 10
Repeat856 – 89843LDL-receptor class B 15
Repeat859 – 8624YWTD 11
Domain902 – 94241EGF-like 3
Repeat989 – 103547LDL-receptor class B 16
Repeat1036 – 107843LDL-receptor class B 17
Repeat1079 – 112345LDL-receptor class B 18
Repeat1124 – 116441LDL-receptor class B 19
Repeat1165 – 120743LDL-receptor class B 20
Domain1213 – 125442EGF-like 4
Domain1258 – 129639LDL-receptor class A 1
Domain1297 – 133337LDL-receptor class A 2
Domain1335 – 137137LDL-receptor class A 3
Region32 – 288257Beta-propeller 1
Region341 – 602262Beta-propeller 2
Region644 – 903260Beta-propeller 3
Region945 – 1212268Beta-propeller 4
Motif1500 – 15067PPPSP motif A
Motif1538 – 15458PPPSP motif B
Motif1574 – 15818PPPSP motif C
Motif1591 – 15966PPPSP motif D
Motif1605 – 16128PPPSP motif E
Compositional bias1495 – 1610116Pro-rich

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation4461N-linked (GlcNAc...) Potential
Glycosylation4991N-linked (GlcNAc...) Potential
Glycosylation7051N-linked (GlcNAc...) Potential
Glycosylation8781N-linked (GlcNAc...) Potential
Disulfide bond299 ↔ 310 By similarity
Disulfide bond306 ↔ 321 By similarity
Disulfide bond323 ↔ 336 By similarity
Disulfide bond605 ↔ 616 By similarity
Disulfide bond612 ↔ 625 By similarity
Disulfide bond627 ↔ 640 By similarity
Disulfide bond906 ↔ 917 By similarity
Disulfide bond913 ↔ 926 By similarity
Disulfide bond928 ↔ 941 By similarity
Disulfide bond1217 ↔ 1228 By similarity
Disulfide bond1224 ↔ 1238 By similarity
Disulfide bond1240 ↔ 1253 By similarity
Disulfide bond1259 ↔ 1273 By similarity
Disulfide bond1266 ↔ 1286 By similarity
Disulfide bond1280 ↔ 1295 By similarity
Disulfide bond1298 ↔ 1310 By similarity
Disulfide bond1305 ↔ 1323 By similarity
Disulfide bond1317 ↔ 1332 By similarity
Disulfide bond1336 ↔ 1348 By similarity
Disulfide bond1343 ↔ 1361 By similarity
Disulfide bond1355 ↔ 1370 By similarity

Natural variations

Natural variant15 – 206Missing Found in a family with osteoporosis pseudoglioma syndrome; impairs protein trafficking to the endoplasmic reticulum and cell membrane.
VAR_058582
Natural variant18 – 203Missing.
VAR_021804
Natural variant201L → LL. Ref.21
VAR_021805
Natural variant291A → T in primary osteoporosis. Ref.28
VAR_063941
Natural variant891Q → R. Ref.21 Ref.25
Corresponds to variant rs41494349 [ dbSNP | Ensembl ].
VAR_021806
Natural variant971A → V. Ref.27
Corresponds to variant rs143433231 [ dbSNP | Ensembl ].
VAR_063942
Natural variant1111D → Y in OPTA1. Ref.21
VAR_021807
Natural variant1451L → F in EVR4. Ref.27
VAR_063943
Natural variant1541R → M in HBM. Ref.29
VAR_063944
Natural variant1711G → R in OPTA1. Ref.21
VAR_021808
Natural variant1711G → V in HBM; also in HBM individuals with enlarged mandible and torus palatinus; abolishes interaction with MESD; impairs transport to cell surface; no enhancement of DKK1 binding by MESD resulting in impaired inhibition of Wnt signaling by DKK1. Ref.11 Ref.16 Ref.19 Ref.20
VAR_021809
Natural variant1731T → M in EVR4; an individual with abnormal retinal vasculature and retinal folds. Ref.22 Ref.26
VAR_018465
Natural variant2031D → N in OPPG. Ref.26
VAR_063945
Natural variant2141A → T in WENHY. Ref.21
VAR_021810
Natural variant2141A → V in WENHY. Ref.21
VAR_021811
Natural variant2421A → T in OPTA1, VBCH2 and WENHY. Ref.21
VAR_021812
Natural variant2441T → M in OPPG; appears to traffic less well than does the wild-type protein; appears to be postranslationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. Ref.26
VAR_063946
Natural variant2531T → I in OPTA1. Ref.21
VAR_021813
Natural variant2821M → V in HBM; lowered LRP5-mediated Wnt signaling. No effect on DKK1 binding.
VAR_063412
Natural variant3071S → F in OPPG. Ref.26
VAR_063947
Natural variant3481R → W in OPPG. Ref.26
VAR_063948
Natural variant3531R → Q in OPPG. Ref.26
VAR_063949
Natural variant3561S → L in idiopathic osteoporosis and OPPG; appears to traffic comparably than does the wild-type protein; appears to be postranslationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. Ref.26 Ref.30
VAR_063950
Natural variant3901T → K in OPPG; is unable to traffic normally; appears to be postranslationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. Ref.26
VAR_063951
Natural variant4001A → E in OPPG. Ref.26
VAR_063952
Natural variant4041G → R in OPPG; appears to traffic less well than does the wild-type protein; appears to be postranslationally modified similar to wild-type protein; has 50% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. Ref.26
VAR_063953
Natural variant4091T → A in OPPG. Ref.34
VAR_063954
Natural variant4341D → N in OPPG; appears to traffic less well than does the wild-type protein; appears to be postranslationally modified similar to wild-type protein; has 50% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. Ref.26
VAR_063955
Natural variant4411E → K in EVR4. Ref.37
VAR_063956
Natural variant4441R → C in EVR4; associated in a EVR1 patient with mutation GLN-417 in FZD4. Ref.27
VAR_063957
Natural variant4551S → L in idiopathic osteoporosis; shows an inhibitory effect on Wnt signal transduction. Ref.30
VAR_063958
Natural variant4601E → K in OPPG. Ref.26
VAR_063959
Natural variant4781W → R in OPPG. Ref.31
VAR_063960
Natural variant4941R → Q in OPPG. Ref.18 Ref.26
VAR_021814
Natural variant5041W → C in OPPG. Ref.31
VAR_063961
Natural variant5111D → A in EVR4. Ref.36
VAR_063962
Natural variant5201G → V in OPPG; appears to traffic comparably than does the wild-type protein; appears to be postranslationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. Ref.26
VAR_063963
Natural variant5221A → T in EVR4. Ref.27
VAR_063964
Natural variant5311N → I in OPPG. Ref.33
VAR_063965
Natural variant5351T → M in EVR4; autosomal recessive. Ref.27
VAR_063966
Natural variant5501G → R in EVR4; autosomal recessive. Ref.32
VAR_063967
Natural variant5701R → Q in EVR4; autosomal recessive; has significantly reduced Wnt or Norrin signal transduction. Ref.24 Ref.26
VAR_021222
Natural variant5701R → W in OPPG. Ref.18 Ref.26
VAR_021815
Natural variant6101G → R in EVR4 and OPPG; appears to traffic less well than does the wild-type protein; appears to be postranslationally modified similar to wild-type protein; has 60% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. Ref.26 Ref.27
VAR_063968
Natural variant6171F → C in EVR4; autosomal recessive. Ref.27
VAR_063969
Natural variant6671V → M. Ref.18 Ref.21 Ref.23
Corresponds to variant rs4988321 [ dbSNP | Ensembl ].
VAR_021816
Natural variant6831D → N in OPPG. Ref.26
VAR_063970
Natural variant7331Y → H in OPPG. Ref.26
VAR_063971
Natural variant7521R → G in EVR4; autosomal recessive. Ref.24
VAR_021223
Natural variant7981T → A in EVR4. Ref.27
VAR_063972
Natural variant8051R → W in EVR4. Ref.36
VAR_063973
Natural variant10361R → Q in primary osteoporosis. Ref.28
Corresponds to variant rs61889560 [ dbSNP | Ensembl ].
VAR_063974
Natural variant10991D → Y in OPPG. Ref.26
VAR_063975
Natural variant11131R → C in OPPG. Ref.26
VAR_063976
Natural variant11211N → D in EVR4. Ref.27
Corresponds to variant rs80358317 [ dbSNP | Ensembl ].
VAR_063977
Natural variant11681Y → H in EVR4; an individual with total retinal detachment and retinoschisis; is unable to transduce Wnt or Norrin signal transduction. Ref.22 Ref.26
VAR_018466
Natural variant12041V → L.
Corresponds to variant rs11607268 [ dbSNP | Ensembl ].
VAR_035208
Natural variant12531C → F in EVR4. Ref.37
VAR_063978
Natural variant13301A → V. Ref.4 Ref.21 Ref.23 Ref.25
Corresponds to variant rs3736228 [ dbSNP | Ensembl ].
VAR_021817
Natural variant13611C → G in EVR4; autosomal dominant; has mildly reduced Wnt or Norrin signal transduction. Ref.22 Ref.26
VAR_018467
Natural variant13671E → K in EVR4; autosomal recessive. Ref.24 Ref.26
Corresponds to variant rs28939709 [ dbSNP | Ensembl ].
VAR_021224
Natural variant14011G → D in OPPG. Ref.26
VAR_063979
Natural variant15251A → V. Ref.2 Ref.22
Corresponds to variant rs1127291 [ dbSNP | Ensembl ].
VAR_021225
Natural variant15371A → T Could be associated with idiopathic osteoporosis; does not result in a significant alteration of Wnt signal transduction. Ref.30
VAR_063980
Natural variant15401T → M. Ref.27
Corresponds to variant rs141407040 [ dbSNP | Ensembl ].
VAR_063981

Experimental info

Sequence conflict1525 – 15284Missing in AAK52433. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O75197 [UniParc].

Last modified April 12, 2005. Version 2.
Checksum: 8BA25D07F51E02CA

FASTA1,615179,145
        10         20         30         40         50         60 
MEAAPPGPPW PLLLLLLLLL ALCGCPAPAA ASPLLLFANR RDVRLVDAGG VKLESTIVVS 

        70         80         90        100        110        120 
GLEDAAAVDF QFSKGAVYWT DVSEEAIKQT YLNQTGAAVQ NVVISGLVSP DGLACDWVGK 

       130        140        150        160        170        180 
KLYWTDSETN RIEVANLNGT SRKVLFWQDL DQPRAIALDP AHGYMYWTDW GETPRIERAG 

       190        200        210        220        230        240 
MDGSTRKIIV DSDIYWPNGL TIDLEEQKLY WADAKLSFIH RANLDGSFRQ KVVEGSLTHP 

       250        260        270        280        290        300 
FALTLSGDTL YWTDWQTRSI HACNKRTGGK RKEILSALYS PMDIQVLSQE RQPFFHTRCE 

       310        320        330        340        350        360 
EDNGGCSHLC LLSPSEPFYT CACPTGVQLQ DNGRTCKAGA EEVLLLARRT DLRRISLDTP 

       370        380        390        400        410        420 
DFTDIVLQVD DIRHAIAIDY DPLEGYVYWT DDEVRAIRRA YLDGSGAQTL VNTEINDPDG 

       430        440        450        460        470        480 
IAVDWVARNL YWTDTGTDRI EVTRLNGTSR KILVSEDLDE PRAIALHPVM GLMYWTDWGE 

       490        500        510        520        530        540 
NPKIECANLD GQERRVLVNA SLGWPNGLAL DLQEGKLYWG DAKTDKIEVI NVDGTKRRTL 

       550        560        570        580        590        600 
LEDKLPHIFG FTLLGDFIYW TDWQRRSIER VHKVKASRDV IIDQLPDLMG LKAVNVAKVV 

       610        620        630        640        650        660 
GTNPCADRNG GCSHLCFFTP HATRCGCPIG LELLSDMKTC IVPEAFLVFT SRAAIHRISL 

       670        680        690        700        710        720 
ETNNNDVAIP LTGVKEASAL DFDVSNNHIY WTDVSLKTIS RAFMNGSSVE HVVEFGLDYP 

       730        740        750        760        770        780 
EGMAVDWMGK NLYWADTGTN RIEVARLDGQ FRQVLVWRDL DNPRSLALDP TKGYIYWTEW 

       790        800        810        820        830        840 
GGKPRIVRAF MDGTNCMTLV DKVGRANDLT IDYADQRLYW TDLDTNMIES SNMLGQERVV 

       850        860        870        880        890        900 
IADDLPHPFG LTQYSDYIYW TDWNLHSIER ADKTSGRNRT LIQGHLDFVM DILVFHSSRQ 

       910        920        930        940        950        960 
DGLNDCMHNN GQCGQLCLAI PGGHRCGCAS HYTLDPSSRN CSPPTTFLLF SQKSAISRMI 

       970        980        990       1000       1010       1020 
PDDQHSPDLI LPLHGLRNVK AIDYDPLDKF IYWVDGRQNI KRAKDDGTQP FVLTSLSQGQ 

      1030       1040       1050       1060       1070       1080 
NPDRQPHDLS IDIYSRTLFW TCEATNTINV HRLSGEAMGV VLRGDRDKPR AIVVNAERGY 

      1090       1100       1110       1120       1130       1140 
LYFTNMQDRA AKIERAALDG TEREVLFTTG LIRPVALVVD NTLGKLFWVD ADLKRIESCD 

      1150       1160       1170       1180       1190       1200 
LSGANRLTLE DANIVQPLGL TILGKHLYWI DRQQQMIERV EKTTGDKRTR IQGRVAHLTG 

      1210       1220       1230       1240       1250       1260 
IHAVEEVSLE EFSAHPCARD NGGCSHICIA KGDGTPRCSC PVHLVLLQNL LTCGEPPTCS 

      1270       1280       1290       1300       1310       1320 
PDQFACATGE IDCIPGAWRC DGFPECDDQS DEEGCPVCSA AQFPCARGQC VDLRLRCDGE 

      1330       1340       1350       1360       1370       1380 
ADCQDRSDEA DCDAICLPNQ FRCASGQCVL IKQQCDSFPD CIDGSDELMC EITKPPSDDS 

      1390       1400       1410       1420       1430       1440 
PAHSSAIGPV IGIILSLFVM GGVYFVCQRV VCQRYAGANG PFPHEYVSGT PHVPLNFIAP 

      1450       1460       1470       1480       1490       1500 
GGSQHGPFTG IACGKSMMSS VSLMGGRGGV PLYDRNHVTG ASSSSSSSTK ATLYPPILNP 

      1510       1520       1530       1540       1550       1560 
PPSPATDPSL YNMDMFYSSN IPATARPYRP YIIRGMAPPT TPCSTDVCDS DYSASRWKAS 

      1570       1580       1590       1600       1610 
KYYLDLNSDS DPYPPPPTPH SQYLSAEDSC PPSPATERSY FHLFPPPPSP CTDSS 

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References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of LR3, a novel LDL receptor family protein with mitogenic activity."
Dong Y., Lathrop W., Weaver D., Qiu Q., Cini J., Bertolini D., Chen D.
Biochem. Biophys. Res. Commun. 251:784-790(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Osteoblast.
[2]"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], VARIANT VAL-1525.
Tissue: Osteoblast.
[3]"The sequence and gene characterization of a 400-kb candidate region for IDDM4 on chromosome 11q13."
Twells R.C.J., Metzker M.L., Brown S.D., Cox R., Garey C., Hammond H., Hey P.J., Levy E., Nakagawa Y., Philips M.S., Todd J.A., Hess J.F.
Genomics 72:231-242(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Low-density lipoprotein receptor-related protein 5 (LRP5) is essential for normal cholesterol metabolism and glucose-induced insulin secretion."
Fujino T., Asaba H., Kang M.J., Ikeda Y., Sone H., Takada S., Kim D.H., Ioka R.X., Ono M., Tomoyori H., Okubo M., Murase T., Kamataki A., Yamamoto J., Magoori K., Takahashi S., Miyamoto Y., Oishi H. expand/collapse author list , Nose M., Okazaki M., Usui S., Imaizumi K., Yanagisawa M., Sakai J., Yamamoto T.T.
Proc. Natl. Acad. Sci. U.S.A. 100:229-234(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-1330.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
[8]"Head inducer Dickkopf-1 is a ligand for Wnt coreceptor LRP6."
Semenov M.V., Tamai K., Brott B.K., Kuhl M., Sokol S., He X.
Curr. Biol. 11:951-961(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FZD8 IN WNT-FZD-LRP5-LRP6 COMPLEX, INTERACTION WITH DKK1, FUNCTION.
[9]"Low-density lipoprotein receptor-related protein-5 binds to Axin and regulates the canonical Wnt signaling pathway."
Mao J., Wang J., Liu B., Pan W., Farr G.H. III, Flynn C., Yuan H., Takada S., Kimelman D., Li L., Wu D.
Mol. Cell 7:801-809(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AXIN1.
[10]"A mechanism for Wnt coreceptor activation."
Tamai K., Zeng X., Liu C., Zhang X., Harada Y., Chang Z., He X.
Mol. Cell 13:149-156(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH AXIN1.
[11]"The LRP5 high-bone-mass G171V mutation disrupts LRP5 interaction with Mesd."
Zhang Y., Wang Y., Li X., Zhang J., Mao J., Li Z., Zheng J., Li L., Harris S., Wu D.
Mol. Cell. Biol. 24:4677-4684(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MESD, CHARACTERIZATION OF VARIANT HBM VAL-171.
[12]"Sclerostin binds to LRP5/6 and antagonizes canonical Wnt signaling."
Li X., Zhang Y., Kang H., Liu W., Liu P., Zhang J., Harris S.E., Wu D.
J. Biol. Chem. 280:19883-19887(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DKK1 AND SOST, FUNCTION.
[13]"SOST is a ligand for LRP5/LRP6 and a Wnt signaling inhibitor."
Semenov M., Tamai K., He X.
J. Biol. Chem. 280:26770-26775(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WNT1 IN THE WNT-FZD-LRP5-LRP6 COMPLEX, INTERACTION WITH SOST.
[14]"Negative regulation of LRP6 function by casein kinase I epsilon phosphorylation."
Swiatek W., Kang H., Garcia B.A., Shabanowitz J., Coombs G.S., Hunt D.F., Virshup D.M.
J. Biol. Chem. 281:12233-12241(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSNK1E.
[15]"Requirement for natively unstructured regions of mesoderm development candidate 2 in promoting low-density lipoprotein receptor-related protein 6 maturation."
Koduri V., Blacklow S.C.
Biochemistry 46:6570-6577(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MESD.
[16]"A cell-based Dkk1 binding assay reveals roles for extracellular domains of LRP5 in Dkk1 interaction and highlights differences between wild-type and the high bone mass mutant LRP5(G171V)."
Murrills R.J., Matteo J.J., Bhat B.M., Coleburn V.E., Allen K.M., Chen W., Damagnez V., Bhat R.A., Bex F.J., Bodine P.V.
J. Cell. Biochem. 108:1066-1075(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DKK1 AND MESD, CHARACTERIZATION OF VARIANT VAL-171.
[17]"APCDD1 is a novel Wnt inhibitor mutated in hereditary hypotrichosis simplex."
Shimomura Y., Agalliu D., Vonica A., Luria V., Wajid M., Baumer A., Belli S., Petukhova L., Schinzel A., Brivanlou A.H., Barres B.A., Christiano A.M.
Nature 464:1043-1047(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APCDD1.
[18]"LDL receptor-related protein 5 (LRP5) affects bone accrual and eye development."
Gong Y., Slee R.B., Fukai N., Rawadi G., Roman-Roman S., Reginato A.M., Wang H., Cundy T., Glorieux F.H., Lev D., Zacharin M., Oexle K., Marcelino J., Suwairi W., Heeger S., Sabatakos G., Apte S., Adkins W.N. expand/collapse author list , Allgrove J., Arslan-Kirchner M., Batch J.A., Beighton P., Black G.C., Boles R.G., Boon L.M., Borrone C., Brunner H.G., Carle G.F., Dallapiccola B., De Paepe A., Floege B., Halfhide M.L., Hall B., Hennekam R.C.M., Hirose T., Jans A., Jueppner H., Kim C.A., Keppler-Noreuil K., Kohlschuetter A., LaCombe D., Lambert M., Lemyre E., Letteboer T., Peltonen L., Ramesar R.S., Romanengo M., Somer H., Steichen-Gersdorf E., Steinmann B., Sullivan B., Superti-Furga A., Swoboda W., van den Boogaard M.-J., Van Hul W., Vikkula M., Votruba M., Zabel B., Garcia T., Baron R., Olsen B.R., Warman M.L.
Cell 107:513-523(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPPG GLN-494 AND TRP-570, VARIANT MET-667.
[19]"A mutation in the LDL receptor-related protein 5 gene results in the autosomal dominant high-bone-mass trait."
Little R.D., Carulli J.P., Del Mastro R.G., Dupuis J., Osborne M., Folz C., Manning S.P., Swain P.M., Zhao S.-C., Eustace B., Lappe M.M., Spitzer L., Zweier S., Braunschweiger K., Benchekroun Y., Hu X., Adair R., Chee L. expand/collapse author list , FitzGerald M.G., Tulig C., Caruso A., Tzellas N., Bawa A., Franklin B., McGuire S., Nogues X., Gong G., Allen K.M., Anisowicz A., Morales A.J., Lomedico P.T., Recker S.M., Van Eerdewegh P., Recker R.R., Johnson M.L.
Am. J. Hum. Genet. 70:11-19(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HBM VAL-171.
[20]"High bone density due to a mutation in LDL-receptor-related protein 5."
Boyden L.M., Mao J., Belsky J., Mitzner L., Farhi A., Mitnick M.A., Wu D., Insogna K., Lifton R.P.
N. Engl. J. Med. 346:1513-1521(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HBM VAL-171, CHARACTERIZATION OF VARIANT HBM VAL-171.
[21]"Six novel missense mutations in the LDL receptor-related protein 5 (LRP5) gene in different conditions with an increased bone density."
Van Wesenbeeck L., Cleiren E., Gram J., Beals R.K., Benichou O., Scopelliti D., Key L., Renton T., Bartels C., Gong Y., Warman M.L., de Vernejoul M.-C., Bollerslev J., Van Hul W.
Am. J. Hum. Genet. 72:763-771(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPTA1 TYR-111; ARG-171; THR-242 AND ILE-253, VARIANTS WENHY THR-214; VAL-214 AND THR-242, VARIANT VBCH2 THR-242, VARIANTS 18-LEU--LEU-20 DEL; LEU-20 INS; ARG-89; MET-667 AND VAL-1330.
[22]"Mutations in LRP5 or FZD4 underlie the common familial exudative vitreoretinopathy locus on chromosome 11q."
Toomes C., Bottomley H.M., Jackson R.M., Towns K.V., Scott S., Mackey D.A., Craig J.E., Jiang L., Yang Z., Trembath R., Woodruff G., Gregory-Evans C.Y., Gregory-Evans K., Parker M.J., Black G.C.M., Downey L.M., Zhang K., Inglehearn C.F.
Am. J. Hum. Genet. 74:721-730(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EVR4 MET-173; HIS-1168 AND GLY-1361, VARIANT VAL-1525.
[23]"Polymorphisms in the low-density lipoprotein receptor-related protein 5 (LRP5) gene are associated with variation in vertebral bone mass, vertebral bone size, and stature in whites."
Ferrari S.L., Deutsch S., Choudhury U., Chevalley T., Bonjour J.-P., Dermitzakis E.T., Rizzoli R., Antonarakis S.E.
Am. J. Hum. Genet. 74:866-875(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MET-667 AND VAL-1330.
[24]"Autosomal recessive familial exudative vitreoretinopathy is associated with mutations in LRP5."
Jiao X., Ventruto V., Trese M.T., Shastry B.S., Hejtmancik J.F.
Am. J. Hum. Genet. 75:878-884(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EVR4 GLN-570; GLY-752 AND LYS-1367.
[25]"LRP5, low-density-lipoprotein-receptor-related protein 5, is a determinant for bone mineral density."
Mizuguchi T., Furuta I., Watanabe Y., Tsukamoto K., Tomita H., Tsujihata M., Ohta T., Kishino T., Matsumoto N., Minakami H., Niikawa N., Yoshiura K.
J. Hum. Genet. 49:80-86(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-89 AND VAL-1330, FUNCTION, INVOLVEMENT IN OSTEOPOROSIS.
[26]"Clinical and molecular findings in osteoporosis-pseudoglioma syndrome."
Osteoporosis-Pseudoglioma collaborative group
Ai M., Heeger S., Bartels C.F., Schelling D.K.
Am. J. Hum. Genet. 77:741-753(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPPG ASN-203; MET-244; PHE-307; TRP-348; GLN-353; LEU-356; LYS-390; GLU-400; ARG-404; ASN-434; LYS-460; GLN-494; VAL-520; TRP-570; ARG-610; ASN-683; HIS-733; TYR-1099; CYS-1113 AND ASP-1401, CHARACTERIZATION OF VARIANTS OPPG MET-244; LEU-356; LYS-390; ARG-404; ASN-434; VAL-520 AND ARG-610, CHARACTERIZATION OF VARIANTS EVR4 MET-173; GLN-570; HIS-1168; GLY-1361 AND LYS-1367.
[27]"Complexity of the genotype-phenotype correlation in familial exudative vitreoretinopathy with mutations in the LRP5 and/or FZD4 genes."
Qin M., Hayashi H., Oshima K., Tahira T., Hayashi K., Kondo H.
Hum. Mutat. 26:104-112(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EVR4 PHE-145; CYS-444; THR-522; MET-535; ARG-610; CYS-617; ALA-798 AND ASP-1121, VARIANTS VAL-97 AND MET-1540.
[28]"Heterozygous mutations in the LDL receptor-related protein 5 (LRP5) gene are associated with primary osteoporosis in children."
Hartikka H., Makitie O., Mannikko M., Doria A.S., Daneman A., Cole W.G., Ala-Kokko L., Sochett E.B.
J. Bone Miner. Res. 20:783-789(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PRIMARY OSTEOPOROSIS THR-29 AND GLN-1036.
[29]"Oropharyngeal skeletal disease accompanying high bone mass and novel LRP5 mutation."
Rickels M.R., Zhang X., Mumm S., Whyte M.P.
J. Bone Miner. Res. 20:878-885(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HBM MET-154.
[30]"Missense mutations in LRP5 are not a common cause of idiopathic osteoporosis in adult men."
Crabbe P., Balemans W., Willaert A., van Pottelbergh I., Cleiren E., Coucke P.J., Ai M., Goemaere S., van Hul W., de Paepe A., Kaufman J.-M.
J. Bone Miner. Res. 20:1951-1959(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IDIOPATHIC OSTEOPOROSIS LEU-356 AND LEU-455, VARIANT THR-1537, CHARACTERIZATION OF VARIANTS IDIOPATHIC OSTEOPOROSIS LEU-356 AND LEU-455, CHARACTERIZATION OF VARIANT THR-1537.
[31]"A family with osteoporosis pseudoglioma syndrome due to compound heterozygosity of two novel mutations in the LRP5 gene."
Cheung W.M.W., Jin L.Y., Smith D.K., Cheung P.T., Kwan E.Y.W., Low L., Kung A.W.C.
Bone 39:470-476(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPPG ARG-478 AND CYS-504.
[32]"Reduced bone mineral density and hyaloid vasculature remnants in a consanguineous recessive FEVR family with a mutation in LRP5."
Downey L.M., Bottomley H.M., Sheridan E., Ahmed M., Gilmour D.F., Inglehearn C.F., Reddy A., Agrawal A., Bradbury J., Toomes C.
Br. J. Ophthalmol. 90:1163-1167(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EVR4 ARG-550.
[33]"A novel mutation in the LRP5 gene is associated with osteoporosis-pseudoglioma syndrome."
Barros E.R., Dias da Silva M.R., Kunii I.S., Hauache O.M., Lazaretti-Castro M.
Osteoporos. Int. 18:1017-1018(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OPPG ILE-531.
[34]"Osteoporosis-pseudoglioma syndrome: description of 9 new cases and beneficial response to bisphosphonates."
Streeten E.A., McBride D., Puffenberger E., Hoffman M.E., Pollin T.I., Donnelly P., Sack P., Morton H.
Bone 43:584-590(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OPPG ALA-409.
[35]"A mutation in the signal sequence of LRP5 in a family with an osteoporosis-pseudoglioma syndrome (OPPG)-like phenotype indicates a novel disease mechanism for trinucleotide repeats."
Chung B.D., Kayserili H., Ai M., Freudenberg J., Uzumcu A., Uyguner O., Bartels C.F., Honing S., Ramirez A., Hanisch F.G., Nurnberg G., Nurnberg P., Warman M.L., Wollnik B., Kubisch C., Netzer C.
Hum. Mutat. 30:641-648(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT 15-LEU--LEU-20 DEL.
[36]"Clinical and molecular evaluation of probands and family members with familial exudative vitreoretinopathy."
Boonstra F.N., van Nouhuys C.E., Schuil J., de Wijs I.J., van der Donk K.P., Nikopoulos K., Mukhopadhyay A., Scheffer H., Tilanus M.A.D., Cremers F.P.M., Hoefsloot L.H.
Invest. Ophthalmol. Vis. Sci. 50:4379-4385(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EVR4 ALA-511 AND TRP-805.
[37]"Overview of the mutation spectrum in familial exudative vitreoretinopathy and Norrie disease with identification of 21 novel variants in FZD4, LRP5, and NDP."
Nikopoulos K., Venselaar H., Collin R.W.J., Riveiro-Alvarez R., Boonstra F.N., Hooymans J.M., Mukhopadhyay A., Shears D., van Bers M., de Wijs I.J., van Essen A.J., Sijmons R.H., Tilanus M.A.D., van Nouhuys C.E., Ayuso C., Hoefsloot L.H., Cremers F.P.M.
Hum. Mutat. 31:656-666(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EVR4 LYS-441 AND PHE-1253.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF077820 mRNA. Translation: AAC72791.1.
AF064548 mRNA. Translation: AAC36467.1.
AF283321, AF283320 Genomic DNA. Translation: AAK52433.1.
AB017498 mRNA. Translation: BAA33051.1.
AP000807 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74705.1.
BC150595 mRNA. Translation: AAI50596.1.
PIRJE0372.
RefSeqNP_002326.2. NM_002335.2.
UniGeneHs.6347.

3D structure databases

ProteinModelPortalO75197.
SMRO75197. Positions 32-1367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110220. 8 interactions.
DIPDIP-47265N.
IntActO75197. 7 interactions.
MINTMINT-1189744.
STRING9606.ENSP00000294304.

PTM databases

PhosphoSiteO75197.

Proteomic databases

PaxDbO75197.
PRIDEO75197.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294304; ENSP00000294304; ENSG00000162337.
GeneID4041.
KEGGhsa:4041.
UCSCuc001ont.3. human.

Organism-specific databases

CTD4041.
GeneCardsGC11P068080.
HGNCHGNC:6697. LRP5.
HPACAB013001.
MIM144750. phenotype.
166710. phenotype.
259770. phenotype.
601813. phenotype.
601884. phenotype.
603506. gene.
607634. phenotype.
607636. phenotype.
neXtProtNX_O75197.
Orphanet2783. Autosomal dominant osteopetrosis type 1.
2790. Autosomal dominant osteosclerosis, Worth type.
891. Familial exudative vitreoretinopathy.
3416. Hyperostosis corticalis generalisata.
85193. Idiopathic juvenile osteoporosis.
2788. Osteoporosis - pseudoglioma.
178377. Osteosclerosis - developmental delay - craniosynostosis.
90050. Retinopathy of prematurity.
PharmGKBPA30455.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG121718.
HOGENOMHOG000230697.
HOVERGENHBG049167.
InParanoidO75197.
KOK03068.
OMALFWTCEA.
OrthoDBEOG75XGK3.
PhylomeDBO75197.
TreeFamTF315253.

Enzyme and pathway databases

SignaLinkO75197.

Gene expression databases

ArrayExpressO75197.
BgeeO75197.
CleanExHS_LRP5.
GenevestigatorO75197.

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. 13 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

GeneWikiLRP5.
GenomeRNAi4041.
NextBio15826.
PROO75197.
SOURCESearch...

Entry information

Entry nameLRP5_HUMAN
AccessionPrimary (citable) accession number: O75197
Secondary accession number(s): Q96TD6, Q9UES7, Q9UP66
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: April 12, 2005
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM