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O75096 (LRP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1905 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processDifferentiation
Endocytosis
Wnt signaling pathway
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionDevelopmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

dendrite morphogenesis

Inferred from sequence or structural similarity. Source: UniProt

dorsal/ventral pattern formation

Inferred from electronic annotation. Source: Ensembl

embryonic digit morphogenesis

Inferred from electronic annotation. Source: Ensembl

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix organization

Traceable author statement. Source: Reactome

hair follicle development

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from direct assay Ref.5. Source: UniProt

limb development

Inferred from direct assay Ref.5. Source: UniProt

negative regulation of axonogenesis

Inferred from sequence or structural similarity. Source: UniProt

negative regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype Ref.5Ref.6. Source: UniProtKB

negative regulation of ossification

Inferred from mutant phenotype Ref.6. Source: UniProtKB

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

positive regulation of presynaptic membrane organization

Inferred from sequence or structural similarity. Source: UniProt

postsynaptic membrane assembly

Inferred from sequence or structural similarity. Source: UniProt

presynaptic membrane assembly

Inferred from sequence or structural similarity. Source: UniProt

protein heterotetramerization

Inferred from sequence or structural similarity. Source: UniProt

proximal/distal pattern formation

Inferred from electronic annotation. Source: Ensembl

regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

skeletal muscle acetylcholine-gated channel clustering

Inferred from sequence or structural similarity. Source: UniProt

synapse organization

Inferred from sequence or structural similarity. Source: UniProt

synaptic growth at neuromuscular junction

Inferred from sequence or structural similarity. Source: UniProt

   Cellular_componentcell surface

Inferred from direct assay Ref.5. Source: UniProt

dendrite

Inferred from sequence or structural similarity. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuromuscular junction

Inferred from sequence or structural similarity. Source: UniProt

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProt

postsynaptic density

Inferred from sequence or structural similarity. Source: UniProt

synaptic membrane

Inferred from sequence or structural similarity. Source: UniProt

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

receptor tyrosine kinase binding

Inferred from sequence or structural similarity. Source: UniProt

scaffold protein binding

Inferred from sequence or structural similarity. Source: UniProt

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 19051885Low-density lipoprotein receptor-related protein 4
PRO_0000017325

Regions

Topological domain21 – 17251705Extracellular Potential
Transmembrane1726 – 174621Helical; Potential
Topological domain1747 – 1905159Cytoplasmic Potential
Domain26 – 6742LDL-receptor class A 1
Domain70 – 10637LDL-receptor class A 2
Domain109 – 14436LDL-receptor class A 3
Domain147 – 18337LDL-receptor class A 4
Domain190 – 22637LDL-receptor class A 5
Domain230 – 26637LDL-receptor class A 6
Domain269 – 30537LDL-receptor class A 7
Domain311 – 35040LDL-receptor class A 8
Domain354 – 39441EGF-like 1; calcium-binding Potential
Domain395 – 43440EGF-like 2; calcium-binding Potential
Repeat480 – 52243LDL-receptor class B 1
Repeat523 – 56543LDL-receptor class B 2
Repeat566 – 60944LDL-receptor class B 3
Repeat610 – 65243LDL-receptor class B 4
Repeat653 – 69341LDL-receptor class B 5
Domain698 – 73740EGF-like 3
Repeat785 – 82743LDL-receptor class B 6
Repeat828 – 87043LDL-receptor class B 7
Repeat871 – 91444LDL-receptor class B 8
Repeat915 – 95642LDL-receptor class B 9
Repeat957 – 99842LDL-receptor class B 10
Repeat1093 – 113543LDL-receptor class B 11
Repeat1136 – 117843LDL-receptor class B 12
Repeat1179 – 122244LDL-receptor class B 13
Repeat1223 – 126341LDL-receptor class B 14
Repeat1264 – 130643LDL-receptor class B 15
Repeat1397 – 143943LDL-receptor class B 16
Repeat1440 – 148243LDL-receptor class B 17
Repeat1483 – 152644LDL-receptor class B 18
Repeat1527 – 156842LDL-receptor class B 19
Repeat1569 – 161042LDL-receptor class B 20
Motif1766 – 17694Endocytosis signal Potential

Amino acid modifications

Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation4981N-linked (GlcNAc...) Potential
Glycosylation7191N-linked (GlcNAc...) Potential
Glycosylation9011N-linked (GlcNAc...) Potential
Glycosylation10771N-linked (GlcNAc...) Potential
Glycosylation14151N-linked (GlcNAc...) Potential
Glycosylation14671N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 44 By similarity
Disulfide bond34 ↔ 57 By similarity
Disulfide bond51 ↔ 66 By similarity
Disulfide bond71 ↔ 83 By similarity
Disulfide bond78 ↔ 96 By similarity
Disulfide bond90 ↔ 105 By similarity
Disulfide bond110 ↔ 122 By similarity
Disulfide bond117 ↔ 135 By similarity
Disulfide bond129 ↔ 143 By similarity
Disulfide bond148 ↔ 160 By similarity
Disulfide bond155 ↔ 173 By similarity
Disulfide bond167 ↔ 182 By similarity
Disulfide bond191 ↔ 203 By similarity
Disulfide bond198 ↔ 216 By similarity
Disulfide bond210 ↔ 225 By similarity
Disulfide bond231 ↔ 243 By similarity
Disulfide bond238 ↔ 256 By similarity
Disulfide bond250 ↔ 265 By similarity
Disulfide bond270 ↔ 282 By similarity
Disulfide bond277 ↔ 295 By similarity
Disulfide bond289 ↔ 304 By similarity
Disulfide bond312 ↔ 324 By similarity
Disulfide bond319 ↔ 337 By similarity
Disulfide bond331 ↔ 349 By similarity
Disulfide bond358 ↔ 369 By similarity
Disulfide bond365 ↔ 378 By similarity
Disulfide bond380 ↔ 393 By similarity
Disulfide bond399 ↔ 409 By similarity
Disulfide bond405 ↔ 418 By similarity
Disulfide bond420 ↔ 433 By similarity
Disulfide bond702 ↔ 713 By similarity
Disulfide bond709 ↔ 722 By similarity
Disulfide bond724 ↔ 736 By similarity

Natural variations

Natural variant1371D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. Ref.5
VAR_063776
Natural variant1601C → Y in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. Ref.5
VAR_063777
Natural variant3141L → S.
Corresponds to variant rs7926667 [ dbSNP | Ensembl ].
VAR_058290
Natural variant4491D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. Ref.5
VAR_063778
Natural variant4611T → P in CLSS. Ref.5
VAR_063779
Natural variant4731L → F in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. Ref.5
VAR_063780
Natural variant5291D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. Ref.5
VAR_063781
Natural variant10171C → R in CLSS. Ref.5
VAR_063782
Natural variant10861I → V. Ref.1 Ref.2 Ref.4
Corresponds to variant rs6485702 [ dbSNP | Ensembl ].
VAR_057955
Natural variant11701R → 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 variant11861W → 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 variant12031A → V.
Corresponds to variant rs2306033 [ dbSNP | Ensembl ].
VAR_058291
Natural variant12381A → T.
Corresponds to variant rs2306031 [ dbSNP | Ensembl ].
VAR_058292
Natural variant15541S → G. Ref.1 Ref.2 Ref.4
Corresponds to variant rs2306029 [ dbSNP | Ensembl ].
VAR_057956
Natural variant16461R → Q. Ref.1 Ref.2 Ref.4
Corresponds to variant rs3816614 [ dbSNP | Ensembl ].
VAR_057957

Experimental info

Sequence conflict1472 – 14754EPRA → D in BAE19679. Ref.2
Sequence conflict14781V → A in BAE19679. Ref.2
Sequence conflict18621T → M in BAD83615. Ref.1
Sequence conflict18621T → M in BAA32468. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O75096 [UniParc].

Last modified November 24, 2009. Version 4.
Checksum: A39117C18279F9AA

FASTA1,905212,045
        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 

« Hide

References

« Hide '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. 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].
[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. expand/collapse author list , 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. expand/collapse author list , 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, VARIANTS SOST2 TRP-1170 AND SER-1186, CHARACTERIZATION OF VARIANTS SOST2 TRP-1170 AND SER-1186, IDENTIFICATION BY MASS SPECTROMETRY.
+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.
RefSeqNP_002325.2. NM_002334.3.
UniGeneHs.4930.

3D structure databases

ProteinModelPortalO75096.
SMRO75096. Positions 25-1650.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110218. 5 interactions.
IntActO75096. 3 interactions.
STRING9606.ENSP00000367888.

PTM databases

PhosphoSiteO75096.

Proteomic databases

PaxDbO75096.
PRIDEO75096.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378623; ENSP00000367888; ENSG00000134569.
GeneID4038.
KEGGhsa:4038.
UCSCuc001ndn.4. human.

Organism-specific databases

CTD4038.
GeneCardsGC11M048796.
H-InvDBHIX0009607.
HGNCHGNC:6696. LRP4.
HPAHPA011934.
HPA012300.
MIM212780. phenotype.
604270. gene.
614305. phenotype.
neXtProtNX_O75096.
Orphanet3258. Cenani-Lenz syndrome.
3152. Sclerosteosis.
PharmGKBPA30454.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG235850.
HOGENOMHOG000047507.
HOVERGENHBG049163.
InParanoidO75096.
OMAPAPPCNL.
OrthoDBEOG75XGK3.
PhylomeDBO75096.
TreeFamTF315253.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressO75096.
BgeeO75096.
CleanExHS_LRP4.
GenevestigatorO75096.

Family and domain databases

Gene3D2.120.10.30. 4 hits.
4.10.400.10. 8 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamPF12662. cEGF. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00181. EGF. 4 hits.
SM00179. EGF_CA. 1 hit.
SM00192. LDLa. 8 hits.
SM00135. LY. 20 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 8 hits.
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS01186. EGF_2. 3 hits.
PS01187. EGF_CA. 1 hit.
PS01209. LDLRA_1. 8 hits.
PS50068. LDLRA_2. 8 hits.
PS51120. LDLRB. 20 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiLow_density_lipoprotein_receptor-related_protein_4.
GenomeRNAi4038.
NextBio15818.
PROO75096.
SOURCESearch...

Entry information

Entry nameLRP4_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 123 of the entry and version 4 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