O75197 (LRP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Low-density lipoprotein receptor-related protein 5
Short name=LRP-5

Gene names

Name:	LRP5
Synonyms:	LR3, LRP7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1615 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.11 Ref.24
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
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.21 Ref.23 Ref.25 Ref.26 Ref.31 Ref.35 Ref.36 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.24 Ref.27 Ref.29 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.17 Ref.25 Ref.30 Ref.32 Ref.33 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.18 Ref.19 Ref.28 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.20 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.20 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.20
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 process	Endocytosis Wnt signaling pathway
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Osteogenesis imperfecta Osteopetrosis
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor 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 receptor 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 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 regulation of blood pressure Inferred from mutant phenotype PubMed 18721193. Source: BHF-UCL regulation of canonical Wnt receptor 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 retinal blood vessel morphogenesis Inferred from mutant phenotype Ref.21Ref.23. Source: BHF-UCL
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell integral to 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_function	Wnt-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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Chain	32 – 1615	1584	Low-density lipoprotein receptor-related protein 5		PRO_0000017328
Regions
	Topological domain	32 – 1384	1353	Extracellular Potential
	Transmembrane	1385 – 1407	23	Helical; Potential
	Topological domain	1408 – 1615	208	Cytoplasmic Potential
	Repeat	75 – 119	45	LDL-receptor class B 1
	Repeat	78 – 81	4	YWTD 1
	Repeat	120 – 162	43	LDL-receptor class B 2
	Repeat	123 – 126	4	YWTD 2
	Repeat	163 – 206	44	LDL-receptor class B 3
	Repeat	166 – 169	4	YWTD 3
	Repeat	207 – 247	41	LDL-receptor class B 4
	Repeat	248 – 290	43	LDL-receptor class B 5
	Repeat	251 – 254	4	YWTD 4
	Domain	295 – 337	43	EGF-like 1
	Repeat	385 – 427	43	LDL-receptor class B 6
	Repeat	388 – 391	4	YWTD 5
	Repeat	428 – 470	43	LDL-receptor class B 7
	Repeat	431 – 434	4	YWTD 6
	Repeat	471 – 514	44	LDL-receptor class B 8
	Repeat	474 – 477	4	YWTD 7
	Repeat	515 – 557	43	LDL-receptor class B 9
	Repeat	558 – 600	43	LDL-receptor class B 10
	Repeat	559 – 562	4	YWTD 8
	Domain	601 – 641	41	EGF-like 2
	Repeat	687 – 729	43	LDL-receptor class B 11
	Repeat	690 – 693	4	YWTD 9
	Repeat	730 – 772	43	LDL-receptor class B 12
	Repeat	773 – 815	43	LDL-receptor class B 13
	Repeat	816 – 855	40	LDL-receptor class B 14
	Repeat	819 – 822	4	YWTD 10
	Repeat	856 – 898	43	LDL-receptor class B 15
	Repeat	859 – 862	4	YWTD 11
	Domain	902 – 942	41	EGF-like 3
	Repeat	989 – 1035	47	LDL-receptor class B 16
	Repeat	1036 – 1078	43	LDL-receptor class B 17
	Repeat	1079 – 1123	45	LDL-receptor class B 18
	Repeat	1124 – 1164	41	LDL-receptor class B 19
	Repeat	1165 – 1207	43	LDL-receptor class B 20
	Domain	1213 – 1254	42	EGF-like 4
	Domain	1258 – 1296	39	LDL-receptor class A 1
	Domain	1297 – 1333	37	LDL-receptor class A 2
	Domain	1335 – 1371	37	LDL-receptor class A 3
	Region	32 – 288	257	Beta-propeller 1
	Region	341 – 602	262	Beta-propeller 2
	Region	644 – 903	260	Beta-propeller 3
	Region	945 – 1212	268	Beta-propeller 4
	Motif	1500 – 1506	7	PPPSP motif A
	Motif	1538 – 1545	8	PPPSP motif B
	Motif	1574 – 1581	8	PPPSP motif C
	Motif	1591 – 1596	6	PPPSP motif D
	Motif	1605 – 1612	8	PPPSP motif E
	Compositional bias	1495 – 1610	116	Pro-rich
Amino acid modifications
	Glycosylation	93	1	N-linked (GlcNAc...) Potential
	Glycosylation	138	1	N-linked (GlcNAc...) Potential
	Glycosylation	446	1	N-linked (GlcNAc...) Potential
	Glycosylation	499	1	N-linked (GlcNAc...) Potential
	Glycosylation	705	1	N-linked (GlcNAc...) Potential
	Glycosylation	878	1	N-linked (GlcNAc...) Potential
	Disulfide bond	299 ↔ 310		By similarity
	Disulfide bond	306 ↔ 321		By similarity
	Disulfide bond	323 ↔ 336		By similarity
	Disulfide bond	605 ↔ 616		By similarity
	Disulfide bond	612 ↔ 625		By similarity
	Disulfide bond	627 ↔ 640		By similarity
	Disulfide bond	906 ↔ 917		By similarity
	Disulfide bond	913 ↔ 926		By similarity
	Disulfide bond	928 ↔ 941		By similarity
	Disulfide bond	1217 ↔ 1228		By similarity
	Disulfide bond	1224 ↔ 1238		By similarity
	Disulfide bond	1240 ↔ 1253		By similarity
	Disulfide bond	1259 ↔ 1273		By similarity
	Disulfide bond	1266 ↔ 1286		By similarity
	Disulfide bond	1280 ↔ 1295		By similarity
	Disulfide bond	1298 ↔ 1310		By similarity
	Disulfide bond	1305 ↔ 1323		By similarity
	Disulfide bond	1317 ↔ 1332		By similarity
	Disulfide bond	1336 ↔ 1348		By similarity
	Disulfide bond	1343 ↔ 1361		By similarity
	Disulfide bond	1355 ↔ 1370		By similarity
Natural variations
	Natural variant	15 – 20	6	Missing Found in a family with osteoporosis pseudoglioma syndrome; impairs protein trafficking to the endoplasmic reticulum and cell membrane.		VAR_058582
	Natural variant	18 – 20	3	Missing.		VAR_021804
	Natural variant	20	1	L → LL. Ref.20		VAR_021805
	Natural variant	29	1	A → T in primary osteoporosis. Ref.27		VAR_063941
	Natural variant	89	1	Q → R. Ref.20 Ref.24 Corresponds to variant rs41494349 [ dbSNP | Ensembl ].		VAR_021806
	Natural variant	97	1	A → V. Ref.26		VAR_063942
	Natural variant	111	1	D → Y in OPTA1. Ref.20		VAR_021807
	Natural variant	145	1	L → F in EVR4. Ref.26		VAR_063943
	Natural variant	154	1	R → M in HBM. Ref.28		VAR_063944
	Natural variant	171	1	G → R in OPTA1. Ref.20		VAR_021808
	Natural variant	171	1	G → V in HBM; also in HBM individuals with enlarged mandible and torus palatinus; no enhancement of DKK1 binding by MESD resulting in impaired inhibition of Wnt signaling by DKK1. Ref.15 Ref.18 Ref.19		VAR_021809
	Natural variant	173	1	T → M in EVR4; an individual with abnormal retinal vasculature and retinal folds. Ref.21 Ref.25		VAR_018465
	Natural variant	203	1	D → N in OPPG. Ref.25		VAR_063945
	Natural variant	214	1	A → T in WENHY. Ref.20		VAR_021810
	Natural variant	214	1	A → V in WENHY. Ref.20		VAR_021811
	Natural variant	242	1	A → T in OPTA1, VBCH2 and WENHY. Ref.20		VAR_021812
	Natural variant	244	1	T → 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.25		VAR_063946
	Natural variant	253	1	T → I in OPTA1. Ref.20		VAR_021813
	Natural variant	282	1	M → V in HBM; lowered LRP5-mediated Wnt signaling. No effect on DKK1 binding.		VAR_063412
	Natural variant	307	1	S → F in OPPG. Ref.25		VAR_063947
	Natural variant	348	1	R → W in OPPG. Ref.25		VAR_063948
	Natural variant	353	1	R → Q in OPPG. Ref.25		VAR_063949
	Natural variant	356	1	S → 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.25 Ref.29		VAR_063950
	Natural variant	390	1	T → 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.25		VAR_063951
	Natural variant	400	1	A → E in OPPG. Ref.25		VAR_063952
	Natural variant	404	1	G → 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.25		VAR_063953
	Natural variant	409	1	T → A in OPPG. Ref.33		VAR_063954
	Natural variant	434	1	D → 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.25		VAR_063955
	Natural variant	441	1	E → K in EVR4. Ref.36		VAR_063956
	Natural variant	444	1	R → C in EVR4; associated in a EVR1 patient with mutation GLN-417 in FZD4. Ref.26		VAR_063957
	Natural variant	455	1	S → L in idiopathic osteoporosis; shows an inhibitory effect on Wnt signal transduction. Ref.29		VAR_063958
	Natural variant	460	1	E → K in OPPG. Ref.25		VAR_063959
	Natural variant	478	1	W → R in OPPG. Ref.30		VAR_063960
	Natural variant	494	1	R → Q in OPPG. Ref.17 Ref.25		VAR_021814
	Natural variant	504	1	W → C in OPPG. Ref.30		VAR_063961
	Natural variant	511	1	D → A in EVR4. Ref.35		VAR_063962
	Natural variant	520	1	G → 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.25		VAR_063963
	Natural variant	522	1	A → T in EVR4. Ref.26		VAR_063964
	Natural variant	531	1	N → I in OPPG. Ref.32		VAR_063965
	Natural variant	535	1	T → M in EVR4; autosomal recessive. Ref.26		VAR_063966
	Natural variant	550	1	G → R in EVR4; autosomal recessive. Ref.31		VAR_063967
	Natural variant	570	1	R → Q in EVR4; autosomal recessive; has significantly reduced Wnt or Norrin signal transduction. Ref.23 Ref.25		VAR_021222
	Natural variant	570	1	R → W in OPPG. Ref.17 Ref.25		VAR_021815
	Natural variant	610	1	G → 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.25 Ref.26		VAR_063968
	Natural variant	617	1	F → C in EVR4; autosomal recessive. Ref.26		VAR_063969
	Natural variant	667	1	V → M. Ref.17 Ref.20 Ref.22 Corresponds to variant rs4988321 [ dbSNP | Ensembl ].		VAR_021816
	Natural variant	683	1	D → N in OPPG. Ref.25		VAR_063970
	Natural variant	733	1	Y → H in OPPG. Ref.25		VAR_063971
	Natural variant	752	1	R → G in EVR4; autosomal recessive. Ref.23		VAR_021223
	Natural variant	798	1	T → A in EVR4. Ref.26		VAR_063972
	Natural variant	805	1	R → W in EVR4. Ref.35		VAR_063973
	Natural variant	1036	1	R → Q in primary osteoporosis. Ref.27		VAR_063974
	Natural variant	1099	1	D → Y in OPPG. Ref.25		VAR_063975
	Natural variant	1113	1	R → C in OPPG. Ref.25		VAR_063976
	Natural variant	1121	1	N → D in EVR4. Ref.26		VAR_063977
	Natural variant	1168	1	Y → H in EVR4; an individual with total retinal detachment and retinoschisis; is unable to transduce Wnt or Norrin signal transduction. Ref.21 Ref.25		VAR_018466
	Natural variant	1204	1	V → L. Corresponds to variant rs11607268 [ dbSNP | Ensembl ].		VAR_035208
	Natural variant	1253	1	C → F in EVR4. Ref.36		VAR_063978
	Natural variant	1330	1	A → V. Ref.4 Ref.20 Ref.22 Ref.24 Corresponds to variant rs3736228 [ dbSNP | Ensembl ].		VAR_021817
	Natural variant	1361	1	C → G in EVR4; autosomal dominant; has mildly reduced Wnt or Norrin signal transduction. Ref.21 Ref.25		VAR_018467
	Natural variant	1367	1	E → K in EVR4; autosomal recessive. Ref.23 Ref.25 Corresponds to variant rs28939709 [ dbSNP | Ensembl ].		VAR_021224
	Natural variant	1401	1	G → D in OPPG. Ref.25		VAR_063979
	Natural variant	1525	1	A → V. Ref.2 Ref.21 Corresponds to variant rs1127291 [ dbSNP | Ensembl ].		VAR_021225
	Natural variant	1537	1	A → T Could be associated with idiopathic osteoporosis; does not result in a significant alteration of Wnt signal transduction. Ref.29		VAR_063980
	Natural variant	1540	1	T → M. Ref.26		VAR_063981
Experimental info
	Sequence conflict	1525 – 1528	4	Missing in AAK52433. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O75197 [UniParc]. Last modified April 12, 2005. Version 2. Checksum: 8BA25D07F51E02CA	FASTA	1,615	179,145
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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. , 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.
[18]	"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. , 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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.

Web resources

GeneReviews

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.
IPI	IPI00744811.
PIR	JE0372.
RefSeq	NP_002326.2. NM_002335.2.
UniGene	Hs.6347.
3D structure databases
ProteinModelPortal	O75197.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-47265N.
IntAct	O75197. 2 interactions.
MINT	MINT-1189744.
STRING	9606.ENSP00000294304.
PTM databases
PhosphoSite	O75197.
Proteomic databases
PaxDb	O75197.
PRIDE	O75197.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000294304; ENSP00000294304; ENSG00000162337.
GeneID	4041.
KEGG	hsa:4041.
UCSC	uc001ont.3. human.
Organism-specific databases
CTD	4041.
GeneCards	GC11P068080.
HGNC	HGNC:6697. LRP5.
HPA	CAB013001.
MIM	144750. phenotype. 166710. phenotype. 259770. phenotype. 601813. phenotype. 601884. phenotype. 603506. gene. 607634. phenotype. 607636. phenotype.
neXtProt	NX_O75197.
Orphanet	2783. 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.
PharmGKB	PA30455.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG121718.
HOGENOM	HOG000230697.
HOVERGEN	HBG049167.
InParanoid	O75197.
KO	K03068.
OMA	LFWTCEA.
OrthoDB	EOG4RNB7H.
PhylomeDB	O75197.
Enzyme and pathway databases
SignaLink	O75197.
Gene expression databases
ArrayExpress	O75197.
Bgee	O75197.
CleanEx	HS_LRP5.
Genevestigator	O75197.
GermOnline	ENSG00000162337. Homo sapiens.
Family and domain databases
Gene3D	2.120.10.30. 4 hits. 4.10.400.10. 3 hits.
InterPro	IPR011042. 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]
Pfam	PF00057. Ldl_recept_a. 3 hits. PF00058. Ldl_recept_b. 13 hits. [Graphical view]
PIRSF	PIRSF036314. LDL_recpt-rel_p5/6. 1 hit.
SMART	SM00181. EGF. 4 hits. SM00192. LDLa. 3 hits. SM00135. LY. 20 hits. [Graphical view]
SUPFAM	SSF57424. LDL_rcpt_classA_cys-rich. 3 hits.
PROSITE	PS00022. EGF_1. False negative. PS01186. EGF_2. False negative. PS50026. EGF_3. False negative. PS01187. EGF_CA. False negative. PS01209. LDLRA_1. 3 hits. PS50068. LDLRA_2. 3 hits. PS51120. LDLRB. 20 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	4041.
NextBio	15826.
SOURCE	Search...

Entry information

Entry name

LRP5_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.