ID LIGO1_MOUSE Reviewed; 614 AA. AC Q9D1T0; Q3TQJ4; Q6VVF9; Q7TT38; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 10-AUG-2010, entry version 84. DE RecName: Full=Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1; DE AltName: Full=Leucine-rich repeat neuronal protein 6A; DE AltName: Full=Leucine-rich repeat neuronal protein 1; DE Flags: Precursor; GN Name=Lingo1; Synonyms=Lern1, Lrrn6a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 411-614, DEVELOPMENTAL STAGE, AND TISSUE RP SPECIFICITY. RX PubMed=14686891; DOI=10.1111/j.1460-9568.2003.03003.x; RA Carim-Todd L., Escarceller M., Estivill X., Sumoy L.; RT "LRRN6A/LERN1 (leucine-rich repeat neuronal protein 1), a novel gene RT with enriched expression in limbic system and neocortex."; RL Eur. J. Neurosci. 18:3167-3182(2003). RN [4] RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND RP INTERACTION WITH NGRF; RTN4R AND MYT1L. RX PubMed=18186492; DOI=10.1002/dneu.20607; RA Llorens F., Gil V., Iraola S., Carim-Todd L., Marti E., Estivill X., RA Soriano E., Del Rio J.A., Sumoy L.; RT "Developmental analysis of Lingo-1/Lern1 protein expression in the RT mouse brain: Interaction of its intracellular domain with Myt1l."; RL Dev. Neurobiol. 68:521-541(2008). RN [5] RP INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=17726113; DOI=10.1073/pnas.0700901104; RA Inoue H., Lin L., Lee X., Shao Z., Mendes S., Snodgrass-Belt P., RA Sweigard H., Engber T., Pepinsky B., Yang L., Beal M.F., Mi S., RA Isacson O.; RT "Inhibition of the leucine-rich repeat protein LINGO-1 enhances RT survival, structure, and function of dopaminergic neurons in RT Parkinson's disease models."; RL Proc. Natl. Acad. Sci. U.S.A. 104:14430-14435(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, AND MASS RP SPECTROMETRY. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., RA Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in RT naive and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). CC -!- FUNCTION: Functional component of the Nogo receptor signaling CC complex (RTN4R/NGFR) in RhoA activation responsible for some CC inhibition of axonal regeneration by myelin-associated factors. Is CC also an important negative regulator of oligodentrocyte CC differentiation and axonal myelination (By similarity). CC -!- SUBUNIT: Homotetramer. Forms ternary complex with RTN4R/NGFR and CC RTN4R/TNFRSF19 (By similarity). CC -!- INTERACTION: CC P12023:App; NbExp=1; IntAct=EBI-2012981, EBI-78814; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. CC -!- TISSUE SPECIFICITY: Highly specific expression in the central CC nervous system. Predominant expression in neocortex, amygdala, CC hippocampus, thalamus and entorhinal cortex, with lower levels in CC cerebellum and basal nuclei. CC -!- DEVELOPMENTAL STAGE: Expressed broadly at high levels in the whole CC embryo and becomes progressively restricted to the central nervous CC system by E14.5. Extensively expressed across the central nervous CC system through late embryogenesis and during postnatal CC development, with a peak of expression around the first week after CC birth. CC -!- INDUCTION: Up-regulated in brain from MPTP-intoxicated mice, a CC model for Parkinson disease. CC -!- DOMAIN: The intracellular domain of LINGO1 interact with MYT1L. CC -!- PTM: N-glycosylated. Contains predominantly high-mannose glycans CC (By similarity). CC -!- DISRUPTION PHENOTYPE: In mice lacking Lingo1 and MPTP-intoxicated, CC a model for Parkinson disease, the dopaminergic neurons survival CC is increased and behavioral abnormalities reduced. CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like) CC domain. CC -!- SIMILARITY: Contains 13 LRR (leucine-rich) repeats. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK027262; BAB32403.1; -; mRNA. DR EMBL; AK163538; BAE37388.1; -; mRNA. DR EMBL; BC052384; AAH52384.2; -; mRNA. DR EMBL; BC065696; AAH65696.1; -; mRNA. DR EMBL; AY324324; AAQ97219.1; -; mRNA. DR IPI; IPI00134200; -. DR RefSeq; NP_851419.1; -. DR UniGene; Mm.246605; -. DR HSSP; P21809; 2FT3. DR ProteinModelPortal; Q9D1T0; -. DR SMR; Q9D1T0; 36-508. DR IntAct; Q9D1T0; 2. DR STRING; Q9D1T0; -. DR PhosphoSite; Q9D1T0; -. DR PRIDE; Q9D1T0; -. DR Ensembl; ENSMUST00000053568; ENSMUSP00000059050; ENSMUSG00000049556; Mus musculus. DR Ensembl; ENSMUST00000114247; ENSMUSP00000109885; ENSMUSG00000049556; Mus musculus. DR Ensembl; ENSMUST00000114256; ENSMUSP00000109894; ENSMUSG00000049556; Mus musculus. DR GeneID; 235402; -. DR KEGG; mmu:235402; -. DR UCSC; uc009pth.1; mouse. DR CTD; 235402; -. DR MGI; MGI:1915522; Lingo1. DR eggNOG; maNOG11092; -. DR HOVERGEN; HBG057546; -. DR InParanoid; Q9D1T0; -. DR OrthoDB; EOG9JWXZR; -. DR PhylomeDB; Q9D1T0; -. DR NextBio; 382644; -. DR ArrayExpress; Q9D1T0; -. DR Bgee; Q9D1T0; -. DR Genevestigator; Q9D1T0; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:MGI. DR GO; GO:0021954; P:central nervous system neuron development; IDA:MGI. DR GO; GO:0048715; P:negative regulation of oligodendrocyte diff...; IMP:MGI. DR GO; GO:0031175; P:neuron projection development; IDA:MGI. DR GO; GO:0043491; P:protein kinase B signaling cascade; IDA:MGI. DR InterPro; IPR000483; Cys-rich_flank_reg_C. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR000372; LRR-contain_N. DR Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1. DR Pfam; PF07679; I-set; 1. DR Pfam; PF00560; LRR_1; 3. DR SMART; SM00408; IGc2; 1. DR SMART; SM00369; LRR_TYP; 1. DR SMART; SM00082; LRRCT; 1. DR SMART; SM00013; LRRNT; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS51450; LRR; 10. PE 1: Evidence at protein level; KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain; KW Leucine-rich repeat; Membrane; Phosphoprotein; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 35 Potential. FT CHAIN 36 614 Leucine-rich repeat and immunoglobulin- FT like domain-containing nogo receptor- FT interacting protein 1. FT /FTId=PRO_0000328643. FT TOPO_DOM 36 555 Extracellular (Potential). FT TRANSMEM 556 576 Helical; (Potential). FT TOPO_DOM 577 614 Cytoplasmic (Potential). FT REPEAT 64 87 LRR 1. FT REPEAT 88 111 LRR 2. FT REPEAT 112 135 LRR 3. FT REPEAT 137 159 LRR 4. FT REPEAT 160 183 LRR 5. FT REPEAT 184 207 LRR 6. FT REPEAT 209 231 LRR 7. FT REPEAT 256 279 LRR 8. FT REPEAT 280 303 LRR 9. FT REPEAT 305 327 LRR 10. FT REPEAT 328 351 LRR 11. FT REPEAT 353 377 LRR 12. FT DOMAIN 405 507 Ig-like C2-type. FT REPEAT 453 478 LRR 13. FT MOD_RES 596 596 Phosphoserine. FT CARBOHYD 138 138 N-linked (GlcNAc...) (Potential). FT CARBOHYD 196 196 N-linked (GlcNAc...) (Potential). FT CARBOHYD 258 258 N-linked (GlcNAc...) (Potential). FT CARBOHYD 268 268 N-linked (GlcNAc...) (Potential). FT CARBOHYD 287 287 N-linked (GlcNAc...) (Potential). FT CARBOHYD 335 335 N-linked (GlcNAc...) (Potential). FT CARBOHYD 486 486 N-linked (GlcNAc...) (Potential). FT CARBOHYD 536 536 N-linked (GlcNAc...) (Potential). FT DISULFID 36 42 By similarity. FT DISULFID 40 51 By similarity. FT DISULFID 367 390 By similarity. FT DISULFID 369 415 By similarity. FT DISULFID 440 491 By similarity. FT CONFLICT 491 491 C -> G (in Ref. 3; AAQ97219). SQ SEQUENCE 614 AA; 69101 MW; 41CFF40C21335681 CRC64; MLAGGMRSMP SPLLACWQPI LLLVLGSVLS GSATGCPPRC ECSAQDRAVL CHRKRFVAVP EGIPTETRLL DLGKNRIKTL NQDEFASFPH LEELELNENI VSAVEPGAFN NLFNLRTLGL RSNRLKLIPL GVFTGLSNLT KLDISENKIV ILLDYMFQDL YNLKSLEVGD NDLVYISHRA FSGLNSLEQL TLEKCNLTSI PTEALSHLHG LIVLRLRHLN INAIRDYSFK RLYRLKVLEI SHWPYLDTMT PNCLYGLNLT SLSITHCNLT AVPYLAVRHL VYLRFLNLSY NPIGTIEGSM LHELLRLQEI QLVGGQLAVV EPYAFRGLNY LRVLNVSGNQ LTTLEESAFH SVGNLETLIL DSNPLACDCR LLWVFRRRWR LNFNRQQPTC ATPEFVQGKE FKDFPDVLLP NYFTCRRAHI RDRKAQQVFV DEGHTVQFVC RADGDPPPAI LWLSPRKHLV SAKSNGRLTV FPDGTLEVRY AQVQDNGTYL CIAANAGGND SMPAHLHVRS YSPDWPHQPN KTFAFISNQP GEGEANSTRA TVPFPFDIKT LIIATTMGFI SFLGVVLFCL VLLFLWSRGK GNTKHNIEIE YVPRKSDAGI SSADAPRKFN MKMI //