LIGO1_XENTR
ID LIGO1_XENTR Reviewed; 606 AA.
AC A4IIW9; A8WGE9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1;
DE Flags: Precursor;
GN Name=lingo1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in regulating axonal regeneration and
CC plasticity in the adult central nervous system. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR EMBL; BC136185; AAI36186.1; -; mRNA.
DR EMBL; BC154684; AAI54685.1; -; mRNA.
DR RefSeq; NP_001093719.1; NM_001100249.1.
DR RefSeq; XP_012821306.1; XM_012965852.2.
DR RefSeq; XP_012821308.1; XM_012965854.2.
DR RefSeq; XP_012821309.1; XM_012965855.2.
DR RefSeq; XP_012821310.1; XM_012965856.2.
DR RefSeq; XP_012821311.1; XM_012965857.2.
DR RefSeq; XP_012821312.1; XM_012965858.2.
DR RefSeq; XP_017947388.1; XM_018091899.1.
DR AlphaFoldDB; A4IIW9; -.
DR SMR; A4IIW9; -.
DR PaxDb; A4IIW9; -.
DR DNASU; 100101739; -.
DR Ensembl; ENSXETT00000033400; ENSXETP00000033400; ENSXETG00000015270.
DR GeneID; 100101739; -.
DR KEGG; xtr:100101739; -.
DR CTD; 84894; -.
DR Xenbase; XB-GENE-921957; lingo1.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; A4IIW9; -.
DR OMA; MVAREAT; -.
DR OrthoDB; 399926at2759; -.
DR PhylomeDB; A4IIW9; -.
DR TreeFam; TF334360; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000015270; Expressed in brain and 11 other tissues.
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; 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; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
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; 8.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 9.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..606
FT /note="Leucine-rich repeat and immunoglobulin-like domain-
FT containing nogo receptor-interacting protein 1"
FT /id="PRO_0000328647"
FT TOPO_DOM 28..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..57
FT /note="LRRNT"
FT REPEAT 58..79
FT /note="LRR 1"
FT REPEAT 82..103
FT /note="LRR 2"
FT REPEAT 106..127
FT /note="LRR 3"
FT REPEAT 130..151
FT /note="LRR 4"
FT REPEAT 154..175
FT /note="LRR 5"
FT REPEAT 178..199
FT /note="LRR 6"
FT REPEAT 202..223
FT /note="LRR 7"
FT REPEAT 250..271
FT /note="LRR 8"
FT REPEAT 274..295
FT /note="LRR 9"
FT REPEAT 298..319
FT /note="LRR 10"
FT REPEAT 322..343
FT /note="LRR 11"
FT DOMAIN 355..409
FT /note="LRRCT"
FT DOMAIN 397..496
FT /note="Ig-like C2-type"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..34
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 32..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 359..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 361..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 432..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 354
FT /note="K -> R (in Ref. 1; AAI54685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 606 AA; 68704 MW; 61DAC8DDD1808029 CRC64;
MILQLPSCLC PILLIVVGSI LSGSASGCPQ RCDCSPQDRS VLCHRKRYLD VPEGIPTDTR
LLDLSKNRIK ALNQDEFSAF PYLEELELNE NIVSIIEPGA FNGLFNLRSL GLRSNRLKLI
PLGVFTGLSN LTQLDISENK IVILLDDMFQ DLYNLKSLEV GDNDLVYISH RAFRGLNSLE
ELTLEKCNLT SVPTEALSHL HGLITLKLRY LNINVIRDYS FKRLYRLKNL EIAHWPYLDT
MTSNGLYGLN LTSLSITHSN LSSIPYVAIR HLVYLRFLNL SYNPITAVEG SMLYELLRLQ
EFHLVGGQLS VVEPYAFRGL NHLKVLNVSS NYLSTLEESS FHSVGNLETL ILDKNPLACD
CRLLWIFRRR WRLNFSRQQP SCSSPEYVQG KEFKDFPDVL QPNYFTCRRA RIQDHSAQVV
YVDEGHTVHF FCRADGDPPP TILWQSPRKT FITSKSNGRL TVFPDGTLEV RYAQVQDNGT
YHCIASNAGG NDTSLAHLHV RSYSPNWPHK PNKTFAFMSN QPNESDVNST RASVPFPFDI
KTLIIATTMG FISFLGVVLF CLVLLFLWSR GKGNTKHNIE IEYVPRKSDA GLSSADAPRK
FNMKMI
