LIGO1_MACFA
ID LIGO1_MACFA Reviewed; 614 AA.
AC Q9N008;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1;
DE Flags: Precursor;
GN Name=LINGO1; ORFNames=QccE-15489;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RX PubMed=11574149; DOI=10.1016/s0378-1119(01)00665-5;
RA Osada N., Hida M., Kususda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K.;
RT "Assignment of 118 novel cDNAs of cynomolgus monkey brain to human
RT chromosomes.";
RL Gene 275:31-37(2001).
RN [2]
RP ERRATUM OF PUBMED:11574149.
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K., Kususda J.;
RL Gene 278:267-267(2001).
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. Acts in conjunction with RTN4 and RTN4R in regulating
CC neuronal precursor cell motility during cortical development (By
CC similarity). {ECO:0000250|UniProtKB:Q96FE5,
CC ECO:0000250|UniProtKB:Q9D1T0}.
CC -!- SUBUNIT: Homotetramer. Forms a ternary complex with RTN4R/NGFR and
CC RTN4R/TNFRSF19 (By similarity). Interacts with NGRF, RTN4R and MYT1L
CC (By similarity). {ECO:0000250|UniProtKB:Q96FE5,
CC ECO:0000250|UniProtKB:Q9D1T0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9D1T0};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9D1T0}.
CC -!- DOMAIN: The intracellular domain of LINGO1 interacts with MYT1L.
CC {ECO:0000250|UniProtKB:Q9D1T0}.
CC -!- PTM: N-glycosylated. Contains predominantly high-mannose glycans (By
CC similarity). {ECO:0000250}.
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DR EMBL; AB046639; BAB03557.1; -; mRNA.
DR RefSeq; NP_001306386.1; NM_001319457.1.
DR AlphaFoldDB; Q9N008; -.
DR SMR; Q9N008; -.
DR STRING; 9541.XP_005560242.1; -.
DR GeneID; 102134975; -.
DR CTD; 84894; -.
DR eggNOG; KOG0619; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript 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_0000328644"
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:0000250|UniProtKB:Q9D1T0"
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"
SQ SEQUENCE 614 AA; 69188 MW; BA6C8BC7C993BE9A CRC64;
MLAGGVRSMP 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 NPISTIEGSM
LHELLRLQEI QLVGGQLAMV EPYAFRGLNY LRVLNVSGNQ LTTLEESVFH SVGNLETLIL
DSNPLACDCR LLWVFRRRWR LNFNRQQPTC ATPEFVQGKE FKDFPDVLLP NYFTCRRARI
RDRKAQQVFV DEGHTVQFVC RADGDPPPAI LWLSPRKHLV SAKSNGRLTV FPDGTLEVRY
AQVQDNGTYL CIAANAGGND SMPAHLHVRS YSPDWPHQPN KTFAFIPNQP GEGEANSTRA
TVPFPFDIKT LIIATTMGFI SFLGVVLFCL VLLFLWSRGK GNTKHNIEIE YVPRKSDAGI
SSADAPRKFN MKMI
