O75096 (LRP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Low-density lipoprotein receptor-related protein 4
Short name=LRP-4

Alternative name(s):
Multiple epidermal growth factor-like domains 7

Gene names

Name:	LRP4
Synonyms:	KIAA0816, LRP10, MEGF7

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	1905 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	Mediates SOST-dependent inhibition of bone formation. Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling. Plays a key role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Directly binds AGRIN and recruits it to the MUSK signaling complex. Mediates the AGRIN-induced phosphorylation of MUSK, the kinase of the complex. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Alternatively, may be involved in the negative regulation of the canonical Wnt signaling pathway, being able to antagonize the LRP6-mediated activation of this pathway. More generally, has been proposed to function as a cell surface endocytic receptor binding and internalizing extracellular ligands for degradation by lysosomes. Ref.5 Ref.6
Subunit structure	Homooligomer. Interacts with MUSK; the heterodimer forms an AGRIN receptor complex that binds AGRIN resulting in activation of MUSK By similarity. Interacts (via the extracellular domain) with SOST; the interaction facilitates the inhibition of Wnt signaling. Ref.6
Subcellular location	Membrane; Single-pass type I membrane protein Potential.
Tissue specificity	Expressed in bone; present in osteoblasts and osteocytes. No expression is observed in osteoclast. Expressed in several regions of the brain. Ref.6
Involvement in disease	Cenani-Lenz syndactyly syndrome (CLSS) [MIM:212780]: A congenital malformation syndrome defined as complete and complex syndactyly of the hands combined with malformations of the forearm bones and similar manifestations in the lower limbs. It is characterized by fusion and disorganization of metacarpal and phalangeal bones, radius and ulnar shortening, radioulnar synostosis, and severe syndactyly of hands and feet. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Sclerosteosis 2 (SOST2) [MIM:614305]: A sclerosing bone dysplasia characterized by a generalized hyperostosis and sclerosis leading to a markedly thickened skull, with mandible, ribs, clavicles and all long bones also being affected. Due to narrowing of the foramina of the cranial nerves, facial nerve palsy, hearing loss and atrophy of the optic nerves can occur. Sclerosteosis is clinically and radiologically very similar to van Buchem disease, mainly differentiated by hand malformations and a large stature in sclerosteosis patients. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6
Sequence similarities	Belongs to the LDLR family. Contains 3 EGF-like domains. Contains 8 LDL-receptor class A domains. Contains 20 LDL-receptor class B repeats.
Sequence caution	The sequence BAE19679.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Differentiation Endocytosis Wnt signaling pathway
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium
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 Inferred from electronic annotation. Source: UniProtKB-KW dorsal/ventral pattern formation Inferred from electronic annotation. Source: Compara embryonic digit morphogenesis Inferred from electronic annotation. Source: Compara endocytosis Inferred from electronic annotation. Source: UniProtKB-KW hair follicle development Inferred from electronic annotation. Source: Compara kidney development Inferred from electronic annotation. Source: Compara negative regulation of canonical Wnt receptor signaling pathway Inferred from direct assay Ref.5. Source: UniProtKB negative regulation of ossification Inferred from mutant phenotype Ref.6. Source: UniProtKB odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara proximal/distal pattern formation Inferred from electronic annotation. Source: Compara receptor clustering Inferred from electronic annotation. Source: Compara regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara synaptic growth at neuromuscular junction Inferred from electronic annotation. Source: Compara
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 1905	1885	Low-density lipoprotein receptor-related protein 4		PRO_0000017325
Regions
	Topological domain	21 – 1725	1705	Extracellular Potential
	Transmembrane	1726 – 1746	21	Helical; Potential
	Topological domain	1747 – 1905	159	Cytoplasmic Potential
	Domain	26 – 67	42	LDL-receptor class A 1
	Domain	70 – 106	37	LDL-receptor class A 2
	Domain	109 – 144	36	LDL-receptor class A 3
	Domain	147 – 183	37	LDL-receptor class A 4
	Domain	190 – 226	37	LDL-receptor class A 5
	Domain	230 – 266	37	LDL-receptor class A 6
	Domain	269 – 305	37	LDL-receptor class A 7
	Domain	311 – 350	40	LDL-receptor class A 8
	Domain	354 – 394	41	EGF-like 1; calcium-binding Potential
	Domain	395 – 434	40	EGF-like 2; calcium-binding Potential
	Repeat	480 – 522	43	LDL-receptor class B 1
	Repeat	523 – 565	43	LDL-receptor class B 2
	Repeat	566 – 609	44	LDL-receptor class B 3
	Repeat	610 – 652	43	LDL-receptor class B 4
	Repeat	653 – 693	41	LDL-receptor class B 5
	Domain	698 – 737	40	EGF-like 3
	Repeat	785 – 827	43	LDL-receptor class B 6
	Repeat	828 – 870	43	LDL-receptor class B 7
	Repeat	871 – 914	44	LDL-receptor class B 8
	Repeat	915 – 956	42	LDL-receptor class B 9
	Repeat	957 – 998	42	LDL-receptor class B 10
	Repeat	1093 – 1135	43	LDL-receptor class B 11
	Repeat	1136 – 1178	43	LDL-receptor class B 12
	Repeat	1179 – 1222	44	LDL-receptor class B 13
	Repeat	1223 – 1263	41	LDL-receptor class B 14
	Repeat	1264 – 1306	43	LDL-receptor class B 15
	Repeat	1397 – 1439	43	LDL-receptor class B 16
	Repeat	1440 – 1482	43	LDL-receptor class B 17
	Repeat	1483 – 1526	44	LDL-receptor class B 18
	Repeat	1527 – 1568	42	LDL-receptor class B 19
	Repeat	1569 – 1610	42	LDL-receptor class B 20
	Motif	1766 – 1769	4	Endocytosis signal Potential
Amino acid modifications
	Modified residue	1887	1	Phosphoserine By similarity
	Glycosylation	264	1	N-linked (GlcNAc...) Potential
	Glycosylation	498	1	N-linked (GlcNAc...) Potential
	Glycosylation	719	1	N-linked (GlcNAc...) Potential
	Glycosylation	901	1	N-linked (GlcNAc...) Potential
	Glycosylation	1077	1	N-linked (GlcNAc...) Potential
	Glycosylation	1415	1	N-linked (GlcNAc...) Potential
	Glycosylation	1467	1	N-linked (GlcNAc...) Potential
	Disulfide bond	27 ↔ 44		By similarity
	Disulfide bond	34 ↔ 57		By similarity
	Disulfide bond	51 ↔ 66		By similarity
	Disulfide bond	71 ↔ 83		By similarity
	Disulfide bond	78 ↔ 96		By similarity
	Disulfide bond	90 ↔ 105		By similarity
	Disulfide bond	110 ↔ 122		By similarity
	Disulfide bond	117 ↔ 135		By similarity
	Disulfide bond	129 ↔ 143		By similarity
	Disulfide bond	148 ↔ 160		By similarity
	Disulfide bond	155 ↔ 173		By similarity
	Disulfide bond	167 ↔ 182		By similarity
	Disulfide bond	191 ↔ 203		By similarity
	Disulfide bond	198 ↔ 216		By similarity
	Disulfide bond	210 ↔ 225		By similarity
	Disulfide bond	231 ↔ 243		By similarity
	Disulfide bond	238 ↔ 256		By similarity
	Disulfide bond	250 ↔ 265		By similarity
	Disulfide bond	270 ↔ 282		By similarity
	Disulfide bond	277 ↔ 295		By similarity
	Disulfide bond	289 ↔ 304		By similarity
	Disulfide bond	312 ↔ 324		By similarity
	Disulfide bond	319 ↔ 337		By similarity
	Disulfide bond	331 ↔ 349		By similarity
	Disulfide bond	358 ↔ 369		By similarity
	Disulfide bond	365 ↔ 378		By similarity
	Disulfide bond	380 ↔ 393		By similarity
	Disulfide bond	399 ↔ 409		By similarity
	Disulfide bond	405 ↔ 418		By similarity
	Disulfide bond	420 ↔ 433		By similarity
	Disulfide bond	702 ↔ 713		By similarity
	Disulfide bond	709 ↔ 722		By similarity
	Disulfide bond	724 ↔ 736		By similarity
Natural variations
	Natural variant	137	1	D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. Ref.5		VAR_063776
	Natural variant	160	1	C → Y in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. Ref.5		VAR_063777
	Natural variant	314	1	L → S. Corresponds to variant rs7926667 [ dbSNP | Ensembl ].		VAR_058290
	Natural variant	449	1	D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. Ref.5		VAR_063778
	Natural variant	461	1	T → P in CLSS. Ref.5		VAR_063779
	Natural variant	473	1	L → F in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. Ref.5		VAR_063780
	Natural variant	529	1	D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. Ref.5		VAR_063781
	Natural variant	1017	1	C → R in CLSS. Ref.5		VAR_063782
	Natural variant	1086	1	I → V. Ref.1 Ref.2 Ref.4 Corresponds to variant rs6485702 [ dbSNP | Ensembl ].		VAR_057955
	Natural variant	1170	1	R → W in SOST2; impairs the interaction with SOST; loss of function as facilitator of SOST-mediated inhibition of Wnt signaling. Ref.6		VAR_066630
	Natural variant	1186	1	W → S in SOST2; impairs the interaction with SOST; loss of function as facilitator of SOST-mediated inhibition of Wnt signaling. Ref.6		VAR_066631
	Natural variant	1203	1	A → V. Corresponds to variant rs2306033 [ dbSNP | Ensembl ].		VAR_058291
	Natural variant	1238	1	A → T. Corresponds to variant rs2306031 [ dbSNP | Ensembl ].		VAR_058292
	Natural variant	1554	1	S → G. Ref.1 Ref.2 Ref.4 Corresponds to variant rs2306029 [ dbSNP | Ensembl ].		VAR_057956
	Natural variant	1646	1	R → Q. Ref.1 Ref.2 Ref.4 Corresponds to variant rs3816614 [ dbSNP | Ensembl ].		VAR_057957
Experimental info
	Sequence conflict	1472 – 1475	4	EPRA → D in BAE19679. Ref.2
	Sequence conflict	1478	1	V → A in BAE19679. Ref.2
	Sequence conflict	1862	1	T → M in BAD83615. Ref.1
	Sequence conflict	1862	1	T → M in BAA32468. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O75096 [UniParc]. Last modified November 24, 2009. Version 4. Checksum: A39117C18279F9AA	FASTA	1,905	212,045
	10 20 30 40 50 60 MRRQWGALLL GALLCAHGLA SSPECACGRS HFTCAVSALG ECTCIPAQWQ CDGDNDCGDH 70 80 90 100 110 120 SDEDGCILPT CSPLDFHCDN GKCIRRSWVC DGDNDCEDDS DEQDCPPREC EEDEFPCQNG 130 140 150 160 170 180 YCIRSLWHCD GDNDCGDNSD EQCDMRKCSD KEFRCSDGSC IAEHWYCDGD TDCKDGSDEE 190 200 210 220 230 240 NCPSAVPAPP CNLEEFQCAY GRCILDIYHC DGDDDCGDWS DESDCSSHQP CRSGEFMCDS 250 260 270 280 290 300 GLCINAGWRC DGDADCDDQS DERNCTTSMC TAEQFRCHSG RCVRLSWRCD GEDDCADNSD 310 320 330 340 350 360 EENCENTGSP QCALDQFLCW NGRCIGQRKL CNGVNDCGDN SDESPQQNCR PRTGEENCNV 370 380 390 400 410 420 NNGGCAQKCQ MVRGAVQCTC HTGYRLTEDG HTCQDVNECA EEGYCSQGCT NSEGAFQCWC 430 440 450 460 470 480 ETGYELRPDR RSCKALGPEP VLLFANRIDI RQVLPHRSEY TLLLNNLENA IALDFHHRRE 490 500 510 520 530 540 LVFWSDVTLD RILRANLNGS NVEEVVSTGL ESPGGLAVDW VHDKLYWTDS GTSRIEVANL 550 560 570 580 590 600 DGAHRKVLLW QNLEKPRAIA LHPMEGTIYW TDWGNTPRIE ASSMDGSGRR IIADTHLFWP 610 620 630 640 650 660 NGLTIDYAGR RMYWVDAKHH VIERANLDGS HRKAVISQGL PHPFAITVFE DSLYWTDWHT 670 680 690 700 710 720 KSINSANKFT GKNQEIIRNK LHFPMDIHTL HPQRQPAGKN RCGDNNGGCT HLCLPSGQNY 730 740 750 760 770 780 TCACPTGFRK ISSHACAQSL DKFLLFARRM DIRRISFDTE DLSDDVIPLA DVRSAVALDW 790 800 810 820 830 840 DSRDDHVYWT DVSTDTISRA KWDGTGQEVV VDTSLESPAG LAIDWVTNKL YWTDAGTDRI 850 860 870 880 890 900 EVANTDGSMR TVLIWENLDR PRDIVVEPMG GYMYWTDWGA SPKIERAGMD ASGRQVIISS 910 920 930 940 950 960 NLTWPNGLAI DYGSQRLYWA DAGMKTIEFA GLDGSKRKVL IGSQLPHPFG LTLYGERIYW 970 980 990 1000 1010 1020 TDWQTKSIQS ADRLTGLDRE TLQENLENLM DIHVFHRRRP PVSTPCAMEN GGCSHLCLRS 1030 1040 1050 1060 1070 1080 PNPSGFSCTC PTGINLLSDG KTCSPGMNSF LIFARRIDIR MVSLDIPYFA DVVVPINITM 1090 1100 1110 1120 1130 1140 KNTIAIGVDP QEGKVYWSDS TLHRISRANL DGSQHEDIIT TGLQTTDGLA VDAIGRKVYW 1150 1160 1170 1180 1190 1200 TDTGTNRIEV GNLDGSMRKV LVWQNLDSPR AIVLYHEMGF MYWTDWGENA KLERSGMDGS 1210 1220 1230 1240 1250 1260 DRAVLINNNL GWPNGLTVDK ASSQLLWADA HTERIEAADL NGANRHTLVS PVQHPYGLTL 1270 1280 1290 1300 1310 1320 LDSYIYWTDW QTRSIHRADK GTGSNVILVR SNLPGLMDMQ AVDRAQPLGF NKCGSRNGGC 1330 1340 1350 1360 1370 1380 SHLCLPRPSG FSCACPTGIQ LKGDGKTCDP SPETYLLFSS RGSIRRISLD TSDHTDVHVP 1390 1400 1410 1420 1430 1440 VPELNNVISL DYDSVDGKVY YTDVFLDVIR RADLNGSNME TVIGRGLKTT DGLAVDWVAR 1450 1460 1470 1480 1490 1500 NLYWTDTGRN TIEASRLDGS CRKVLINNSL DEPRAIAVFP RKGYLFWTDW GHIAKIERAN 1510 1520 1530 1540 1550 1560 LDGSERKVLI NTDLGWPNGL TLDYDTRRIY WVDAHLDRIE SADLNGKLRQ VLVSHVSHPF 1570 1580 1590 1600 1610 1620 ALTQQDRWIY WTDWQTKSIQ RVDKYSGRNK ETVLANVEGL MDIIVVSPQR QTGTNACGVN 1630 1640 1650 1660 1670 1680 NGGCTHLCFA RASDFVCACP DEPDSRPCSL VPGLVPPAPR ATGMSEKSPV LPNTPPTTLY 1690 1700 1710 1720 1730 1740 SSTTRTRTSL EEVEGRCSER DARLGLCARS NDAVPAAPGE GLHISYAIGG LLSILLILVV 1750 1760 1770 1780 1790 1800 IAALMLYRHK KSKFTDPGMG NLTYSNPSYR TSTQEVKIEA IPKPAMYNQL CYKKEGGPDH 1810 1820 1830 1840 1850 1860 NYTKEKIKIV EGICLLSGDD AEWDDLKQLR SSRGGLLRDH VCMKTDTVSI QASSGSLDDT 1870 1880 1890 1900 ETEQLLQEEQ SECSSVHTAA TPERRGSLPD TGWKHERKLS SESQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Low density lipoprotein receptor-related protein 10." Ishikawa K., Fujimoto H., Kim D., Saeki S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-1086; GLY-1554 AND GLN-1646. Tissue: Brain.
[2]	"Identification of high-molecular-weight proteins with multiple EGF-like motifs by motif-trap screening." Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O. Genomics 51:27-34(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-1086; GLY-1554 AND GLN-1646. Tissue: Brain.
[3]	"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].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-1086; GLY-1554 AND GLN-1646. Tissue: Muscle.
[5]	"LRP4 mutations alter Wnt/beta-catenin signaling and cause limb and kidney malformations in Cenani-Lenz syndrome." Li Y., Pawlik B., Elcioglu N., Aglan M., Kayserili H., Yigit G., Percin F., Goodman F., Nurnberg G., Cenani A., Urquhart J., Chung B.D., Ismail S., Amr K., Aslanger A.D., Becker C., Netzer C., Scambler P. , Eyaid W., Hamamy H., Clayton-Smith J., Hennekam R., Nurnberg P., Herz J., Temtamy S.A., Wollnik B. Am. J. Hum. Genet. 86:696-706(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN THE REGULATION OF CANONICAL WTN SIGNALING, VARIANTS CLSS ASN-137; TYR-160; ASN-449; PRO-461; PHE-473; ASN-529 AND ARG-1017, CHARACTERIZATION OF VARIANTS CLSS ASN-137; TYR-160; ASN-449; PHE-473 AND ASN-529.
[6]	"Bone overgrowth-associated mutations in the LRP4 gene impair sclerostin facilitator function." Leupin O., Piters E., Halleux C., Hu S., Kramer I., Morvan F., Bouwmeester T., Schirle M., Bueno-Lozano M., Fuentes F.J., Itin P.H., Boudin E., de Freitas F., Jennes K., Brannetti B., Charara N., Ebersbach H., Geisse S. , Lu C.X., Bauer A., Van Hul W., Kneissel M. J. Biol. Chem. 286:19489-19500(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SOST, TISSUE SPECIFICITY, MASS SPECTROMETRY, VARIANTS SOST2 TRP-1170 AND SER-1186, CHARACTERIZATION OF VARIANTS SOST2 TRP-1170 AND SER-1186.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB084910 mRNA. Translation: BAD83615.1. AB011540 mRNA. Translation: BAA32468.1. AB231861 mRNA. Translation: BAE19679.1. Different initiation. AC021573 Genomic DNA. No translation available. BC037360 mRNA. Translation: AAH37360.1. BC041048 mRNA. Translation: AAH41048.1. BC136667 mRNA. Translation: AAI36668.1. BC136668 mRNA. Translation: AAI36669.1.
IPI	IPI00930747.
RefSeq	NP_002325.2. NM_002334.3.
UniGene	Hs.4930.
3D structure databases
ProteinModelPortal	O75096.
SMR	O75096. Positions 27-1640.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75096. 3 interactions.
STRING	9606.ENSP00000367888.
PTM databases
PhosphoSite	O75096.
Proteomic databases
PaxDb	O75096.
PRIDE	O75096.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000378623; ENSP00000367888; ENSG00000134569.
GeneID	4038.
KEGG	hsa:4038.
UCSC	uc001ndn.4. human.
Organism-specific databases
CTD	4038.
GeneCards	GC11M046919.
H-InvDB	HIX0009607.
HGNC	HGNC:6696. LRP4.
HPA	HPA011934. HPA012300.
MIM	212780. phenotype. 604270. gene. 614305. phenotype.
neXtProt	NX_O75096.
Orphanet	3258. Cenani-Lenz syndactyly. 3152. Sclerosteosis.
PharmGKB	PA30454.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG235850.
HOGENOM	HOG000047507.
HOVERGEN	HBG049163.
InParanoid	O75096.
OMA	PAPPCNL.
OrthoDB	EOG405S05.
Gene expression databases
ArrayExpress	O75096.
Bgee	O75096.
CleanEx	HS_LRP4.
Genevestigator	O75096.
GermOnline	ENSG00000134569. Homo sapiens.
Family and domain databases
Gene3D	2.120.10.30. 4 hits. 4.10.400.10. 8 hits.
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR026823. cEGF. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR009030. Growth_fac_rcpt. IPR023415. LDLR_class-A_CS. IPR000033. LDLR_classB_rpt. IPR002172. LDrepeatLR_classA_rpt. [Graphical view]
Pfam	PF12662. cEGF. 1 hit. PF00057. Ldl_recept_a. 8 hits. PF00058. Ldl_recept_b. 16 hits. [Graphical view]
SMART	SM00181. EGF. 4 hits. SM00179. EGF_CA. 1 hit. SM00192. LDLa. 8 hits. SM00135. LY. 20 hits. [Graphical view]
SUPFAM	SSF57184. Grow_fac_recept. 1 hit. SSF57424. LDL_rcpt_classA_cys-rich. 8 hits.
PROSITE	PS00010. ASX_HYDROXYL. 1 hit. PS00022. EGF_1. False negative. PS01186. EGF_2. 3 hits. PS50026. EGF_3. False negative. PS01187. EGF_CA. 1 hit. PS01209. LDLRA_1. 8 hits. PS50068. LDLRA_2. 8 hits. PS51120. LDLRB. 20 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	4038.
NextBio	15818.
SOURCE	Search...

Entry information

Entry name

LRP4_HUMAN

Accession

Primary (citable) accession number: O75096
Secondary accession number(s): B2RN39, Q4AC85, Q5KTZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	November 24, 2009
Last modified:	May 1, 2013
This is version 113 of the entry and version 4 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.