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Reviewed, UniProtKB/Swiss-Prot Q9D1T0 (LIGO1_MOUSE)

Last modified October 13, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1
Alternative name(s):
    Leucine-rich repeat neuronal protein 6A
    Leucine-rich repeat neuronal protein 1
Gene names
Name: Lingo1
Synonyms: Lern1, Lrrn6a
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Functional component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. Is also an important negative regulator of oligodentrocyte differentiation and axonal myelination By similarity.

Subunit structure

Homotetramer. Forms ternary complex with RTN4R/NGFR and RTN4R/TNFRSF19 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Ref.4

Tissue specificity

Highly specific expression in the central nervous system. Predominant expression in neocortex, amygdala, hippocampus, thalamus and entorhinal cortex, with lower levels in cerebellum and basal nuclei. Ref.4 Ref.3

Developmental stage

Expressed broadly at high levels in the whole embryo and becomes progressively restricted to the central nervous system by E14.5. Extensively expressed across the central nervous system through late embryogenesis and during postnatal development, with a peak of expression around the first week after birth. Ref.4 Ref.3

Induction

Up-regulated in brain from MPTP-intoxicated mice, a model for Parkinson disease. Ref.5

Domain

The intracellular domain of LINGO1 interact with MYT1L.

Post-translational modification

N-glycosylated. Contains predominantly high-mannose glycans By similarity.

Disruption phenotype

In mice lacking Lingo1 and MPTP-intoxicated, a model for Parkinson disease, the dopaminergic neurons survival is increased and behavioral abnormalities reduced. Ref.5

Sequence similarities

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 13 LRR (leucine-rich) repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AppP120231EBI-2012981,EBI-78814

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 614579Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1
PRO_0000328643

Regions

Topological domain36 – 555520Extracellular Potential
Transmembrane556 – 57621 Potential
Topological domain577 – 61438Cytoplasmic Potential
Repeat64 – 8724LRR 1
Repeat88 – 11124LRR 2
Repeat112 – 13524LRR 3
Repeat137 – 15923LRR 4
Repeat160 – 18324LRR 5
Repeat184 – 20724LRR 6
Repeat209 – 23123LRR 7
Repeat256 – 27924LRR 8
Repeat280 – 30324LRR 9
Repeat305 – 32723LRR 10
Repeat328 – 35124LRR 11
Repeat353 – 37725LRR 12
Domain405 – 507103Ig-like C2-type
Repeat453 – 47826LRR 13

Amino acid modifications

Modified residue5961Phosphoserine Ref.6
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation2681N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation4861N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 42 By similarity
Disulfide bond40 ↔ 51 By similarity
Disulfide bond367 ↔ 390 By similarity
Disulfide bond369 ↔ 415 By similarity
Disulfide bond440 ↔ 491 By similarity

Experimental info

Sequence conflict4911C → G in AAQ97219. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9D1T0-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 41CFF40C21335681

FASTA61469,101
        10         20         30         40         50         60 
MLAGGMRSMP SPLLACWQPI LLLVLGSVLS GSATGCPPRC ECSAQDRAVL CHRKRFVAVP 

        70         80         90        100        110        120 
EGIPTETRLL DLGKNRIKTL NQDEFASFPH LEELELNENI VSAVEPGAFN NLFNLRTLGL 

       130        140        150        160        170        180 
RSNRLKLIPL GVFTGLSNLT KLDISENKIV ILLDYMFQDL YNLKSLEVGD NDLVYISHRA 

       190        200        210        220        230        240 
FSGLNSLEQL TLEKCNLTSI PTEALSHLHG LIVLRLRHLN INAIRDYSFK RLYRLKVLEI 

       250        260        270        280        290        300 
SHWPYLDTMT PNCLYGLNLT SLSITHCNLT AVPYLAVRHL VYLRFLNLSY NPIGTIEGSM 

       310        320        330        340        350        360 
LHELLRLQEI QLVGGQLAVV EPYAFRGLNY LRVLNVSGNQ LTTLEESAFH SVGNLETLIL 

       370        380        390        400        410        420 
DSNPLACDCR LLWVFRRRWR LNFNRQQPTC ATPEFVQGKE FKDFPDVLLP NYFTCRRAHI 

       430        440        450        460        470        480 
RDRKAQQVFV DEGHTVQFVC RADGDPPPAI LWLSPRKHLV SAKSNGRLTV FPDGTLEVRY 

       490        500        510        520        530        540 
AQVQDNGTYL CIAANAGGND SMPAHLHVRS YSPDWPHQPN KTFAFISNQP GEGEANSTRA 

       550        560        570        580        590        600 
TVPFPFDIKT LIIATTMGFI SFLGVVLFCL VLLFLWSRGK GNTKHNIEIE YVPRKSDAGI 

       610 
SSADAPRKFN MKMI 

« Hide

References

« Hide 'large scale' references
[1]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[3]"LRRN6A/LERN1 (leucine-rich repeat neuronal protein 1), a novel gene with enriched expression in limbic system and neocortex."
Carim-Todd L., Escarceller M., Estivill X., Sumoy L.
Eur. J. Neurosci. 18:3167-3182(2003) [PubMed: 14686891] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 411-614, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[4]"Developmental analysis of Lingo-1/Lern1 protein expression in the mouse brain: Interaction of its intracellular domain with Myt1l."
Llorens F., Gil V., Iraola S., Carim-Todd L., Marti E., Estivill X., Soriano E., Del Rio J.A., Sumoy L.
Dev. Neurobiol. 68:521-541(2008) [PubMed: 18186492] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH NGRF; RTN4R AND MYT1L.
[5]"Inhibition of the leucine-rich repeat protein LINGO-1 enhances survival, structure, and function of dopaminergic neurons in Parkinson's disease models."
Inoue H., Lin L., Lee X., Shao Z., Mendes S., Snodgrass-Belt P., Sweigard H., Engber T., Pepinsky B., Yang L., Beal M.F., Mi S., Isacson O.
Proc. Natl. Acad. Sci. U.S.A. 104:14430-14435(2007) [PubMed: 17726113] [Abstract]
Cited for: INDUCTION, DISRUPTION PHENOTYPE.
[6]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, MASS SPECTROMETRY.
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

AK027262 mRNA. Translation: BAB32403.1.
AK163538 mRNA. Translation: BAE37388.1.
BC052384 mRNA. Translation: AAH52384.2.
BC065696 mRNA. Translation: AAH65696.1.
AY324324 mRNA. Translation: AAQ97219.1.
IPIIPI00134200.
RefSeqNP_851419.1.
UniGeneMm.246605

3D structure databases

HSSPHSSP built from PDB template 1OZN based on UniProtKB Q9BZR6.
SMRQ9D1T0. Positions 36-508.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9D1T0. 1 interaction.
STRINGQ9D1T0.

PTM databases

PhosphoSiteQ9D1T0.

Proteomic databases

PRIDEQ9D1T0.

Genome annotation databases

EnsemblENSMUST00000053568; ENSMUSP00000059050; ENSMUSG00000049556; Mus musculus. [Genome view]
ENSMUST00000114247; ENSMUSP00000109885; ENSMUSG00000049556; Mus musculus. [Genome view]
ENSMUST00000114256; ENSMUSP00000109894; ENSMUSG00000049556; Mus musculus. [Genome view]
GeneID235402.
KEGGmmu:235402.
UCSCuc009pth.1. mouse.

Organism-specific databases

CTD235402.
MGIMGI:1915522. Lingo1.

Phylogenomic databases

HOGENOMQ9D1T0.
HOVERGENQ9D1T0.

Gene expression databases

ArrayExpressQ9D1T0.
BgeeQ9D1T0.
GenevestigatorQ9D1T0.

Family and domain databases

InterProIPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR001611. Leu-rich_rpt.
IPR000372. Leu-rich_rpt_Cys-rich-dom_N.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000483. LRR_C.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PfamPF07679. I-set. 1 hit.
PF00560. LRR_1. 7 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTSM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 1 hit.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio382644.
SOURCESearch...

Entry information

Entry nameLIGO1_MOUSE
AccessionPrimary (citable) accession number: Q9D1T0
Secondary accession number(s): Q3TQJ4, Q6VVF9, Q7TT38
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 1, 2001
Last modified: October 13, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents