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Q8VI56 (LRP4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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):
LDLR dan
Gene names
Name:Lrp4
Synonyms:Kiaa0816
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.6 Ref.7

Subunit structure

Homooligomer. Interacts with MUSK; the heterodimer forms an AGRIN receptor complex that binds AGRIN resulting in activation of MUSK. Interacts (via the extracellular domain) with SOST; the interaction facilitates the inhibition of Wnt signaling By similarity. Ref.6

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

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 BAC27835.1 differs from that shown. Reason: Intron retention.

The sequence BAC29416.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processDifferentiation
Endocytosis
Wnt signaling pathway
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   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

anatomical structure development

Inferred from mutant phenotype PubMed 17119023. Source: MGI

dendrite morphogenesis

Inferred from sequence or structural similarity. Source: UniProt

dorsal/ventral pattern formation

Inferred from mutant phenotype PubMed 16207730PubMed 17119023. Source: MGI

embryonic digit morphogenesis

Inferred from mutant phenotype PubMed 16517118. Source: MGI

embryonic limb morphogenesis

Inferred from mutant phenotype PubMed 16207730PubMed 17119023. Source: MGI

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

hair follicle development

Inferred from mutant phenotype PubMed 17119023. Source: MGI

kidney development

Inferred from mutant phenotype PubMed 17119023. Source: MGI

negative regulation of Wnt signaling pathway

Inferred from direct assay PubMed 16207730. Source: MGI

negative regulation of axonogenesis

Inferred from mutant phenotype PubMed 22854782. Source: UniProt

negative regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of ossification

Inferred from electronic annotation. Source: Ensembl

odontogenesis of dentin-containing tooth

Inferred from mutant phenotype PubMed 17119023. Source: MGI

positive regulation of presynaptic membrane organization

Inferred from direct assay PubMed 22854782. Source: UniProt

postsynaptic membrane assembly

Inferred from mutant phenotype PubMed 22038977. Source: UniProt

presynaptic membrane assembly

Inferred from mutant phenotype PubMed 22038977. Source: UniProt

protein heterotetramerization

Inferred from sequence or structural similarity. Source: UniProt

protein localization

Inferred from mutant phenotype PubMed 17119023. Source: MGI

proximal/distal pattern formation

Inferred from mutant phenotype PubMed 17119023. Source: MGI

receptor clustering

Inferred from mutant phenotype PubMed 17119023. Source: MGI

regulation of protein phosphorylation

Inferred from mutant phenotype Ref.6. Source: UniProtKB

skeletal muscle acetylcholine-gated channel clustering

Inferred from mutant phenotype PubMed 22038977PubMed 22854782. Source: UniProt

synapse organization

Inferred from sequence or structural similarity. Source: UniProt

synaptic growth at neuromuscular junction

Inferred from direct assay PubMed 18957220. Source: UniProt

   Cellular_componentcell surface

Inferred from sequence or structural similarity. 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 direct assay PubMed 18957220. Source: UniProt

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProt

plasma membrane

Inferred from direct assay PubMed 16263759. Source: MGI

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

protein binding

Inferred from physical interaction Ref.6PubMed 24140340. Source: IntAct

protein homodimerization activity

Inferred from direct assay Ref.6. Source: UniProtKB

receptor tyrosine kinase binding

Inferred from physical interaction Ref.6. Source: UniProtKB

scaffold protein binding

Inferred from sequence or structural similarity. Source: UniProt

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AgrnP253043EBI-2106160,EBI-2106099From a different organism.
Mesdc2Q9ERE72EBI-2106160,EBI-6662606

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VI56-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8VI56-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1564-1620: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 19051885Low-density lipoprotein receptor-related protein 4
PRO_0000017326

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; atypical
Domain395 – 43440EGF-like 2; calcium-binding
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

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

Alternative sequence1564 – 162057Missing in isoform 2.
VSP_010034

Experimental info

Sequence conflict1961F → L in BAC27835. Ref.4
Sequence conflict3251I → L in BAC29416. Ref.4
Sequence conflict3801C → R in AAL36970. Ref.1
Sequence conflict682 – 6854HFPM → LHTP Ref.5
Sequence conflict13301G → S in AAL36970. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: 282CA859B76D9BAD

FASTA1,905211,954
        10         20         30         40         50         60 
MRRWWGALLL GALLCAHGIA SSLECACGRS HFTCAVSALG ECTCIPAQWQ CDGDNDCGDH 

        70         80         90        100        110        120 
SDEDGCTLPT CSPLDFHCDN GKCIRRSWVC DGDNDCEDDS DEQDCPPREC EEDEFPCQNG 

       130        140        150        160        170        180 
YCIRSLWHCD GDNDCGDNSD EQCDMRKCSD KEFRCSDGSC IAEHWYCDGD TDCKDGSDEE 

       190        200        210        220        230        240 
SCPSAVPSPP CNLEEFQCAY GRCILDIYHC DGDDDCGDWS DESDCSSHQP CRSGEFMCDS 

       250        260        270        280        290        300 
GLCINSGWRC DGDADCDDQS DERNCTTSMC TAEQFRCRSG RCVRLSWRCD GEDDCADNSD 

       310        320        330        340        350        360 
EENCENTGSP QCASDQFLCW NGRCIGQRKL CNGINDCGDS SDESPQQNCR PRTGEENCNV 

       370        380        390        400        410        420 
NNGGCAQKCQ MVRGAVQCTC HTGYRLTEDG RTCQDVNECA EEGYCSQGCT NTEGAFQCWC 

       430        440        450        460        470        480 
EAGYELRPDR RSCKALGPEP VLLFANRIDI RQVLPHRSEY TLLLNNLENA IALDFHHRRE 

       490        500        510        520        530        540 
LVFWSDVTLD RILRANLNGS NVEEVVSTGL ESPGGLAVDW VHDKLYWTDS GTSRIEVANL 

       550        560        570        580        590        600 
DGAHRKVLLW QSLEKPRAIA 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 INSHACAQSL 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 ASSRQVIISS 

       910        920        930        940        950        960 
NLTWPNGLAI DYGSQRLYWA DAGMKTIEFA GLDGSKRKVL IGSQLPHPFG LTLYGQRIYW 

       970        980        990       1000       1010       1020 
TDWQTKSIQS ADRLTGLDRE TLQENLENLM DIHVFHRQRP PVTTLCAVEN GGCSHLCLRS 

      1030       1040       1050       1060       1070       1080 
PNPSGFSCTC PTGINLLRDG KTCSPGMNSF LIFARRIDVR MVSLDIPYFA DVVVPINMTM 

      1090       1100       1110       1120       1130       1140 
KNTIAIGVDP LEGKVYWSDS TLHRISRASL DGSQHEDIIT TGLQTTDGLA VDAIGRKVYW 

      1150       1160       1170       1180       1190       1200 
TDTGTNRIEV GNLDGSMRKV LVWQNLDSPR AIVLYHEMGF MYWTDWGENA KLERSGMDGS 

      1210       1220       1230       1240       1250       1260 
DRTVLINNNL GWPNGLTVDK TSSQLLWADA HTERIEVADL NGANRHTLVS PVQHPYGLTL 

      1270       1280       1290       1300       1310       1320 
LDSYIYWTDW QTRSIHRADK STGSNVILVR SNLPGLMDIQ AVDRAQPLGF NKCGSRNGGC 

      1330       1340       1350       1360       1370       1380 
SHLCLPRPSG FSCACPTGIQ LKGDRKTCDP SPETYLLFSS RGSIRRISLD TDDHTDVHVP 

      1390       1400       1410       1420       1430       1440 
VPGLNNVISL DYDSVHGKVY YTDVFLDVIR RADLNGSNME TVIGHGLKTT 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 DEPDGHPCSL VPGLVPPAPR ATSMNEKSPV LPNTLPTTLH 

      1690       1700       1710       1720       1730       1740 
SSTTKTRTSL EGAGGRCSER DAQLGLCAHS NEAVPAAPGE GLHVSYAIGG LLSILLILLV 

      1750       1760       1770       1780       1790       1800 
IAALMLYRHR KSKFTDPGMG NLTYSNPSYR TSTQEVKLEA APKPAVYNQL CYKKEGGPDH 

      1810       1820       1830       1840       1850       1860 
SYTKEKIKIV EGIRLLAGDD AEWGDLKQLR SSRGGLLRDH VCMKTDTVSI QASSGSLDDT 

      1870       1880       1890       1900 
ETEQLLQEEQ SECSSVHTAA TPERRGSLPD TGWKHERKLS SESQV 

« Hide

Isoform 2 [UniParc].

Checksum: D494D4B76036B93F
Show »

FASTA1,848205,373

References

« Hide 'large scale' references
[1]"Characterization of an insertional mutation responsible for abnormal limb development."
Simon-Chazottes D.C., Tutois S., Bourgade F., Evans M.J., Kuehn M.R., Guenet J.-L.
(In) Proceedings of the 14th international mouse genome conference, abstract#B10, Narita (2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: C57BL/6J.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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] (ISOFORM 1).
Tissue: Brain.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-566 (ISOFORMS 1/2).
Strain: C57BL/6J.
Tissue: Bone and Olfactory bulb.
[5]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 682-1905 (ISOFORM 2).
Tissue: Brain.
[6]"Lrp4 is a receptor for Agrin and forms a complex with MuSK."
Kim N., Stiegler A.L., Cameron T.O., Hallock P.T., Gomez A.M., Huang J.H., Hubbard S.R., Dustin M.L., Burden S.J.
Cell 135:334-342(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, FUNCTION AS RECEPTOR FOR AGRIN, INTERACTION WITH AGRIN AND MUSK.
[7]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF247637 mRNA. Translation: AAL36970.1.
AL732478, AL691489 Genomic DNA. Translation: CAM24075.1.
BC132240 mRNA. Translation: AAI32241.1.
AK032360 mRNA. Translation: BAC27835.1. Different termination.
AK036406 mRNA. Translation: BAC29416.1. Sequence problems.
AK129224 Transcribed RNA. Translation: BAC98034.1.
CCDSCCDS16432.1. [Q8VI56-1]
RefSeqNP_001139329.1. NM_001145857.1.
NP_766256.3. NM_172668.3. [Q8VI56-1]
UniGeneMm.275149.
Mm.469960.

3D structure databases

ProteinModelPortalQ8VI56.
SMRQ8VI56. Positions 27-1640.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8VI56. 13 interactions.
MINTMINT-6801185.

PTM databases

PhosphoSiteQ8VI56.

Proteomic databases

PaxDbQ8VI56.
PRIDEQ8VI56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028689; ENSMUSP00000028689; ENSMUSG00000027253. [Q8VI56-1]
GeneID228357.
KEGGmmu:228357.
UCSCuc008kvx.2. mouse. [Q8VI56-1]

Organism-specific databases

CTD4038.
MGIMGI:2442252. Lrp4.
RougeSearch...

Phylogenomic databases

eggNOGNOG235850.
GeneTreeENSGT00750000117273.
HOGENOMHOG000047507.
HOVERGENHBG049163.
InParanoidA2AGT4.
OMAPAPPCNL.
OrthoDBEOG75XGK3.
PhylomeDBQ8VI56.
TreeFamTF315253.

Gene expression databases

BgeeQ8VI56.
GenevestigatorQ8VI56.

Family and domain databases

Gene3D2.120.10.30. 4 hits.
4.10.400.10. 7 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
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]
PfamPF07645. EGF_CA. 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.
PS00022. EGF_1. 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

NextBio378964.
PROQ8VI56.
SOURCESearch...

Entry information

Entry nameLRP4_MOUSE
AccessionPrimary (citable) accession number: Q8VI56
Secondary accession number(s): A2AGT4 expand/collapse secondary AC list , Q8BPX5, Q8CBB3, Q8CCP5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot