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 28-JAN-2026, entry version 195. 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; Q7L985: LINGO2; NbExp=4; IntAct=EBI-719955, EBI-21691123; 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. 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; 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_001301186.2. [Q96FE5-2] DR RefSeq; NP_001288116.1; NM_001301187.2. [Q96FE5-2] DR RefSeq; NP_001288118.1; NM_001301189.2. [Q96FE5-2] DR RefSeq; NP_001288120.1; NM_001301191.2. [Q96FE5-2] DR RefSeq; NP_001288121.1; NM_001301192.2. [Q96FE5-2] DR RefSeq; NP_001288123.1; NM_001301194.2. [Q96FE5-2] DR RefSeq; NP_001288124.1; NM_001301195.2. [Q96FE5-2] DR RefSeq; NP_001288126.1; NM_001301197.2. [Q96FE5-2] DR RefSeq; NP_001288127.1; NM_001301198.2. [Q96FE5-2] DR RefSeq; NP_001288128.1; NM_001301199.2. [Q96FE5-2] DR RefSeq; NP_001288129.1; NM_001301200.2. [Q96FE5-2] DR RefSeq; NP_116197.4; NM_032808.6. [Q96FE5-1] DR RefSeq; XP_011520420.1; XM_011522118.3. [Q96FE5-2] DR RefSeq; XP_016878171.1; XM_017022682.2. [Q96FE5-2] DR RefSeq; XP_024305859.1; XM_024450091.2. [Q96FE5-2] DR RefSeq; XP_054234980.1; XM_054379005.1. [Q96FE5-2] DR RefSeq; XP_054234981.1; XM_054379006.1. [Q96FE5-2] DR RefSeq; XP_054234982.1; XM_054379007.1. [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; 55. DR CORUM; Q96FE5; -. DR DIP; DIP-60981N; -. DR FunCoup; Q96FE5; 427. DR IntAct; Q96FE5; 56. 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 GlyCosmos; Q96FE5; 10 sites, No reported glycans. DR GlyGen; Q96FE5; 10 sites, 3 N-linked glycans (3 sites). DR iPTMnet; Q96FE5; -. DR PhosphoSitePlus; Q96FE5; -. DR BioMuta; LINGO1; -. DR DMDM; 74760819; -. DR jPOST; Q96FE5; -. DR MassIVE; Q96FE5; -. DR PaxDb; 9606-ENSP00000347451; -. DR PeptideAtlas; Q96FE5; -. DR ProteomicsDB; 76516; -. [Q96FE5-1] DR ProteomicsDB; 76517; -. [Q96FE5-2] DR ABCD; Q96FE5; 2 sequenced antibodies. DR Antibodypedia; 2624; 441 antibodies from 36 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 AGR; HGNC:21205; -. DR ClinPGx; PA162394087; -. DR CTD; 84894; -. DR DisGeNET; 84894; -. DR GeneCards; LINGO1; -. DR HGNC; HGNC:21205; LINGO1. DR HPA; ENSG00000169783; Tissue enriched (brain). DR MalaCards; LINGO1; -. DR MIM; 609791; gene. DR MIM; 618103; phenotype. DR OpenTargets; ENSG00000169783; -. 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; 10061535at2759; -. DR PAN-GO; Q96FE5; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q96FE5; -. DR PathwayCommons; Q96FE5; -. DR Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation). DR SignaLink; Q96FE5; -. DR SIGNOR; Q96FE5; -. DR Agora; ENSG00000169783; -. DR BioGRID-ORCS; 84894; 14 hits in 1141 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. 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 157 other cell types or tissues. DR ExpressionAtlas; Q96FE5; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005154; F:epidermal growth factor receptor binding; IBA:GO_Central. DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central. DR GO; GO:0048666; P:neuron development; IBA:GO_Central. DR CDD; cd20969; IgI_Lingo-1; 1. DR FunFam; 2.60.40.10:FF:000076; Leucine-rich repeat and Ig domain-containing 4; 1. DR FunFam; 3.80.10.10:FF:000014; Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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; IPR032675; LRR_dom_sf. DR InterPro; IPR050541; LRR_TM_domain-containing. DR InterPro; IPR000372; LRRNT. DR PANTHER; PTHR24369; ANTIGEN BSP, PUTATIVE-RELATED; 1. DR PANTHER; PTHR24369:SF178; LEUCINE-RICH REPEAT AND IMMUNOGLOBULIN-LIKE DOMAIN-CONTAINING NOGO RECEPTOR-INTERACTING PROTEIN 1; 1. DR Pfam; PF07679; I-set; 1. DR Pfam; PF13855; LRR_8; 3. DR SMART; SM00409; IG; 1. DR SMART; SM00408; IGc2; 1. DR SMART; SM00369; LRR_TYP; 9. DR SMART; SM00013; LRRNT; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF52058; L domain-like; 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 Proteomics identification; Reference proteome; Repeat; Signal; KW 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 //