LIGO1_HUMAN
ID LIGO1_HUMAN Reviewed; 620 AA.
AC Q96FE5; D3DW80; Q6NUK3; Q6UXM3; Q6VVG0; Q6VVG1; Q6VVG2; Q8N3K5; Q96K52;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1;
DE AltName: Full=Leucine-rich repeat and immunoglobulin domain-containing 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; ORFNames=UNQ201/PRO227;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP PHE-183.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-620.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH NGFR AND RTN4R.
RX PubMed=14966521; DOI=10.1038/nn1188;
RA Mi S., Lee X., Shao Z., Thill G., Ji B., Relton J., Levesque M.,
RA Allaire N., Perrin S., Sands B., Crowell T., Cate R.L., McCoy J.M.,
RA Pepinsky R.B.;
RT "LINGO-1 is a component of the Nogo-66 receptor/p75 signaling complex.";
RL Nat. Neurosci. 7:221-228(2004).
RN [8]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=15895088; DOI=10.1038/nn1460;
RA Mi S., Miller R.H., Lee X., Scott M.L., Shulag-Morskaya S., Shao Z.,
RA Chang J., Thill G., Levesque M., Zhang M., Hession C., Sah D., Trapp B.,
RA He Z., Jung V., McCoy J.M., Pepinsky R.B.;
RT "LINGO-1 negatively regulates myelination by oligodendrocytes.";
RL Nat. Neurosci. 8:745-751(2005).
RN [9]
RP INTERACTION WITH TNFRSF19, AND FUNCTION.
RX PubMed=15694321; DOI=10.1016/j.neuron.2004.12.040;
RA Park J.B., Yiu G., Kaneko S., Wang J., Chang J., He X.L., Garcia K.C.,
RA He Z.;
RT "A TNF receptor family member, TROY, is a coreceptor with Nogo receptor in
RT mediating the inhibitory activity of myelin inhibitors.";
RL Neuron 45:345-351(2005).
RN [10]
RP TISSUE SPECIFICITY.
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 [11]
RP INTERACTION WITH RTN4R.
RX PubMed=19052207; DOI=10.1523/jneurosci.3828-08.2008;
RA Budel S., Padukkavidana T., Liu B.P., Feng Z., Hu F., Johnson S.,
RA Lauren J., Park J.H., McGee A.W., Liao J., Stillman A., Kim J.E.,
RA Yang B.Z., Sodi S., Gelernter J., Zhao H., Hisama F., Arnsten A.F.,
RA Strittmatter S.M.;
RT "Genetic variants of Nogo-66 receptor with possible association to
RT schizophrenia block myelin inhibition of axon growth.";
RL J. Neurosci. 28:13161-13172(2008).
RN [12]
RP INVOLVEMENT IN MRT64, AND VARIANTS MRT64 CYS-288 AND HIS-290.
RX PubMed=28837161; DOI=10.1038/gim.2017.113;
RA Ansar M., Riazuddin S., Sarwar M.T., Makrythanasis P., Paracha S.A.,
RA Iqbal Z., Khan J., Assir M.Z., Hussain M., Razzaq A., Polla D.L., Taj A.S.,
RA Holmgren A., Batool N., Misceo D., Iwaszkiewicz J., de Brouwer A.P.M.,
RA Guipponi M., Hanquinet S., Zoete V., Santoni F.A., Frengen E., Ahmed J.,
RA Riazuddin S., van Bokhoven H., Antonarakis S.E.;
RT "Biallelic variants in LINGO1 are associated with autosomal recessive
RT intellectual disability, microcephaly, speech and motor delay.";
RL Genet. Med. 20:778-784(2018).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 40-516, FUNCTION, SUBUNIT,
RP INTERACTION WITH NGFR AND RTN4R, DISULFIDE BONDS, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND GLYCOSYLATION AT ASN-144; ASN-202; ASN-264; ASN-274;
RP ASN-293; ASN-341 AND ASN-492.
RX PubMed=17005555; DOI=10.1074/jbc.m607314200;
RA Mosyak L., Wood A., Dwyer B., Buddha M., Johnson M., Aulabaugh A.,
RA Zhong X., Presman E., Benard S., Kelleher K., Wilhelm J., Stahl M.L.,
RA Kriz R., Gao Y., Cao Z., Ling H.P., Pangalos M.N., Walsh F.S., Somers W.S.;
RT "The structure of the Lingo-1 ectodomain, a module implicated in central
RT nervous system repair inhibition.";
RL J. Biol. Chem. 281:36378-36390(2006).
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 (PubMed:14966521,
CC PubMed:15694321). Is also an important negative regulator of
CC oligodentrocyte differentiation and axonal myelination
CC (PubMed:15895088). Acts in conjunction with RTN4 and RTN4R in
CC regulating neuronal precursor cell motility during cortical development
CC (By similarity). {ECO:0000250|UniProtKB:Q9D1T0,
CC ECO:0000269|PubMed:14966521, ECO:0000269|PubMed:15694321,
CC ECO:0000269|PubMed:15895088}.
CC -!- SUBUNIT: Homotetramer (PubMed:17005555). Forms a ternary complex with
CC RTN4R/NGFR and RTN4R/TNFRSF19 (PubMed:14966521, PubMed:15694321,
CC PubMed:17005555). Interacts with NGRF and MYT1L (By similarity).
CC Interacts with RTN4R (PubMed:19052207). {ECO:0000250|UniProtKB:Q9D1T0,
CC ECO:0000269|PubMed:14966521, ECO:0000269|PubMed:15694321,
CC ECO:0000269|PubMed:17005555, ECO:0000269|PubMed:19052207}.
CC -!- INTERACTION:
CC Q96FE5; P05067: APP; NbExp=3; IntAct=EBI-719955, EBI-77613;
CC Q96FE5; P05067-4: APP; NbExp=2; IntAct=EBI-719955, EBI-302641;
CC Q96FE5; P00533: EGFR; NbExp=2; IntAct=EBI-719955, EBI-297353;
CC Q96FE5; P23142-4: FBLN1; NbExp=3; IntAct=EBI-719955, EBI-11956479;
CC Q96FE5; O43559: FRS3; NbExp=3; IntAct=EBI-719955, EBI-725515;
CC Q96FE5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-719955, EBI-618309;
CC Q96FE5; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-719955, EBI-3918847;
CC Q96FE5; Q6L8G9: KRTAP5-6; NbExp=3; IntAct=EBI-719955, EBI-10250562;
CC Q96FE5; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-719955, EBI-3958099;
CC Q96FE5; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-719955, EBI-1044640;
CC Q96FE5; Q8N5G2: MACO1; NbExp=3; IntAct=EBI-719955, EBI-2683507;
CC Q96FE5; P08138: NGFR; NbExp=2; IntAct=EBI-719955, EBI-1387782;
CC Q96FE5; Q9P121-3: NTM; NbExp=3; IntAct=EBI-719955, EBI-12027160;
CC Q96FE5; Q96R06: SPAG5; NbExp=3; IntAct=EBI-719955, EBI-413317;
CC Q96FE5; P14373: TRIM27; NbExp=3; IntAct=EBI-719955, EBI-719493;
CC Q96FE5; Q99M75: Rtn4r; Xeno; NbExp=2; IntAct=EBI-719955, EBI-7370412;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9D1T0};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9D1T0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96FE5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96FE5-2; Sequence=VSP_032749;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the central nervous
CC system. Highest level in the in amygdala, hippocampus, thalamus and
CC cerebral cortex. In the rest of the brain a basal expression seems to
CC be always present. Up-regulated in substantia nigra neurons from
CC Parkinson disease patients. {ECO:0000269|PubMed:14686891,
CC ECO:0000269|PubMed:15895088, ECO:0000269|PubMed:17726113}.
CC -!- DOMAIN: The intracellular domain of LINGO1 interacts with MYT1L.
CC {ECO:0000250|UniProtKB:Q9D1T0}.
CC -!- PTM: N-glycosylated. Contains predominantly high-mannose glycans.
CC {ECO:0000269|PubMed:17005555}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 64
CC (MRT64) [MIM:618103]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRT64
CC patients have moderate to severe intellectual disability, delayed motor
CC development, aggressive behavior, and slurred or absent speech.
CC {ECO:0000269|PubMed:28837161}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AY324320; AAQ97216.1; -; mRNA.
DR EMBL; AY324322; AAQ97217.1; -; mRNA.
DR EMBL; AY324323; AAQ97218.1; -; mRNA.
DR EMBL; AY358284; AAQ88651.1; -; mRNA.
DR EMBL; AK027500; BAB55157.1; -; mRNA.
DR EMBL; AK291363; BAF84052.1; -; mRNA.
DR EMBL; CH471136; EAW99195.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99196.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99197.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99198.1; -; Genomic_DNA.
DR EMBL; BC011057; AAH11057.2; -; mRNA.
DR EMBL; BC068558; AAH68558.1; -; mRNA.
DR EMBL; AL834260; CAD38935.1; -; mRNA.
DR CCDS; CCDS45313.1; -. [Q96FE5-1]
DR CCDS; CCDS73766.1; -. [Q96FE5-2]
DR RefSeq; NP_001288115.1; NM_001301186.1. [Q96FE5-2]
DR RefSeq; NP_001288116.1; NM_001301187.1. [Q96FE5-2]
DR RefSeq; NP_001288118.1; NM_001301189.1. [Q96FE5-2]
DR RefSeq; NP_001288120.1; NM_001301191.1. [Q96FE5-2]
DR RefSeq; NP_001288121.1; NM_001301192.1. [Q96FE5-2]
DR RefSeq; NP_001288123.1; NM_001301194.1. [Q96FE5-2]
DR RefSeq; NP_001288124.1; NM_001301195.1. [Q96FE5-2]
DR RefSeq; NP_001288126.1; NM_001301197.1. [Q96FE5-2]
DR RefSeq; NP_001288127.1; NM_001301198.1. [Q96FE5-2]
DR RefSeq; NP_001288128.1; NM_001301199.1. [Q96FE5-2]
DR RefSeq; NP_001288129.1; NM_001301200.1. [Q96FE5-2]
DR RefSeq; NP_116197.4; NM_032808.6. [Q96FE5-1]
DR RefSeq; XP_011520420.1; XM_011522118.2. [Q96FE5-2]
DR RefSeq; XP_016878171.1; XM_017022682.1. [Q96FE5-2]
DR PDB; 2ID5; X-ray; 2.70 A; A/B/C/D=40-516.
DR PDB; 4OQT; X-ray; 3.23 A; A=40-517.
DR PDBsum; 2ID5; -.
DR PDBsum; 4OQT; -.
DR AlphaFoldDB; Q96FE5; -.
DR SMR; Q96FE5; -.
DR BioGRID; 124334; 50.
DR CORUM; Q96FE5; -.
DR DIP; DIP-60981N; -.
DR IntAct; Q96FE5; 32.
DR MINT; Q96FE5; -.
DR STRING; 9606.ENSP00000347451; -.
DR ChEMBL; CHEMBL3712965; -.
DR GuidetoPHARMACOLOGY; 2882; -.
DR TCDB; 8.A.43.1.15; the neat-domain containing methaemoglobin heme sequestration (n-mhs) family.
DR GlyConnect; 1450; 1 N-Linked glycan (1 site).
DR GlyGen; Q96FE5; 10 sites.
DR iPTMnet; Q96FE5; -.
DR PhosphoSitePlus; Q96FE5; -.
DR BioMuta; LINGO1; -.
DR DMDM; 74760819; -.
DR EPD; Q96FE5; -.
DR jPOST; Q96FE5; -.
DR MassIVE; Q96FE5; -.
DR PaxDb; Q96FE5; -.
DR PeptideAtlas; Q96FE5; -.
DR PRIDE; Q96FE5; -.
DR ProteomicsDB; 76516; -. [Q96FE5-1]
DR ProteomicsDB; 76517; -. [Q96FE5-2]
DR ABCD; Q96FE5; 2 sequenced antibodies.
DR Antibodypedia; 2624; 418 antibodies from 35 providers.
DR DNASU; 84894; -.
DR Ensembl; ENST00000355300.7; ENSP00000347451.6; ENSG00000169783.13. [Q96FE5-1]
DR Ensembl; ENST00000561030.5; ENSP00000453853.1; ENSG00000169783.13. [Q96FE5-2]
DR GeneID; 84894; -.
DR KEGG; hsa:84894; -.
DR MANE-Select; ENST00000355300.7; ENSP00000347451.6; NM_032808.7; NP_116197.4.
DR UCSC; uc002bct.2; human. [Q96FE5-1]
DR CTD; 84894; -.
DR DisGeNET; 84894; -.
DR GeneCards; LINGO1; -.
DR HGNC; HGNC:21205; LINGO1.
DR HPA; ENSG00000169783; Tissue enhanced (brain).
DR MalaCards; LINGO1; -.
DR MIM; 609791; gene.
DR MIM; 618103; phenotype.
DR neXtProt; NX_Q96FE5; -.
DR OpenTargets; ENSG00000169783; -.
DR Orphanet; 862; NON RARE IN EUROPE: Hereditary essential tremor.
DR PharmGKB; PA162394087; -.
DR VEuPathDB; HostDB:ENSG00000169783; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154996; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; Q96FE5; -.
DR OMA; MVAREAT; -.
DR OrthoDB; 399926at2759; -.
DR PhylomeDB; Q96FE5; -.
DR TreeFam; TF334360; -.
DR PathwayCommons; Q96FE5; -.
DR Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
DR SignaLink; Q96FE5; -.
DR SIGNOR; Q96FE5; -.
DR BioGRID-ORCS; 84894; 14 hits in 1063 CRISPR screens.
DR ChiTaRS; LINGO1; human.
DR EvolutionaryTrace; Q96FE5; -.
DR GeneWiki; LINGO1; -.
DR GenomeRNAi; 84894; -.
DR Pharos; Q96FE5; Tbio.
DR PRO; PR:Q96FE5; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q96FE5; protein.
DR Bgee; ENSG00000169783; Expressed in cortical plate and 155 other tissues.
DR ExpressionAtlas; Q96FE5; baseline and differential.
DR Genevisible; Q96FE5; HS.
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; TAS:Reactome.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IBA:GO_Central.
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 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Intellectual disability; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..620
FT /note="Leucine-rich repeat and immunoglobulin-like domain-
FT containing nogo receptor-interacting protein 1"
FT /id="PRO_0000328642"
FT TOPO_DOM 42..561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..71
FT /note="LRRNT"
FT REPEAT 72..93
FT /note="LRR 1"
FT REPEAT 96..117
FT /note="LRR 2"
FT REPEAT 120..141
FT /note="LRR 3"
FT REPEAT 144..165
FT /note="LRR 4"
FT REPEAT 168..189
FT /note="LRR 5"
FT REPEAT 192..213
FT /note="LRR 6"
FT REPEAT 216..237
FT /note="LRR 7"
FT REPEAT 264..285
FT /note="LRR 8"
FT REPEAT 288..309
FT /note="LRR 9"
FT REPEAT 312..333
FT /note="LRR 10"
FT REPEAT 336..357
FT /note="LRR 11"
FT DOMAIN 369..423
FT /note="LRRCT"
FT DOMAIN 411..513
FT /note="Ig-like C2-type"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D1T0"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17005555"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17005555"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17005555"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17005555"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17005555"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17005555"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17005555"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17005555"
FT DISULFID 46..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17005555"
FT DISULFID 373..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17005555"
FT DISULFID 375..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17005555"
FT DISULFID 446..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17005555"
FT VAR_SEQ 1..6
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032749"
FT VARIANT 183
FT /note="S -> F (in dbSNP:rs9855)"
FT /evidence="ECO:0000269|PubMed:14686891"
FT /id="VAR_042436"
FT VARIANT 288
FT /note="Y -> C (in MRT64; dbSNP:rs750612085)"
FT /evidence="ECO:0000269|PubMed:28837161"
FT /id="VAR_081164"
FT VARIANT 290
FT /note="R -> H (in MRT64; dbSNP:rs757077698)"
FT /evidence="ECO:0000269|PubMed:28837161"
FT /id="VAR_081165"
FT CONFLICT 46
FT /note="C -> Y (in Ref. 5; AAH68558)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="R -> C (in Ref. 2; AAQ88651)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="L -> Q (in Ref. 2; AAQ88651)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="K -> R (in Ref. 5; AAH68558)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="P -> R (in Ref. 5; AAH68558)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="S -> L (in Ref. 3; BAB55157)"
FT /evidence="ECO:0000305"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2ID5"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2ID5"
FT TURN 88..93
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2ID5"
FT TURN 112..117
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2ID5"
FT TURN 160..165
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:2ID5"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:2ID5"
FT TURN 257..262
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:2ID5"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2ID5"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:2ID5"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:2ID5"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:2ID5"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:2ID5"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:2ID5"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:2ID5"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:2ID5"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:2ID5"
FT TURN 416..419
FT /evidence="ECO:0007829|PDB:4OQT"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:4OQT"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:2ID5"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:4OQT"
FT STRAND 493..501
FT /evidence="ECO:0007829|PDB:2ID5"
FT STRAND 504..515
FT /evidence="ECO:0007829|PDB:2ID5"
SQ SEQUENCE 620 AA; 69876 MW; 1A96D311A20180C1 CRC64;
MQVSKRMLAG GVRSMPSPLL ACWQPILLLV LGSVLSGSAT GCPPRCECSA QDRAVLCHRK
RFVAVPEGIP TETRLLDLGK NRIKTLNQDE FASFPHLEEL ELNENIVSAV EPGAFNNLFN
LRTLGLRSNR LKLIPLGVFT GLSNLTKLDI SENKIVILLD YMFQDLYNLK SLEVGDNDLV
YISHRAFSGL NSLEQLTLEK CNLTSIPTEA LSHLHGLIVL RLRHLNINAI RDYSFKRLYR
LKVLEISHWP YLDTMTPNCL YGLNLTSLSI THCNLTAVPY LAVRHLVYLR FLNLSYNPIS
TIEGSMLHEL LRLQEIQLVG GQLAVVEPYA FRGLNYLRVL NVSGNQLTTL EESVFHSVGN
LETLILDSNP LACDCRLLWV FRRRWRLNFN RQQPTCATPE FVQGKEFKDF PDVLLPNYFT
CRRARIRDRK AQQVFVDEGH TVQFVCRADG DPPPAILWLS PRKHLVSAKS NGRLTVFPDG
TLEVRYAQVQ DNGTYLCIAA NAGGNDSMPA HLHVRSYSPD WPHQPNKTFA FISNQPGEGE
ANSTRATVPF PFDIKTLIIA TTMGFISFLG VVLFCLVLLF LWSRGKGNTK HNIEIEYVPR
KSDAGISSAD APRKFNMKMI
