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Protein

Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1

Gene

Lingo1

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

Functioni

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). Acts in conjunction with RTN4 and RTN4R in regulating neuronal precursor cell motility during cortical development.By similarity1 Publication1 Publication

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: MGI

GO - Biological processi

  • axonogenesis Source: GO_Central
  • central nervous system neuron development Source: MGI
  • negative regulation of oligodendrocyte differentiation Source: MGI
  • neuron projection development Source: MGI
  • protein kinase B signaling Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-193634. Axonal growth inhibition (RHOA activation).

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1
Alternative name(s):
Leucine-rich repeat neuronal protein 1
Leucine-rich repeat neuronal protein 6A
Gene namesi
Name:Lingo1
Synonyms:Lern1, Lrrn6a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1915522. Lingo1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 555520ExtracellularSequence analysisAdd
BLAST
Transmembranei556 – 57621HelicalSequence analysisAdd
BLAST
Topological domaini577 – 61438CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

In mice lacking Lingo1 and MPTP-intoxicated, a model for Parkinson disease, the dopaminergic neurons survival is increased and behavioral abnormalities reduced.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence analysisAdd
BLAST
Chaini36 – 614579Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1PRO_0000328643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 42PROSITE-ProRule annotation
Disulfide bondi40 ↔ 51PROSITE-ProRule annotation
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence analysis
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence analysis
Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence analysis
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence analysis
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence analysis
Disulfide bondi367 ↔ 390PROSITE-ProRule annotation
Disulfide bondi369 ↔ 415PROSITE-ProRule annotation
Disulfide bondi440 ↔ 491PROSITE-ProRule annotation
Glycosylationi486 – 4861N-linked (GlcNAc...)Sequence analysis
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence analysis
Modified residuei596 – 5961PhosphoserineCombined sources

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9D1T0.
PaxDbiQ9D1T0.
PRIDEiQ9D1T0.

PTM databases

iPTMnetiQ9D1T0.
PhosphoSiteiQ9D1T0.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

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.2 Publications

Inductioni

Up-regulated in brain from MPTP-intoxicated mice, a model for Parkinson disease.1 Publication

Gene expression databases

BgeeiQ9D1T0.
ExpressionAtlasiQ9D1T0. baseline and differential.
GenevisibleiQ9D1T0. MM.

Interactioni

Subunit structurei

Homotetramer. Forms a ternary complex with RTN4R/NGFR and RTN4R/TNFRSF19 (By similarity). Interacts with NGRF and MYT1L (PubMed:18186492). Interacts with RTN4R (PubMed:18186492, PubMed:22923615).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AppP120232EBI-2012981,EBI-78814

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: MGI

Protein-protein interaction databases

DIPiDIP-46968N.
IntActiQ9D1T0. 1 interaction.
STRINGi10090.ENSMUSP00000059050.

Structurei

3D structure databases

ProteinModelPortaliQ9D1T0.
SMRiQ9D1T0. Positions 36-510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 6530LRRNTAdd
BLAST
Repeati66 – 8722LRR 1Add
BLAST
Repeati90 – 11122LRR 2Add
BLAST
Repeati114 – 13522LRR 3Add
BLAST
Repeati138 – 15922LRR 4Add
BLAST
Repeati162 – 18322LRR 5Add
BLAST
Repeati186 – 20722LRR 6Add
BLAST
Repeati210 – 23122LRR 7Add
BLAST
Repeati258 – 27922LRR 8Add
BLAST
Repeati282 – 30322LRR 9Add
BLAST
Repeati306 – 32722LRR 10Add
BLAST
Repeati330 – 35122LRR 11Add
BLAST
Domaini363 – 41755LRRCTAdd
BLAST
Domaini405 – 507103Ig-like C2-typeAdd
BLAST

Domaini

The intracellular domain of LINGO1 interacts with MYT1L.1 Publication

Sequence similaritiesi

Contains 11 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.
HOGENOMiHOG000246971.
HOVERGENiHBG057546.
InParanoidiQ9D1T0.
OrthoDBiEOG715Q3P.
PhylomeDBiQ9D1T0.
TreeFamiTF334360.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR007110. 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.
IPR000372. LRRNT.
[Graphical view]
PfamiPF07679. I-set. 1 hit.
PF13855. LRR_8. 3 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 9 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 10 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9D1T0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAGGMRSMP SPLLACWQPI LLLVLGSVLS GSATGCPPRC ECSAQDRAVL
60 70 80 90 100
CHRKRFVAVP EGIPTETRLL DLGKNRIKTL NQDEFASFPH LEELELNENI
110 120 130 140 150
VSAVEPGAFN NLFNLRTLGL RSNRLKLIPL GVFTGLSNLT KLDISENKIV
160 170 180 190 200
ILLDYMFQDL YNLKSLEVGD NDLVYISHRA FSGLNSLEQL TLEKCNLTSI
210 220 230 240 250
PTEALSHLHG LIVLRLRHLN INAIRDYSFK RLYRLKVLEI SHWPYLDTMT
260 270 280 290 300
PNCLYGLNLT SLSITHCNLT AVPYLAVRHL VYLRFLNLSY NPIGTIEGSM
310 320 330 340 350
LHELLRLQEI QLVGGQLAVV EPYAFRGLNY LRVLNVSGNQ LTTLEESAFH
360 370 380 390 400
SVGNLETLIL DSNPLACDCR LLWVFRRRWR LNFNRQQPTC ATPEFVQGKE
410 420 430 440 450
FKDFPDVLLP NYFTCRRAHI RDRKAQQVFV DEGHTVQFVC RADGDPPPAI
460 470 480 490 500
LWLSPRKHLV SAKSNGRLTV FPDGTLEVRY AQVQDNGTYL CIAANAGGND
510 520 530 540 550
SMPAHLHVRS YSPDWPHQPN KTFAFISNQP GEGEANSTRA TVPFPFDIKT
560 570 580 590 600
LIIATTMGFI SFLGVVLFCL VLLFLWSRGK GNTKHNIEIE YVPRKSDAGI
610
SSADAPRKFN MKMI
Length:614
Mass (Da):69,101
Last modified:June 1, 2001 - v1
Checksum:i41CFF40C21335681
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti491 – 4911C → G in AAQ97219 (PubMed:14686891).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23209.1.
RefSeqiNP_001298005.1. NM_001311076.1.
NP_851419.1. NM_181074.4.
XP_006511151.1. XM_006511088.2.
XP_006511152.1. XM_006511089.2.
XP_006511153.1. XM_006511090.2.
UniGeneiMm.246605.

Genome annotation databases

EnsembliENSMUST00000053568; ENSMUSP00000059050; ENSMUSG00000049556.
ENSMUST00000114247; ENSMUSP00000109885; ENSMUSG00000049556.
GeneIDi235402.
KEGGimmu:235402.
UCSCiuc009pti.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23209.1.
RefSeqiNP_001298005.1. NM_001311076.1.
NP_851419.1. NM_181074.4.
XP_006511151.1. XM_006511088.2.
XP_006511152.1. XM_006511089.2.
XP_006511153.1. XM_006511090.2.
UniGeneiMm.246605.

3D structure databases

ProteinModelPortaliQ9D1T0.
SMRiQ9D1T0. Positions 36-510.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46968N.
IntActiQ9D1T0. 1 interaction.
STRINGi10090.ENSMUSP00000059050.

PTM databases

iPTMnetiQ9D1T0.
PhosphoSiteiQ9D1T0.

Proteomic databases

MaxQBiQ9D1T0.
PaxDbiQ9D1T0.
PRIDEiQ9D1T0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053568; ENSMUSP00000059050; ENSMUSG00000049556.
ENSMUST00000114247; ENSMUSP00000109885; ENSMUSG00000049556.
GeneIDi235402.
KEGGimmu:235402.
UCSCiuc009pti.1. mouse.

Organism-specific databases

CTDi84894.
MGIiMGI:1915522. Lingo1.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118831.
HOGENOMiHOG000246971.
HOVERGENiHBG057546.
InParanoidiQ9D1T0.
OrthoDBiEOG715Q3P.
PhylomeDBiQ9D1T0.
TreeFamiTF334360.

Enzyme and pathway databases

ReactomeiR-MMU-193634. Axonal growth inhibition (RHOA activation).

Miscellaneous databases

ChiTaRSiLingo1. mouse.
PROiQ9D1T0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1T0.
ExpressionAtlasiQ9D1T0. baseline and differential.
GenevisibleiQ9D1T0. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR007110. 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.
IPR000372. LRRNT.
[Graphical view]
PfamiPF07679. I-set. 1 hit.
PF13855. LRR_8. 3 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 9 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 10 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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].
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH NGRF; RTN4R AND MYT1L, DOMAIN.
  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] [Europe PMC] [Abstract]
    Cited for: INDUCTION, DISRUPTION PHENOTYPE.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "Nogo-a regulates neural precursor migration in the embryonic mouse cortex."
    Mathis C., Schroeter A., Thallmair M., Schwab M.E.
    Cereb. Cortex 20:2380-2390(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Olfactomedin 1 interacts with the Nogo A receptor complex to regulate axon growth."
    Nakaya N., Sultana A., Lee H.S., Tomarev S.I.
    J. Biol. Chem. 287:37171-37184(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RTN4R.

Entry informationi

Entry nameiLIGO1_MOUSE
AccessioniPrimary (citable) accession number: Q9D1T0
Secondary accession number(s): Q3TQJ4, Q6VVF9, Q7TT38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 132 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

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.