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Protein

Leucine-rich repeat-containing protein 4

Gene

Lrrc4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Synaptic adhesion protein. Regulates the formation of exitatory synapses through the recruitment of pre-and-postsynaptic proteins. Organize the lamina/pathway-specific differentiation of dendrites. Plays a important role for auditory synaptic responses. Involved in the suppression of glioma.3 Publications

GO - Biological processi

  • postsynaptic density protein 95 clustering Source: MGI
  • regulation of synapse organization Source: MGI
  • synapse organization Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat-containing protein 4
Alternative name(s):
Brain tumor-associated protein MBAG1
Netrin-G2 ligand
Short name:
NGL-2
Gene namesi
Name:Lrrc4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:2182081. Lrrc4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini41 – 526486ExtracellularSequence analysisAdd
BLAST
Transmembranei527 – 54721HelicalSequence analysisAdd
BLAST
Topological domaini548 – 652105CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • dendritic spine Source: MGI
  • excitatory synapse Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • neuron spine Source: MGI
  • postsynaptic membrane Source: MGI
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

Mutant mice dysplay impaired startle response to acoustic stimulus.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4040Sequence analysisAdd
BLAST
Chaini41 – 652612Leucine-rich repeat-containing protein 4PRO_0000014834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 ↔ 51PROSITE-ProRule annotation
Disulfide bondi49 ↔ 60PROSITE-ProRule annotation
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence analysis
Disulfide bondi303 ↔ 328PROSITE-ProRule annotation
Disulfide bondi305 ↔ 349PROSITE-ProRule annotation
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence analysis
Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence analysis
Disulfide bondi373 ↔ 423PROSITE-ProRule annotation
Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence analysis
Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence analysis
Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence analysis
Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence analysis
Glycosylationi449 – 4491N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ99PH1.
PaxDbiQ99PH1.
PRIDEiQ99PH1.

PTM databases

PhosphoSiteiQ99PH1.

Expressioni

Tissue specificityi

Specifically expressed in brain. In the hippocampus, parietal cortex and piriform cortex expressed in proximal segments of CA1 pyramidal neurons.2 Publications

Gene expression databases

BgeeiQ99PH1.
CleanExiMM_LRRC4.
ExpressionAtlasiQ99PH1. baseline and differential.
GenevisibleiQ99PH1. MM.

Interactioni

Subunit structurei

Interacts (via LRR repeats) with NTNG2. Interacts with DLG4. Forms a complex with DLG4 and with NMDA receptors.2 Publications

Protein-protein interaction databases

DIPiDIP-46449N.
STRINGi10090.ENSMUSP00000062158.

Structurei

3D structure databases

ProteinModelPortaliQ99PH1.
SMRiQ99PH1. Positions 43-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 7434LRRNTAdd
BLAST
Repeati75 – 9622LRR 1Add
BLAST
Repeati99 – 12022LRR 2Add
BLAST
Repeati123 – 14422LRR 3Add
BLAST
Repeati147 – 16822LRR 4Add
BLAST
Repeati171 – 19323LRR 5Add
BLAST
Repeati196 – 21722LRR 6Add
BLAST
Repeati218 – 23922LRR 7Add
BLAST
Repeati242 – 26322LRR 8Add
BLAST
Repeati266 – 28722LRR 9Add
BLAST
Domaini299 – 35153LRRCTAdd
BLAST
Domaini352 – 44190Ig-likeAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi454 – 52572Thr-richAdd
BLAST

Domaini

The last 4 C-terminal residues bind to the first 2 PDZ domains of DLG4.

Sequence similaritiesi

Contains 9 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118831.
HOGENOMiHOG000252924.
HOVERGENiHBG052359.
InParanoidiQ99PH1.
KOiK16351.
OMAiNISEDRM.
OrthoDBiEOG769ZHZ.
PhylomeDBiQ99PH1.
TreeFamiTF324303.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR026882. Lrrc4.
IPR000372. LRRNT.
[Graphical view]
PANTHERiPTHR24369:SF9. PTHR24369:SF9. 2 hits.
PfamiPF07679. I-set. 1 hit.
PF13855. LRR_8. 3 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 7 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q99PH1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLWQVTVH HTWNAVLLPV VYLTAQVWIL CAAIAAAASA GPQNCPSVCS
60 70 80 90 100
CSNQFSKVVC TRRGLSEVPQ GIPSNTRYLN LMENNIQMIQ ADTFRHLHHL
110 120 130 140 150
EVLQLGRNSI RQIEVGAFNG LASLNTLELF DNWLTVIPSG AFEYLSKLRE
160 170 180 190 200
LWLRNNPIES IPSYAFNRVP SLMRLDLGEL KKLEYISEGA FEGLFNLKYL
210 220 230 240 250
NLGMCNIKDM PNLTPLVGLE ELEMSGNHFP EIRPGSFHGL SSLKKLWVMN
260 270 280 290 300
SQVSLIERNA FDGLASLVEL NLAHNNLSSL PHDLFTPLRY LVELHLHHNP
310 320 330 340 350
WNCDCDILWL AWWLREYIPT NSTCCGRCHA PMHMRGRYLV EVDQAAFQCS
360 370 380 390 400
APFIMDAPRD LNISEDRMAE LKCRTPPMSS VKWLLPNGTV LSHASRHPRI
410 420 430 440 450
SVLNDGTLNF SRVLLIDTGV YTCMVTNVAG NSNASAYLNV SSAELNTPNF
460 470 480 490 500
SFFTTVTVET TEISPEDITR KYKPVPTTST GYQPAYTTST TVLIQTTRVP
510 520 530 540 550
KQVPVPSTDT TDKMQTSLDE VMKTTKIIIG CFVAVTLLAA AMLIVFYKLR
560 570 580 590 600
KRHQQRSTVT AARTVEIIQV DEDIPAAAPA AATAAPSGVS GEGAVVLPTI
610 620 630 640 650
HDHINYNTYK PAHGAHWTEN SLGNSLHPTV TTISEPYIIQ THTKDKVQET

QI
Length:652
Mass (Da):72,619
Last modified:October 1, 2002 - v2
Checksum:i9D2807A1AEE30062
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2565QVSLI → H in AAL67671 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300458 mRNA. Translation: AAL67671.1.
DQ177325 mRNA. Translation: AAG60620.2.
BC117834 mRNA. Translation: AAI17835.1.
CCDSiCCDS39448.1.
RefSeqiNP_619623.2. NM_138682.2.
UniGeneiMm.443660.

Genome annotation databases

EnsembliENSMUST00000062304; ENSMUSP00000062158; ENSMUSG00000049939.
GeneIDi192198.
KEGGimmu:192198.
UCSCiuc009bcu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300458 mRNA. Translation: AAL67671.1.
DQ177325 mRNA. Translation: AAG60620.2.
BC117834 mRNA. Translation: AAI17835.1.
CCDSiCCDS39448.1.
RefSeqiNP_619623.2. NM_138682.2.
UniGeneiMm.443660.

3D structure databases

ProteinModelPortaliQ99PH1.
SMRiQ99PH1. Positions 43-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46449N.
STRINGi10090.ENSMUSP00000062158.

PTM databases

PhosphoSiteiQ99PH1.

Proteomic databases

MaxQBiQ99PH1.
PaxDbiQ99PH1.
PRIDEiQ99PH1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000062304; ENSMUSP00000062158; ENSMUSG00000049939.
GeneIDi192198.
KEGGimmu:192198.
UCSCiuc009bcu.1. mouse.

Organism-specific databases

CTDi64101.
MGIiMGI:2182081. Lrrc4.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118831.
HOGENOMiHOG000252924.
HOVERGENiHBG052359.
InParanoidiQ99PH1.
KOiK16351.
OMAiNISEDRM.
OrthoDBiEOG769ZHZ.
PhylomeDBiQ99PH1.
TreeFamiTF324303.

Miscellaneous databases

NextBioi371238.
PROiQ99PH1.
SOURCEiSearch...

Gene expression databases

BgeeiQ99PH1.
CleanExiMM_LRRC4.
ExpressionAtlasiQ99PH1. baseline and differential.
GenevisibleiQ99PH1. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR026882. Lrrc4.
IPR000372. LRRNT.
[Graphical view]
PANTHERiPTHR24369:SF9. PTHR24369:SF9. 2 hits.
PfamiPF07679. I-set. 1 hit.
PF13855. LRR_8. 3 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 7 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 7 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and expression analysis of LRRC4, a novel member of leucine-rich repeat (LRR) superfamily."
    Wang J., Qian J., Dong L., Li X., Tan C., Li J., Zhang B., Zhang X., Bin L., Zhou J., Li G.
    Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 29:233-239(2002)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/J.
  2. "Expression and functional characterization of LRRC4, a novel brain-specific member of the LRR superfamily."
    Zhang Q., Wang J., Fan S., Wang L., Cao L., Tang K., Peng C., Li Z., Li W., Gan K., Liu Z., Li X., Shen S., Li G.
    FEBS Lett. 579:3674-3682(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
  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].
  4. "NGL family PSD-95-interacting adhesion molecules regulate excitatory synapse formation."
    Kim S., Burette A., Chung H.S., Kwon S.-K., Woo J., Lee H.W., Kim K., Kim H., Weinberg R.J., Kim E.
    Nat. Neurosci. 9:1294-1301(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NTNG2 AND DLG4.
  5. "Axonal netrin-Gs transneuronally determine lamina-specific subdendritic segments."
    Nishimura-Akiyoshi S., Niimi K., Nakashiba T., Itohara S.
    Proc. Natl. Acad. Sci. U.S.A. 104:14801-14806(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, FUNCTION.
  6. "Netrin-G2 and netrin-G2 ligand are both required for normal auditory responsiveness."
    Zhang W., Rajan I., Savelieva K.V., Wang C.Y., Vogel P., Kelly M., Xu N., Hasson B., Jarman W., Lanthorn T.H.
    Genes Brain Behav. 7:385-392(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NTNG2, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiLRRC4_MOUSE
AccessioniPrimary (citable) accession number: Q99PH1
Secondary accession number(s): Q149E5, Q8VI35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 120 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

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

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.