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UniProtKB - O75096 (LRP4_HUMAN)

UniProt

O75096 - LRP4_HUMAN

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Protein

Low-density lipoprotein receptor-related protein 4

Gene

LRP4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Differentiation, Endocytosis, Wnt signaling pathway

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_163906. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 4
Short name:
LRP-4
Alternative name(s):
Multiple epidermal growth factor-like domains 7
Gene namesi
Name:LRP4
Synonyms:KIAA0816, LRP10, MEGF7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:6696. LRP4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 17251705ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1726 – 174621HelicalSequence AnalysisAdd
BLAST
Topological domaini1747 – 1905159CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Cenani-Lenz syndactyly syndrome (CLSS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:212780
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. 1 Publication
VAR_063776
Natural varianti160 – 1601C → Y in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. 1 Publication
VAR_063777
Natural varianti449 – 4491D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. 1 Publication
VAR_063778
Natural varianti461 – 4611T → P in CLSS. 1 Publication
VAR_063779
Natural varianti473 – 4731L → F in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. 1 Publication
VAR_063780
Natural varianti529 – 5291D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. 1 Publication
VAR_063781
Natural varianti1017 – 10171C → R in CLSS. 1 Publication
VAR_063782
Sclerosteosis 2 (SOST2)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:614305
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1170 – 11701R → W in SOST2; impairs the interaction with SOST; loss of function as facilitator of SOST-mediated inhibition of Wnt signaling. 1 Publication
VAR_066630
Natural varianti1186 – 11861W → S in SOST2; impairs the interaction with SOST; loss of function as facilitator of SOST-mediated inhibition of Wnt signaling. 1 Publication
VAR_066631

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi212780. phenotype.
614305. phenotype.
Orphaneti3258. Cenani-Lenz syndrome.
98913. Postsynaptic congenital myasthenic syndromes.
3152. Sclerosteosis.
PharmGKBiPA30454.

Polymorphism and mutation databases

BioMutaiLRP4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 19051885Low-density lipoprotein receptor-related protein 4PRO_0000017325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 44PROSITE-ProRule annotation
Disulfide bondi34 ↔ 57PROSITE-ProRule annotation
Disulfide bondi51 ↔ 66PROSITE-ProRule annotation
Disulfide bondi71 ↔ 83PROSITE-ProRule annotation
Disulfide bondi78 ↔ 96PROSITE-ProRule annotation
Disulfide bondi90 ↔ 105PROSITE-ProRule annotation
Disulfide bondi110 ↔ 122PROSITE-ProRule annotation
Disulfide bondi117 ↔ 135PROSITE-ProRule annotation
Disulfide bondi129 ↔ 143PROSITE-ProRule annotation
Disulfide bondi148 ↔ 160PROSITE-ProRule annotation
Disulfide bondi155 ↔ 173PROSITE-ProRule annotation
Disulfide bondi167 ↔ 182PROSITE-ProRule annotation
Disulfide bondi191 ↔ 203PROSITE-ProRule annotation
Disulfide bondi198 ↔ 216PROSITE-ProRule annotation
Disulfide bondi210 ↔ 225PROSITE-ProRule annotation
Disulfide bondi231 ↔ 243PROSITE-ProRule annotation
Disulfide bondi238 ↔ 256PROSITE-ProRule annotation
Disulfide bondi250 ↔ 265PROSITE-ProRule annotation
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi270 ↔ 282PROSITE-ProRule annotation
Disulfide bondi277 ↔ 295PROSITE-ProRule annotation
Disulfide bondi289 ↔ 304PROSITE-ProRule annotation
Disulfide bondi312 ↔ 324PROSITE-ProRule annotation
Disulfide bondi319 ↔ 337PROSITE-ProRule annotation
Disulfide bondi331 ↔ 349PROSITE-ProRule annotation
Disulfide bondi358 ↔ 369PROSITE-ProRule annotation
Disulfide bondi365 ↔ 378PROSITE-ProRule annotation
Disulfide bondi380 ↔ 393PROSITE-ProRule annotation
Disulfide bondi399 ↔ 409PROSITE-ProRule annotation
Disulfide bondi405 ↔ 418PROSITE-ProRule annotation
Disulfide bondi420 ↔ 433PROSITE-ProRule annotation
Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi702 ↔ 713PROSITE-ProRule annotation
Disulfide bondi709 ↔ 722PROSITE-ProRule annotation
Glycosylationi719 – 7191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi724 ↔ 736PROSITE-ProRule annotation
Glycosylationi901 – 9011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1077 – 10771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1415 – 14151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1467 – 14671N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO75096.
PaxDbiO75096.
PRIDEiO75096.

PTM databases

PhosphoSiteiO75096.

Expressioni

Tissue specificityi

Expressed in bone; present in osteoblasts and osteocytes. No expression is observed in osteoclast. Expressed in several regions of the brain.1 Publication

Gene expression databases

BgeeiO75096.
CleanExiHS_LRP4.
ExpressionAtlasiO75096. baseline and differential.
GenevisibleiO75096. HS.

Organism-specific databases

HPAiHPA011934.
HPA012300.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SOSTQ9BQB44EBI-310873,EBI-5746563

Protein-protein interaction databases

BioGridi110218. 15 interactions.
IntActiO75096. 4 interactions.
STRINGi9606.ENSP00000367888.

Structurei

3D structure databases

ProteinModelPortaliO75096.
SMRiO75096. Positions 27-1640.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6742LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini70 – 10637LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini109 – 14436LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini147 – 18337LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini190 – 22637LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini230 – 26637LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini269 – 30537LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini311 – 35040LDL-receptor class A 8PROSITE-ProRule annotationAdd
BLAST
Domaini354 – 39441EGF-like 1; calcium-bindingSequence AnalysisAdd
BLAST
Domaini395 – 43440EGF-like 2; calcium-bindingSequence AnalysisAdd
BLAST
Repeati480 – 52243LDL-receptor class B 1Add
BLAST
Repeati523 – 56543LDL-receptor class B 2Add
BLAST
Repeati566 – 60944LDL-receptor class B 3Add
BLAST
Repeati610 – 65243LDL-receptor class B 4Add
BLAST
Repeati653 – 69341LDL-receptor class B 5Add
BLAST
Domaini698 – 73740EGF-like 3Add
BLAST
Repeati785 – 82743LDL-receptor class B 6Add
BLAST
Repeati828 – 87043LDL-receptor class B 7Add
BLAST
Repeati871 – 91444LDL-receptor class B 8Add
BLAST
Repeati915 – 95642LDL-receptor class B 9Add
BLAST
Repeati957 – 99842LDL-receptor class B 10Add
BLAST
Repeati1093 – 113543LDL-receptor class B 11Add
BLAST
Repeati1136 – 117843LDL-receptor class B 12Add
BLAST
Repeati1179 – 122244LDL-receptor class B 13Add
BLAST
Repeati1223 – 126341LDL-receptor class B 14Add
BLAST
Repeati1264 – 130643LDL-receptor class B 15Add
BLAST
Repeati1397 – 143943LDL-receptor class B 16Add
BLAST
Repeati1440 – 148243LDL-receptor class B 17Add
BLAST
Repeati1483 – 152644LDL-receptor class B 18Add
BLAST
Repeati1527 – 156842LDL-receptor class B 19Add
BLAST
Repeati1569 – 161042LDL-receptor class B 20Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1766 – 17694Endocytosis signalSequence Analysis

Sequence similaritiesi

Belongs to the LDLR family.Curated
Contains 3 EGF-like domains.Curated
Contains 8 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 20 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG235850.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000047507.
HOVERGENiHBG049163.
InParanoidiO75096.
OMAiGSQLLWA.
OrthoDBiEOG75XGK3.
PhylomeDBiO75096.
TreeFamiTF315253.

Family and domain databases

Gene3Di2.120.10.30. 4 hits.
4.10.400.10. 8 hits.
InterProiIPR011042. 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.
IPR030799. LRP4.
[Graphical view]
PANTHERiPTHR10529:SF196. PTHR10529:SF196. 1 hit.
PfamiPF12662. cEGF. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 1 hit.
SM00192. LDLa. 8 hits.
SM00135. LY. 20 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 8 hits.
PROSITEiPS00010. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O75096-1 [UniParc]FASTAAdd to basket

« Hide

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

SESQV
Length:1,905
Mass (Da):212,045
Last modified:November 24, 2009 - v4
Checksum:iA39117C18279F9AA
GO

Sequence cautioni

The sequence BAE19679.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1472 – 14754EPRA → D in BAE19679 (PubMed:9693030).Curated
Sequence conflicti1478 – 14781V → A in BAE19679 (PubMed:9693030).Curated
Sequence conflicti1862 – 18621T → M in BAD83615 (Ref. 1) Curated
Sequence conflicti1862 – 18621T → M in BAA32468 (PubMed:9693030).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. 1 Publication
VAR_063776
Natural varianti160 – 1601C → Y in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. 1 Publication
VAR_063777
Natural varianti314 – 3141L → S.
Corresponds to variant rs7926667 [ dbSNP | Ensembl ].		VAR_058290
Natural varianti449 – 4491D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. 1 Publication
VAR_063778
Natural varianti461 – 4611T → P in CLSS. 1 Publication
VAR_063779
Natural varianti473 – 4731L → F in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. 1 Publication
VAR_063780
Natural varianti529 – 5291D → N in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling. 1 Publication
VAR_063781
Natural varianti1017 – 10171C → R in CLSS. 1 Publication
VAR_063782
Natural varianti1086 – 10861I → V.3 Publications
Corresponds to variant rs6485702 [ dbSNP | Ensembl ].		VAR_057955
Natural varianti1170 – 11701R → W in SOST2; impairs the interaction with SOST; loss of function as facilitator of SOST-mediated inhibition of Wnt signaling. 1 Publication
VAR_066630
Natural varianti1186 – 11861W → S in SOST2; impairs the interaction with SOST; loss of function as facilitator of SOST-mediated inhibition of Wnt signaling. 1 Publication
VAR_066631
Natural varianti1203 – 12031A → V.
Corresponds to variant rs2306033 [ dbSNP | Ensembl ].		VAR_058291
Natural varianti1238 – 12381A → T.
Corresponds to variant rs2306031 [ dbSNP | Ensembl ].		VAR_058292
Natural varianti1554 – 15541S → G.3 Publications
Corresponds to variant rs2306029 [ dbSNP | Ensembl ].		VAR_057956
Natural varianti1646 – 16461R → Q.3 Publications
Corresponds to variant rs3816614 [ dbSNP | Ensembl ].		VAR_057957

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31478.1.
RefSeqiNP_002325.2. NM_002334.3.
UniGeneiHs.4930.

Genome annotation databases

EnsembliENST00000378623; ENSP00000367888; ENSG00000134569.
GeneIDi4038.
KEGGihsa:4038.
UCSCiuc001ndn.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31478.1.
RefSeqiNP_002325.2. NM_002334.3.
UniGeneiHs.4930.

3D structure databases

ProteinModelPortaliO75096.
SMRiO75096. Positions 27-1640.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110218. 15 interactions.
IntActiO75096. 4 interactions.
STRINGi9606.ENSP00000367888.

PTM databases

PhosphoSiteiO75096.

Polymorphism and mutation databases

BioMutaiLRP4.

Proteomic databases

MaxQBiO75096.
PaxDbiO75096.
PRIDEiO75096.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378623; ENSP00000367888; ENSG00000134569.
GeneIDi4038.
KEGGihsa:4038.
UCSCiuc001ndn.4. human.

Organism-specific databases

CTDi4038.
GeneCardsiGC11M049899.
H-InvDBHIX0009607.
HGNCiHGNC:6696. LRP4.
HPAiHPA011934.
HPA012300.
MIMi212780. phenotype.
604270. gene.
614305. phenotype.
neXtProtiNX_O75096.
Orphaneti3258. Cenani-Lenz syndrome.
98913. Postsynaptic congenital myasthenic syndromes.
3152. Sclerosteosis.
PharmGKBiPA30454.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG235850.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000047507.
HOVERGENiHBG049163.
InParanoidiO75096.
OMAiGSQLLWA.
OrthoDBiEOG75XGK3.
PhylomeDBiO75096.
TreeFamiTF315253.

Enzyme and pathway databases

ReactomeiREACT_163906. ECM proteoglycans.

Miscellaneous databases

ChiTaRSiLRP4. human.
GeneWikiiLow_density_lipoprotein_receptor-related_protein_4.
GenomeRNAii4038.
NextBioi15818.
PROiO75096.
SOURCEiSearch...

Gene expression databases

BgeeiO75096.
CleanExiHS_LRP4.
ExpressionAtlasiO75096. baseline and differential.
GenevisibleiO75096. HS.

Family and domain databases

Gene3Di2.120.10.30. 4 hits.
4.10.400.10. 8 hits.
InterProiIPR011042. 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.
IPR030799. LRP4.
[Graphical view]
PANTHERiPTHR10529:SF196. PTHR10529:SF196. 1 hit.
PfamiPF12662. cEGF. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 1 hit.
SM00192. LDLa. 8 hits.
SM00135. LY. 20 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 8 hits.
PROSITEiPS00010. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiLRP4_HUMAN
AccessioniPrimary (citable) accession number: O75096
Secondary accession number(s): B2RN39, Q4AC85, Q5KTZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 24, 2009
Last modified: July 22, 2015
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.