Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8VI56

- LRP4_MOUSE

UniProt

Q8VI56 - LRP4_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Low-density lipoprotein receptor-related protein 4

Gene

Lrp4

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. calcium ion binding Source: InterPro
  2. protein homodimerization activity Source: UniProtKB
  3. receptor tyrosine kinase binding Source: UniProtKB
  4. scaffold protein binding Source: UniProt

GO - Biological processi

  1. anatomical structure development Source: MGI
  2. dendrite morphogenesis Source: UniProt
  3. dorsal/ventral pattern formation Source: MGI
  4. embryonic digit morphogenesis Source: MGI
  5. embryonic limb morphogenesis Source: MGI
  6. endocytosis Source: UniProtKB-KW
  7. hair follicle development Source: MGI
  8. kidney development Source: MGI
  9. negative regulation of axonogenesis Source: UniProt
  10. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  11. negative regulation of ossification Source: Ensembl
  12. negative regulation of Wnt signaling pathway Source: MGI
  13. odontogenesis of dentin-containing tooth Source: MGI
  14. positive regulation of presynaptic membrane organization Source: UniProt
  15. postsynaptic membrane assembly Source: UniProt
  16. presynaptic membrane assembly Source: UniProt
  17. protein heterotetramerization Source: UniProt
  18. protein localization Source: MGI
  19. proximal/distal pattern formation Source: MGI
  20. receptor clustering Source: MGI
  21. regulation of protein phosphorylation Source: UniProtKB
  22. skeletal muscle acetylcholine-gated channel clustering Source: UniProt
  23. synapse organization Source: UniProt
  24. synaptic growth at neuromuscular junction Source: UniProt
  25. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Differentiation, Endocytosis, Wnt signaling pathway

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 4
Short name:
LRP-4
Alternative name(s):
LDLR dan
Gene namesi
Name:Lrp4
Synonyms:Kiaa0816
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2442252. Lrp4.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: UniProt
  2. dendrite Source: UniProt
  3. integral component of membrane Source: UniProtKB-KW
  4. neuromuscular junction Source: UniProt
  5. neuronal cell body Source: UniProt
  6. plasma membrane Source: MGI
  7. postsynaptic density Source: UniProt
  8. synaptic membrane Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 19051885Low-density lipoprotein receptor-related protein 4PRO_0000017326Add
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

MaxQBiQ8VI56.
PaxDbiQ8VI56.
PRIDEiQ8VI56.

PTM databases

PhosphoSiteiQ8VI56.

Expressioni

Gene expression databases

BgeeiQ8VI56.
GenevestigatoriQ8VI56.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
AgrnP253043EBI-2106160,EBI-2106099From a different organism.
Mesdc2Q9ERE72EBI-2106160,EBI-6662606

Protein-protein interaction databases

IntActiQ8VI56. 13 interactions.
MINTiMINT-6801185.

Structurei

3D structure databases

ProteinModelPortaliQ8VI56.
SMRiQ8VI56. Positions 27-1640.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

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

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1726 – 174621HelicalSequence AnalysisAdd
BLAST

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; atypicalAdd
BLAST
Domaini395 – 43440EGF-like 2; calcium-bindingAdd
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

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.
InParanoidiQ8VI56.
OMAiPAPPCNL.
OrthoDBiEOG75XGK3.
PhylomeDBiQ8VI56.
TreeFamiTF315253.

Family and domain databases

Gene3Di2.120.10.30. 4 hits.
4.10.400.10. 7 hits.
InterProiIPR011042. 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]
PfamiPF07645. EGF_CA. 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.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8VI56-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRRWWGALLL GALLCAHGIA SSLECACGRS HFTCAVSALG ECTCIPAQWQ
60 70 80 90 100
CDGDNDCGDH SDEDGCTLPT CSPLDFHCDN GKCIRRSWVC DGDNDCEDDS
110 120 130 140 150
DEQDCPPREC EEDEFPCQNG YCIRSLWHCD GDNDCGDNSD EQCDMRKCSD
160 170 180 190 200
KEFRCSDGSC IAEHWYCDGD TDCKDGSDEE SCPSAVPSPP CNLEEFQCAY
210 220 230 240 250
GRCILDIYHC DGDDDCGDWS DESDCSSHQP CRSGEFMCDS GLCINSGWRC
260 270 280 290 300
DGDADCDDQS DERNCTTSMC TAEQFRCRSG RCVRLSWRCD GEDDCADNSD
310 320 330 340 350
EENCENTGSP QCASDQFLCW NGRCIGQRKL CNGINDCGDS SDESPQQNCR
360 370 380 390 400
PRTGEENCNV NNGGCAQKCQ MVRGAVQCTC HTGYRLTEDG RTCQDVNECA
410 420 430 440 450
EEGYCSQGCT NTEGAFQCWC EAGYELRPDR 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
QSLEKPRAIA 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 INSHACAQSL 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 ASSRQVIISS
910 920 930 940 950
NLTWPNGLAI DYGSQRLYWA DAGMKTIEFA GLDGSKRKVL IGSQLPHPFG
960 970 980 990 1000
LTLYGQRIYW TDWQTKSIQS ADRLTGLDRE TLQENLENLM DIHVFHRQRP
1010 1020 1030 1040 1050
PVTTLCAVEN GGCSHLCLRS PNPSGFSCTC PTGINLLRDG KTCSPGMNSF
1060 1070 1080 1090 1100
LIFARRIDVR MVSLDIPYFA DVVVPINMTM KNTIAIGVDP LEGKVYWSDS
1110 1120 1130 1140 1150
TLHRISRASL DGSQHEDIIT TGLQTTDGLA VDAIGRKVYW TDTGTNRIEV
1160 1170 1180 1190 1200
GNLDGSMRKV LVWQNLDSPR AIVLYHEMGF MYWTDWGENA KLERSGMDGS
1210 1220 1230 1240 1250
DRTVLINNNL GWPNGLTVDK TSSQLLWADA HTERIEVADL NGANRHTLVS
1260 1270 1280 1290 1300
PVQHPYGLTL LDSYIYWTDW QTRSIHRADK STGSNVILVR SNLPGLMDIQ
1310 1320 1330 1340 1350
AVDRAQPLGF NKCGSRNGGC SHLCLPRPSG FSCACPTGIQ LKGDRKTCDP
1360 1370 1380 1390 1400
SPETYLLFSS RGSIRRISLD TDDHTDVHVP VPGLNNVISL DYDSVHGKVY
1410 1420 1430 1440 1450
YTDVFLDVIR RADLNGSNME TVIGHGLKTT 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 DEPDGHPCSL
1660 1670 1680 1690 1700
VPGLVPPAPR ATSMNEKSPV LPNTLPTTLH SSTTKTRTSL EGAGGRCSER
1710 1720 1730 1740 1750
DAQLGLCAHS NEAVPAAPGE GLHVSYAIGG LLSILLILLV IAALMLYRHR
1760 1770 1780 1790 1800
KSKFTDPGMG NLTYSNPSYR TSTQEVKLEA APKPAVYNQL CYKKEGGPDH
1810 1820 1830 1840 1850
SYTKEKIKIV EGIRLLAGDD AEWGDLKQLR SSRGGLLRDH VCMKTDTVSI
1860 1870 1880 1890 1900
QASSGSLDDT ETEQLLQEEQ SECSSVHTAA TPERRGSLPD TGWKHERKLS

SESQV
Length:1,905
Mass (Da):211,954
Last modified:June 16, 2009 - v3
Checksum:i282CA859B76D9BAD
GO
Isoform 2 (identifier: Q8VI56-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,848
Mass (Da):205,373
Checksum:iD494D4B76036B93F
GO

Sequence cautioni

The sequence BAC27835.1 differs from that shown. Reason: Intron retention.
The sequence BAC29416.1 differs from that shown. Reason: Intron retention.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961F → L in BAC27835. (PubMed:16141072)Curated
Sequence conflicti325 – 3251I → L in BAC29416. (PubMed:16141072)Curated
Sequence conflicti380 – 3801C → R in AAL36970. 1 PublicationCurated
Sequence conflicti682 – 6854HFPM → LHTP(PubMed:14621295)Curated
Sequence conflicti1330 – 13301G → S in AAL36970. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1564 – 162057Missing in isoform 2. 1 PublicationVSP_010034Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS16432.1. [Q8VI56-1]
RefSeqiNP_001139329.1. NM_001145857.1.
NP_766256.3. NM_172668.3. [Q8VI56-1]
UniGeneiMm.275149.
Mm.469960.

Genome annotation databases

EnsembliENSMUST00000028689; ENSMUSP00000028689; ENSMUSG00000027253. [Q8VI56-1]
GeneIDi228357.
KEGGimmu:228357.
UCSCiuc008kvx.2. mouse. [Q8VI56-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS16432.1. [Q8VI56-1 ]
RefSeqi NP_001139329.1. NM_001145857.1.
NP_766256.3. NM_172668.3. [Q8VI56-1 ]
UniGenei Mm.275149.
Mm.469960.

3D structure databases

ProteinModelPortali Q8VI56.
SMRi Q8VI56. Positions 27-1640.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8VI56. 13 interactions.
MINTi MINT-6801185.

PTM databases

PhosphoSitei Q8VI56.

Proteomic databases

MaxQBi Q8VI56.
PaxDbi Q8VI56.
PRIDEi Q8VI56.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028689 ; ENSMUSP00000028689 ; ENSMUSG00000027253 . [Q8VI56-1 ]
GeneIDi 228357.
KEGGi mmu:228357.
UCSCi uc008kvx.2. mouse. [Q8VI56-1 ]

Organism-specific databases

CTDi 4038.
MGIi MGI:2442252. Lrp4.
Rougei Search...

Phylogenomic databases

eggNOGi NOG235850.
GeneTreei ENSGT00760000118968.
HOGENOMi HOG000047507.
HOVERGENi HBG049163.
InParanoidi Q8VI56.
OMAi PAPPCNL.
OrthoDBi EOG75XGK3.
PhylomeDBi Q8VI56.
TreeFami TF315253.

Miscellaneous databases

NextBioi 378964.
PROi Q8VI56.
SOURCEi Search...

Gene expression databases

Bgeei Q8VI56.
Genevestigatori Q8VI56.

Family and domain databases

Gene3Di 2.120.10.30. 4 hits.
4.10.400.10. 7 hits.
InterProi IPR011042. 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 ]
Pfami PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view ]
PRINTSi PR00261. LDLRECEPTOR.
SMARTi SM00181. EGF. 4 hits.
SM00179. EGF_CA. 1 hit.
SM00192. LDLa. 8 hits.
SM00135. LY. 20 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 8 hits.
PROSITEi PS00010. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. Cited for: FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, FUNCTION AS RECEPTOR FOR AGRIN, INTERACTION WITH AGRIN AND MUSK.
  7. Cited for: FUNCTION.

Entry informationi

Entry nameiLRP4_MOUSE
AccessioniPrimary (citable) accession number: Q8VI56
Secondary accession number(s): A2AGT4
, Q8BPX5, Q8CBB3, Q8CCP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 16, 2009
Last modified: October 29, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3