Reviewed, UniProtKB/Swiss-Prot O75197 (LRP5_HUMAN)

Names and origin

Protein names

Recommended name:
    Low-density lipoprotein receptor-related protein 5

Gene names

Name:	LRP5
Synonyms:	LRP7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	Involved in the Wnt/beta catenin signaling pathway, probably by acting as a coreceptor together with Frizzled for Wnt. Ref.4
Subunit structure	Interacts with different Wnt/Frizzled complexes. Interacts with axin. Ref.4
Subcellular location	Membrane; Single-pass type I membrane protein Potential.
Tissue specificity	Widely expressed, with the highest level of expression in the liver.
Post-translational modification	Phosphorylation of the PPPSP motif creates an inducible docking site for axin.
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	Defects in LRP5 are the cause of vitreoretinopathy exudative type 4 (EVR4) [MIM:601813]. EVR4 is 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. EVR4 inheritance can be autosomal dominant or recessive. Ref.10 Ref.12 Genetic variations in LRP5 may be associated with susceptibility to involutional osteoporosis [MIM:166710]; also known as senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mineral density, disrutption of bone microarchitecture, and the alteration of the amount and variety of non-collagenous proteins in bone. Osteoporotic bones are more at risk of fracture. Defects in LRP5 are the cause of osteoporosis pseudoglioma syndrome (OPPG) [MIM:259770]. OPPG is a recessive disorder characterized by very low bone mass and blindness. Individualy with OPPG are prone to develop bone fractures and deformations and have various eye abnormalities, including phthisis bulbi, retinal detachments, falciform folds or persistent vitreal vasculature. Ref.6 Defects in LRP5 are a cause of high bone mass trait (HBM) [MIM:601884]. HBM is a rare phenotype characterized by exceptionally dense bones. HBM individuals show otherwise a completely normal skeletal structure and no other unusual clinical findings. Ref.7 Ref.8 Defects in LRP5 are a cause of endosteal hyperostosis Worth type (WENHY) [MIM:144750]; also known as autosomal dominant osteosclerosis. WENHY is an autosomal dominant sclerosing bone dysplasia clinically characterizd 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. Ref.9 Defects in LRP5 are the cause of osteopetrosis autosomal dominant type 1 (OPTA1) [MIM:607634]. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder 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 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. Ref.9 Defects in LRP5 are the cause of van Buchem disease type 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. Ref.9
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	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Osteopetrosis
Domain	EGF-like domain Repeat Signal Transmembrane
Molecular function	Developmental protein Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW endocytosis Inferred from electronic annotation. Source: UniProtKB-KW lipid metabolic process Ref.1 Traceable author statement. Source: ProtInc multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cell proliferation Traceable author statement. Source: ProtInc
Cellular component	integral to membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
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	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
	Motif	1500 – 1504	5	PPPSP motif
	Motif	1606 – 1610	5	PPPSP motif
	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	18 – 20	3	Missing Ref.9		VAR_021804
	Natural variant	20	1	L → LL Ref.9		VAR_021805
	Natural variant	89	1	Q → R: dbSNP rs41494349. Ref.9 Ref.13		VAR_021806
	Natural variant	111	1	D → Y in OPTA1. Ref.9		VAR_021807
	Natural variant	171	1	G → R in OPTA1. Ref.9		VAR_021808
	Natural variant	171	1	G → V in HBM; also in HBM individuals with enlarged mandible and torus palatinus; impairs inhibition of Wnt signaling by Dkk-1. Ref.7 Ref.8		VAR_021809
	Natural variant	173	1	T → M in an individual with abnormal retinal vasculature and retinal folds. Ref.10		VAR_018465
	Natural variant	214	1	A → T in WENHY. Ref.9		VAR_021810
	Natural variant	214	1	A → V in WENHY. Ref.9		VAR_021811
	Natural variant	242	1	A → T in OPTA1, VBCH2 and WENHY.		VAR_021812
	Natural variant	253	1	T → I in OPTA1. Ref.9		VAR_021813
	Natural variant	494	1	R → Q in OPPG. Ref.6		VAR_021814
	Natural variant	570	1	R → Q in EVR4; autosomal recessive. Ref.12		VAR_021222
	Natural variant	570	1	R → W in OPPG. Ref.6		VAR_021815
	Natural variant	667	1	V → M: dbSNP rs4988321. Ref.6 Ref.9 Ref.11		VAR_021816
	Natural variant	752	1	R → C in EVR4; autosomal recessive. Ref.12		VAR_021223
	Natural variant	1168	1	Y → H in an individual with total retinal detachment and retinoschisis. Ref.10		VAR_018466
	Natural variant	1204	1	V → L: dbSNP rs11607268.		VAR_035208
	Natural variant	1300	1	A → V: dbSNP rs3736228. Ref.9		VAR_049765
	Natural variant	1330	1	A → V: dbSNP rs3736228. Ref.9 Ref.13 Ref.11 Ref.3		VAR_021817
	Natural variant	1361	1	C → G in EVR4; autosomal dominant. Ref.10		VAR_018467
	Natural variant	1367	1	E → K in EVR4; autosomal recessive. Ref.12		VAR_021224
	Natural variant	1525	1	A → V: dbSNP rs1127291. Ref.10 Ref.1		VAR_021225
Experimental info
	Sequence conflict	1525 – 1528	4	Missing in AAK52433. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O75197-1 [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

[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: 9714764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-1525. Tissue: Osteoblast.
[2]	"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: 11401438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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: 12509515] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-1330.
[4]	"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: 14731402] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH AXIN.
[5]	"LDL receptor-related proteins 5 and 6 in Wnt/beta-catenin signaling: arrows point the way." He X., Semenov M., Tamai K., Zeng X. Development 131:1663-1677(2004) [PubMed: 15084453] [Abstract] Cited for: REVIEW.
[6]	"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: 11719191] [Abstract] Cited for: VARIANTS OPPG GLN-494 AND TRP-570, VARIANT MET-667.
[7]	"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: 11741193] [Abstract] Cited for: VARIANT HBM VAL-171.
[8]	"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: 12015390] [Abstract] Cited for: VARIANT HBM VAL-171, CHARACTERIZATION OF VARIANT HBM VAL-171.
[9]	"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: 12579474] [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.
[10]	"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: 15024691] [Abstract] Cited for: VARIANT EVR4 GLY-1361, VARIANTS MET-173; HIS-1168 AND VAL-1525.
[11]	"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: 15077203] [Abstract] Cited for: VARIANTS MET-667 AND VAL-1330.
[12]	"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: 15346351] [Abstract] Cited for: VARIANTS EVR4 GLN-570; CYS-752 AND LYS-1367.
[13]	"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: 14727154] [Abstract] Cited for: VARIANTS ARG-89 AND VAL-1330, INVOLVEMENT IN INVOLUTIONAL OSTEOPOROSIS.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF064548 mRNA. Translation: AAC36467.1. AF283321, AF283320 Genomic DNA. Translation: AAK52433.1. AB017498 mRNA. Translation: BAA33051.1.
IPI	IPI00744811.
PIR	JE0372.
RefSeq	NP_002326.2.
UniGene	Hs.6347
3D structure databases
HSSP	HSSP built from PDB template 1JRF based on UniProtKB P98162.
ModBase	Search...
PTM databases
PhosphoSite	O75197.
Proteomic databases
PRIDE	O75197.
Genome annotation databases
Ensembl	ENSG00000162337. Homo sapiens. [Contig view]
GeneID	4041.
KEGG	hsa:4041.
Organism-specific databases
GeneCards	GC11P067836.
H-InvDB	HIX0035815.
HGNC	HGNC:6697. LRP5.
HPA	CAB013001.
MIM	144750. phenotype. 166710. phenotype. 259770. phenotype. 601813. phenotype. 601884. phenotype. 603506. gene. 607634. phenotype. 607636. phenotype.
Orphanet	891. Exudative retinopathy, familial. 2783. Osteopetrosis, autosomal dominant, type 1. 2788. Osteoporosis - pseudoglioma. 2790. Osteosclerosis, autosomal dominant, Worth type.
PharmGKB	PA30455.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	O75197.
OMA	O75197. LFWTCEA.
Gene expression databases
ArrayExpress	O75197.
Bgee	O75197.
CleanEx	HS_LRP5.
GermOnline	ENSG00000162337. Homo sapiens.
Family and domain databases
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR018097. EGF_Ca_bd_CS. IPR002172. LDL_rcpt_classA_cys-rich. IPR000033. LDLR. IPR017049. Low_density_Lipo_rcpt-rel_p5/6. [Graphical view]
Gene3D	G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 4 hits. G3DSA:4.10.400.10. LDL_rcpt_classA_cys-rich. 3 hits.
Pfam	PF00008. EGF. 3 hits. PF00057. Ldl_recept_a. 3 hits. PF00058. Ldl_recept_b. 19 hits. [Graphical view]
PIRSF	PIRSF036314. LDL_recpt-rel_p5/6. 1 hit.
PRINTS	PR00261. LDLRECEPTOR.
SMART	SM00181. EGF. 4 hits. SM00192. LDLa. 3 hits. SM00135. LY. 20 hits. [Graphical view]
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 Resources
NextBio	15826.
SOURCE	Search...

Entry information

Entry name

LRP5_HUMAN

Accession

Primary (citable) accession number: O75197
Secondary accession number(s): Q96TD6, Q9UP66

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	April 12, 2005
Last modified:	June 16, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)