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Protein

Low-density lipoprotein receptor-related protein 4

Gene

Lrp4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates SOST-dependent inhibition of bone formation (By similarity). Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling (By similarity). 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.By similarity

GO - Molecular functioni

  • apolipoprotein binding Source: UniProtKB
  • calcium ion binding Source: InterPro
  • receptor tyrosine kinase binding Source: UniProtKB
  • scaffold protein binding Source: UniProtKB

GO - Biological processi

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):
Multiple epidermal growth factor-like domains 7
Gene namesi
Name:Lrp4
Synonyms:Megf7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi619731. Lrp4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 17231703ExtracellularSequence analysisAdd
BLAST
Transmembranei1724 – 174623HelicalSequence analysisAdd
BLAST
Topological domaini1747 – 1905159CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • dendrite Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • neuromuscular junction Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • plasma membrane Source: Reactome
  • postsynaptic density Source: UniProtKB
  • synaptic membrane Source: UniProtKB
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_0000017327Add
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

PaxDbiQ9QYP1.
PRIDEiQ9QYP1.

PTM databases

iPTMnetiQ9QYP1.
PhosphoSiteiQ9QYP1.

Expressioni

Tissue specificityi

Expressed in different regions of the brain, mainly in the olfactory bulb, at lower level in the cerebral cortex and hippocampus.1 Publication

Gene expression databases

ExpressionAtlasiQ9QYP1. baseline and differential.
GenevisibleiQ9QYP1. RN.

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

GO - Molecular functioni

  • apolipoprotein binding Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB
  • scaffold protein binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021353.

Structurei

Secondary structure

1
1905
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi364 – 3696Combined sources
Beta strandi399 – 4024Combined sources
Beta strandi406 – 4094Combined sources
Beta strandi424 – 4263Combined sources
Beta strandi433 – 4386Combined sources
Beta strandi441 – 4455Combined sources
Beta strandi450 – 4534Combined sources
Beta strandi460 – 4645Combined sources
Beta strandi470 – 4767Combined sources
Turni477 – 4804Combined sources
Beta strandi481 – 4866Combined sources
Turni487 – 4904Combined sources
Beta strandi491 – 4966Combined sources
Beta strandi503 – 5064Combined sources
Beta strandi515 – 5195Combined sources
Turni520 – 5234Combined sources
Beta strandi524 – 5296Combined sources
Turni530 – 5334Combined sources
Beta strandi534 – 5396Combined sources
Beta strandi546 – 5494Combined sources
Beta strandi556 – 5627Combined sources
Turni563 – 5664Combined sources
Beta strandi567 – 5726Combined sources
Beta strandi574 – 5763Combined sources
Beta strandi578 – 5836Combined sources
Beta strandi590 – 5923Combined sources
Beta strandi600 – 6067Combined sources
Turni607 – 6104Combined sources
Beta strandi611 – 6166Combined sources
Turni617 – 6204Combined sources
Beta strandi621 – 6266Combined sources
Beta strandi633 – 6364Combined sources
Beta strandi641 – 6499Combined sources
Beta strandi652 – 6576Combined sources
Turni658 – 6614Combined sources
Beta strandi662 – 6676Combined sources
Turni668 – 6703Combined sources
Beta strandi675 – 6784Combined sources
Beta strandi687 – 6904Combined sources
Helixi692 – 6943Combined sources
Turni701 – 7044Combined sources
Helixi705 – 7084Combined sources
Beta strandi710 – 7145Combined sources
Beta strandi717 – 7193Combined sources
Beta strandi721 – 7233Combined sources
Beta strandi728 – 7314Combined sources
Turni732 – 7343Combined sources
Beta strandi735 – 7373Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V64X-ray2.85C/D396-737[»]
3V65X-ray3.30B/D353-737[»]
ProteinModelPortaliQ9QYP1.
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; 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

eggNOGiKOG1215. Eukaryota.
ENOG410XPR2. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000047507.
HOVERGENiHBG049163.
InParanoidiQ9QYP1.
OMAiGSQLLWA.
OrthoDBiEOG75XGK3.
PhylomeDBiQ9QYP1.
TreeFamiTF315253.

Family and domain databases

Gene3Di2.120.10.30. 4 hits.
4.10.400.10. 7 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR030799. LRP4.
[Graphical view]
PANTHERiPTHR10529:SF249. PTHR10529:SF249. 4 hits.
PfamiPF12662. cEGF. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 7 hits.
SM00179. EGF_CA. 2 hits.
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.

Q9QYP1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRWWGALLL GALLCAHGTA SNLECACGRS 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 GLCVNAGWRC
260 270 280 290 300
DGDADCDDQS DERNCTTSMC TAEQFRCRSG RCVRLSWRCD GEDDCADNSD
310 320 330 340 350
EENCENTGSP QCASDQFLCW NGRCIGQRKL CNGVNDCGDN SDESPQQNCR
360 370 380 390 400
PRTGEENCNV NNGGCAQKCQ MIRGAVQCTC HTGYRLTEDG RTCQDVNECA
410 420 430 440 450
EEGYCSQGCT NSEGAFQCWC 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
KWDGTGQKVV VDTSLESPAG LAIDWVTNKL YWTDAGTDRI EVANTDGSMR
860 870 880 890 900
TVLIWENLDR PRDIVVEPMG GYMYWTDWGA SPKIERAGMD ASNRQVIISS
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
PVTTPCAVEN GGCSHLCLRS PSPSGFSCTC PTGINLLLDG 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 LKGDGKTCDP
1360 1370 1380 1390 1400
SPETYLLFSS RGSIRRISLD TDDHTDVHVP VPGLNNVISL DYDSVDGKVY
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 NADLGWPNGL TLDYDTRRIY WVDAHLDRIE SADLNGKLRQ
1560 1570 1580 1590 1600
VLVSHVSHPF ALTQQDRWIY WTDWQTKSIQ RVDKYSGRNK ETVLANVEGL
1610 1620 1630 1640 1650
MDIIVVSPQR QTGTNACGVN NGGCSHLCFA RASDFVCACP DEPDSHPCSL
1660 1670 1680 1690 1700
VPGLMPPAPR ATSLNEKSPV LPNTLPTTLH SSTTRTRTSP EGAEGRCSER
1710 1720 1730 1740 1750
DAQLGLCAHS NEAVPAAPGE GLHVSYAVGG LLSVLLILLV TAALMLYRHR
1760 1770 1780 1790 1800
KSKFTDPGMG NLTYSNPSYR TSTQEVKIEA APKPAMYNQL CYKKEGGPDH
1810 1820 1830 1840 1850
SYTKEKIKIV EGIHLLAGHD AEWGDLKQLR SSRGGLLRDH VCMKTDTVSI
1860 1870 1880 1890 1900
QASSGSLDDT ETEQLLQEEQ SECSSVHTAT TPERRGSLPD TGWKHERKLS

SESQV
Length:1,905
Mass (Da):211,880
Last modified:May 10, 2004 - v2
Checksum:i9562A5729D69E29A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03025549 Genomic DNA. No translation available.
AABR03027097 Genomic DNA. No translation available.
AABR03027512 Genomic DNA. No translation available.
AABR03029369 Genomic DNA. No translation available.
AB011533 mRNA. Translation: BAA88688.1.
UniGeneiRn.21381.

Genome annotation databases

EnsembliENSRNOT00000021353; ENSRNOP00000021353; ENSRNOG00000015285.
UCSCiRGD:619731. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03025549 Genomic DNA. No translation available.
AABR03027097 Genomic DNA. No translation available.
AABR03027512 Genomic DNA. No translation available.
AABR03029369 Genomic DNA. No translation available.
AB011533 mRNA. Translation: BAA88688.1.
UniGeneiRn.21381.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V64X-ray2.85C/D396-737[»]
3V65X-ray3.30B/D353-737[»]
ProteinModelPortaliQ9QYP1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021353.

PTM databases

iPTMnetiQ9QYP1.
PhosphoSiteiQ9QYP1.

Proteomic databases

PaxDbiQ9QYP1.
PRIDEiQ9QYP1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021353; ENSRNOP00000021353; ENSRNOG00000015285.
UCSCiRGD:619731. rat.

Organism-specific databases

RGDi619731. Lrp4.

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XPR2. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000047507.
HOVERGENiHBG049163.
InParanoidiQ9QYP1.
OMAiGSQLLWA.
OrthoDBiEOG75XGK3.
PhylomeDBiQ9QYP1.
TreeFamiTF315253.

Miscellaneous databases

PROiQ9QYP1.

Gene expression databases

ExpressionAtlasiQ9QYP1. baseline and differential.
GenevisibleiQ9QYP1. RN.

Family and domain databases

Gene3Di2.120.10.30. 4 hits.
4.10.400.10. 7 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR030799. LRP4.
[Graphical view]
PANTHERiPTHR10529:SF249. PTHR10529:SF249. 4 hits.
PfamiPF12662. cEGF. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 7 hits.
SM00179. EGF_CA. 2 hits.
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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  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 OF 608-1905, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. Cited for: INTERACTION WITH MUSK.

Entry informationi

Entry nameiLRP4_RAT
AccessioniPrimary (citable) accession number: Q9QYP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 10, 2004
Last modified: May 11, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.