LIGO1_MOUSE
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 03-AUG-2022, entry version 165.
DE RecName: Full=Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1;
DE AltName: Full=Leucine-rich repeat neuronal protein 1;
DE AltName: Full=Leucine-rich repeat neuronal protein 6A;
DE Flags: Precursor;
GN Name=Lingo1; Synonyms=Lern1, Lrrn6a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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/6J; 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 project:
RT 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 with
RT enriched expression in limbic system and neocortex.";
RL Eur. J. Neurosci. 18:3167-3182(2003).
RN [4]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION
RP WITH NGRF; RTN4R AND MYT1L, AND DOMAIN.
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 mouse
RT 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., Isacson O.;
RT "Inhibition of the leucine-rich repeat protein LINGO-1 enhances survival,
RT structure, and function of dopaminergic neurons in Parkinson's disease
RT models.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14430-14435(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION.
RX PubMed=20093372; DOI=10.1093/cercor/bhp307;
RA Mathis C., Schroeter A., Thallmair M., Schwab M.E.;
RT "Nogo-a regulates neural precursor migration in the embryonic mouse
RT cortex.";
RL Cereb. Cortex 20:2380-2390(2010).
RN [8]
RP FUNCTION, AND INTERACTION WITH RTN4R.
RX PubMed=22923615; DOI=10.1074/jbc.m112.389916;
RA Nakaya N., Sultana A., Lee H.S., Tomarev S.I.;
RT "Olfactomedin 1 interacts with the Nogo A receptor complex to regulate axon
RT growth.";
RL J. Biol. Chem. 287:37171-37184(2012).
CC -!- FUNCTION: Functional component of the Nogo receptor signaling complex
CC (RTN4R/NGFR) in RhoA activation responsible for some inhibition of
CC axonal regeneration by myelin-associated factors. Is also an important
CC negative regulator of oligodentrocyte differentiation and axonal
CC myelination (By similarity). Acts in conjunction with RTN4 and RTN4R in
CC regulating neuronal precursor cell motility during cortical
CC development. {ECO:0000250|UniProtKB:Q96FE5,
CC ECO:0000269|PubMed:20093372, ECO:0000305|PubMed:22923615}.
CC -!- SUBUNIT: Homotetramer. Forms a ternary complex with RTN4R/NGFR and
CC RTN4R/TNFRSF19 (By similarity). Interacts with NGRF and MYT1L
CC (PubMed:18186492). Interacts with RTN4R (PubMed:18186492,
CC PubMed:22923615). {ECO:0000250|UniProtKB:Q96FE5,
CC ECO:0000269|PubMed:18186492, ECO:0000269|PubMed:22923615}.
CC -!- INTERACTION:
CC Q9D1T0; P12023: App; NbExp=2; IntAct=EBI-2012981, EBI-78814;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18186492};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:18186492}.
CC -!- TISSUE SPECIFICITY: Highly specific expression in the central nervous
CC system. Predominant expression in neocortex, amygdala, hippocampus,
CC thalamus and entorhinal cortex, with lower levels in cerebellum and
CC basal nuclei. {ECO:0000269|PubMed:14686891,
CC ECO:0000269|PubMed:18186492}.
CC -!- DEVELOPMENTAL STAGE: Expressed broadly at high levels in the whole
CC embryo and becomes progressively restricted to the central nervous
CC system by 14.5 dpc. Extensively expressed across the central nervous
CC system through late embryogenesis and during postnatal development,
CC with a peak of expression around the first week after birth.
CC {ECO:0000269|PubMed:14686891, ECO:0000269|PubMed:18186492}.
CC -!- INDUCTION: Up-regulated in brain from MPTP-intoxicated mice, a model
CC for Parkinson disease. {ECO:0000269|PubMed:17726113}.
CC -!- DOMAIN: The intracellular domain of LINGO1 interacts with MYT1L.
CC {ECO:0000269|PubMed:18186492}.
CC -!- PTM: N-glycosylated. Contains predominantly high-mannose glycans (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: In mice lacking Lingo1 and MPTP-intoxicated, a
CC model for Parkinson disease, the dopaminergic neurons survival is
CC increased and behavioral abnormalities reduced.
CC {ECO:0000269|PubMed:17726113}.
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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 CCDS; CCDS23209.1; -.
DR RefSeq; NP_001298005.1; NM_001311076.1.
DR RefSeq; NP_851419.1; NM_181074.4.
DR RefSeq; XP_006511151.1; XM_006511088.3.
DR RefSeq; XP_006511152.1; XM_006511089.3.
DR RefSeq; XP_006511153.1; XM_006511090.3.
DR RefSeq; XP_017168822.1; XM_017313333.1.
DR RefSeq; XP_017168823.1; XM_017313334.1.
DR RefSeq; XP_017168824.1; XM_017313335.1.
DR RefSeq; XP_017168825.1; XM_017313336.1.
DR AlphaFoldDB; Q9D1T0; -.
DR SMR; Q9D1T0; -.
DR BioGRID; 231654; 1.
DR CORUM; Q9D1T0; -.
DR DIP; DIP-46968N; -.
DR IntAct; Q9D1T0; 2.
DR STRING; 10090.ENSMUSP00000059050; -.
DR GlyConnect; 2465; 2 N-Linked glycans (2 sites).
DR GlyGen; Q9D1T0; 8 sites, 1 N-linked glycan (2 sites).
DR iPTMnet; Q9D1T0; -.
DR PhosphoSitePlus; Q9D1T0; -.
DR MaxQB; Q9D1T0; -.
DR PaxDb; Q9D1T0; -.
DR PRIDE; Q9D1T0; -.
DR ProteomicsDB; 265070; -.
DR ABCD; Q9D1T0; 1 sequenced antibody.
DR Antibodypedia; 2624; 418 antibodies from 35 providers.
DR DNASU; 235402; -.
DR Ensembl; ENSMUST00000053568; ENSMUSP00000059050; ENSMUSG00000049556.
DR Ensembl; ENSMUST00000114247; ENSMUSP00000109885; ENSMUSG00000049556.
DR Ensembl; ENSMUST00000210032; ENSMUSP00000148179; ENSMUSG00000049556.
DR GeneID; 235402; -.
DR KEGG; mmu:235402; -.
DR UCSC; uc009pti.1; mouse.
DR CTD; 84894; -.
DR MGI; MGI:1915522; Lingo1.
DR VEuPathDB; HostDB:ENSMUSG00000049556; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154996; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; Q9D1T0; -.
DR OMA; MVAREAT; -.
DR OrthoDB; 399926at2759; -.
DR PhylomeDB; Q9D1T0; -.
DR TreeFam; TF334360; -.
DR Reactome; R-MMU-193634; Axonal growth inhibition (RHOA activation).
DR BioGRID-ORCS; 235402; 3 hits in 60 CRISPR screens.
DR ChiTaRS; Lingo1; mouse.
DR PRO; PR:Q9D1T0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D1T0; protein.
DR Bgee; ENSMUSG00000049556; Expressed in visual cortex and 213 other tissues.
DR ExpressionAtlas; Q9D1T0; baseline and differential.
DR Genevisible; Q9D1T0; MM.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of 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 differentiation; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13306; LRR_5; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48726; SSF48726; 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; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..614
FT /note="Leucine-rich repeat and immunoglobulin-like domain-
FT containing nogo receptor-interacting protein 1"
FT /id="PRO_0000328643"
FT TOPO_DOM 36..555
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..65
FT /note="LRRNT"
FT REPEAT 66..87
FT /note="LRR 1"
FT REPEAT 90..111
FT /note="LRR 2"
FT REPEAT 114..135
FT /note="LRR 3"
FT REPEAT 138..159
FT /note="LRR 4"
FT REPEAT 162..183
FT /note="LRR 5"
FT REPEAT 186..207
FT /note="LRR 6"
FT REPEAT 210..231
FT /note="LRR 7"
FT REPEAT 258..279
FT /note="LRR 8"
FT REPEAT 282..303
FT /note="LRR 9"
FT REPEAT 306..327
FT /note="LRR 10"
FT REPEAT 330..351
FT /note="LRR 11"
FT DOMAIN 363..417
FT /note="LRRCT"
FT DOMAIN 405..507
FT /note="Ig-like C2-type"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 40..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 367..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 369..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 440..491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 491
FT /note="C -> G (in Ref. 3; AAQ97219)"
FT /evidence="ECO:0000305"
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
