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Protein

Leucine-rich repeat-containing protein 4B

Gene

Lrrc4b

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 excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner (By similarity).By similarity

GO - Molecular functioni

  • protein kinase inhibitor activity Source: GO_Central
  • receptor binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat-containing protein 4B
Alternative name(s):
Netrin-G3 ligand
Short name:
NGL-3
Gene namesi
Name:Lrrc4b
Synonyms:Lrig4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:3027390. Lrrc4b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei575 – 59521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3838Sequence analysisAdd
BLAST
Chaini39 – 709671Leucine-rich repeat-containing protein 4BPRO_0000232387Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence analysis
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence analysis
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence analysis
Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence analysis
Disulfide bondi387 ↔ 438PROSITE-ProRule annotation
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence analysis
Glycosylationi424 – 4241N-linked (GlcNAc...)Sequence analysis
Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence analysis
Glycosylationi446 – 4461N-linked (GlcNAc...)Sequence analysis
Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence analysis
Modified residuei689 – 6891PhosphoserineCombined sources

Post-translational modificationi

N-glycosylated. O-glycosylated; contains sialic acid.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP0C192.
PaxDbiP0C192.
PeptideAtlasiP0C192.
PRIDEiP0C192.

PTM databases

iPTMnetiP0C192.
PhosphoSiteiP0C192.

Expressioni

Gene expression databases

BgeeiP0C192.
CleanExiMM_LRRC4B.
ExpressionAtlasiP0C192. baseline and differential.
GenevisibleiP0C192. MM.

Interactioni

Subunit structurei

Interacts with PTPRF (By similarity). Interacts with DLG4.By similarity1 Publication

GO - Molecular functioni

  • receptor binding Source: BHF-UCL

Protein-protein interaction databases

IntActiP0C192. 1 interaction.
STRINGi10090.ENSMUSP00000053123.

Structurei

Secondary structure

1
709
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi64 – 663Combined sources
Turni67 – 693Combined sources
Beta strandi71 – 733Combined sources
Beta strandi91 – 944Combined sources
Turni105 – 1106Combined sources
Beta strandi116 – 1183Combined sources
Turni129 – 1324Combined sources
Beta strandi140 – 1423Combined sources
Turni153 – 1553Combined sources
Beta strandi164 – 1663Combined sources
Turni177 – 1826Combined sources
Beta strandi187 – 1904Combined sources
Turni202 – 2076Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi235 – 2373Combined sources
Helixi248 – 2514Combined sources
Beta strandi259 – 2613Combined sources
Turni272 – 2776Combined sources
Beta strandi283 – 2853Combined sources
Beta strandi307 – 3093Combined sources
Helixi319 – 3213Combined sources
Helixi322 – 33110Combined sources
Beta strandi341 – 3455Combined sources
Helixi346 – 3483Combined sources
Helixi353 – 3553Combined sources
Helixi358 – 3603Combined sources
Beta strandi367 – 3704Combined sources
Beta strandi379 – 3813Combined sources
Beta strandi383 – 3853Combined sources
Beta strandi388 – 39912Combined sources
Beta strandi423 – 4275Combined sources
Helixi430 – 4323Combined sources
Beta strandi434 – 4418Combined sources
Beta strandi446 – 4538Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZYNX-ray3.20A/B57-365[»]
3ZYOX-ray3.10A57-455[»]
ProteinModelPortaliP0C192.
SMRiP0C192. Positions 57-454.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C192.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 8839LRRNTAdd
BLAST
Repeati89 – 11022LRR 1Add
BLAST
Repeati113 – 13422LRR 2Add
BLAST
Repeati137 – 15822LRR 3Add
BLAST
Repeati161 – 18222LRR 4Add
BLAST
Repeati185 – 20723LRR 5Add
BLAST
Repeati210 – 23122LRR 6Add
BLAST
Repeati232 – 25322LRR 7Add
BLAST
Repeati256 – 27722LRR 8Add
BLAST
Repeati280 – 30122LRR 9Add
BLAST
Domaini313 – 36553LRRCTAdd
BLAST
Domaini366 – 45489Ig-like C2-typeAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 424Poly-Gly
Compositional biasi464 – 48219Gly-richAdd
BLAST
Compositional biasi631 – 6377Poly-Ala

Domaini

The extreme C-terminus binds 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.
InParanoidiP0C192.
KOiK16360.
OMAiTEGMGPG.
OrthoDBiEOG769ZHZ.
PhylomeDBiP0C192.
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.
IPR026883. LRRC4B.
IPR000372. LRRNT.
[Graphical view]
PANTHERiPTHR24369:SF66. PTHR24369:SF66. 4 hits.
PfamiPF07679. I-set. 1 hit.
PF13855. LRR_8. 3 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 8 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.

P0C192-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQAHIRGSP CPLLPPGRMS WPHGALLLLW LFSPPLRAGG GGVAVTSAAG
60 70 80 90 100
GGSPPATSCP AACSCSNQAS RVICTRRELA EVPASIPVNT RYLNLQENSI
110 120 130 140 150
QVIRTDTFKH LRHLEILQLS KNLVRKIEVG AFNGLPSLNT LELFDNRLTT
160 170 180 190 200
VPTQAFEYLS KLRELWLRNN PIESIPSYAF NRVPSLRRLD LGELKRLEYI
210 220 230 240 250
SEAAFEGLVN LRYLNLGMCN LKDIPNLTAL VRLEELELSG NRLDLIRPGS
260 270 280 290 300
FQGLTSLRKL WLMHAQVATI ERNAFDDLKS LEELNLSHNN LMSLPHDLFT
310 320 330 340 350
PLHRLERVHL NHNPWHCNCD VLWLSWWLKE TVPSNTTCCA RCHAPAGLKG
360 370 380 390 400
RYIGELDQSH FTCYAPVIVE PPTDLNVTEG MAAELKCRTG TSMTSVNWLT
410 420 430 440 450
PNGTLMTHGS YRVRISVLHD GTLNFTNVTV QDTGQYTCMV TNSAGNTTAS
460 470 480 490 500
ATLNVSAVDP VAAGGPGGGG PGGGGGAGGA GGYTYFTTVT VETLETQPGE
510 520 530 540 550
EAQQPRGTEK EPPGPTTDGA WGGGRPDAAA PASASTTAPA PRSSRPTEKA
560 570 580 590 600
FTVPITDVTE NALKDLDDVM KTTKIIIGCF VAITFMAAVM LVAFYKLRKQ
610 620 630 640 650
HQLHKHHGPT RTVEIINVED ELPAASAVSV AAAAAVAGGA GVGGDSHLAL
660 670 680 690 700
PALERDHLNH HHYVAAAFKA HYGGNPGGGC GAKGPGLNSI HEPLLFKSGS

KENVQETQI
Length:709
Mass (Da):76,156
Last modified:April 4, 2006 - v1
Checksum:i0C39148F9A8E3586
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti574 – 5741K → R in BAE24378 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC060263 mRNA. Translation: AAH60263.1.
AK140418 mRNA. Translation: BAE24378.1.
CCDSiCCDS21206.1.
RefSeqiNP_937893.1. NM_198250.1.
UniGeneiMm.44173.

Genome annotation databases

EnsembliENSMUST00000058667; ENSMUSP00000053123; ENSMUSG00000047085.
GeneIDi272381.
KEGGimmu:272381.
UCSCiuc009gpj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC060263 mRNA. Translation: AAH60263.1.
AK140418 mRNA. Translation: BAE24378.1.
CCDSiCCDS21206.1.
RefSeqiNP_937893.1. NM_198250.1.
UniGeneiMm.44173.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZYNX-ray3.20A/B57-365[»]
3ZYOX-ray3.10A57-455[»]
ProteinModelPortaliP0C192.
SMRiP0C192. Positions 57-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0C192. 1 interaction.
STRINGi10090.ENSMUSP00000053123.

PTM databases

iPTMnetiP0C192.
PhosphoSiteiP0C192.

Proteomic databases

MaxQBiP0C192.
PaxDbiP0C192.
PeptideAtlasiP0C192.
PRIDEiP0C192.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058667; ENSMUSP00000053123; ENSMUSG00000047085.
GeneIDi272381.
KEGGimmu:272381.
UCSCiuc009gpj.1. mouse.

Organism-specific databases

CTDi94030.
MGIiMGI:3027390. Lrrc4b.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118831.
HOGENOMiHOG000252924.
HOVERGENiHBG052359.
InParanoidiP0C192.
KOiK16360.
OMAiTEGMGPG.
OrthoDBiEOG769ZHZ.
PhylomeDBiP0C192.
TreeFamiTF324303.

Miscellaneous databases

EvolutionaryTraceiP0C192.
PROiP0C192.
SOURCEiSearch...

Gene expression databases

BgeeiP0C192.
CleanExiMM_LRRC4B.
ExpressionAtlasiP0C192. baseline and differential.
GenevisibleiP0C192. 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.
IPR026883. LRRC4B.
IPR000372. LRRNT.
[Graphical view]
PANTHERiPTHR24369:SF66. PTHR24369:SF66. 4 hits.
PfamiPF07679. I-set. 1 hit.
PF13855. LRR_8. 3 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 8 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. "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].
    Strain: C57BL/6J.
    Tissue: Embryonic brain.
  2. "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 63-709.
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  3. "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: INTERACTION WITH DLG4.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart and Lung.

Entry informationi

Entry nameiLRC4B_MOUSE
AccessioniPrimary (citable) accession number: P0C192
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: July 6, 2016
This is version 97 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.