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Database: UniProt
Entry: A4IIW9
LinkDB: A4IIW9
Original site: A4IIW9 
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   27-MAR-2024, entry version 105.
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   STRING; 8364.ENSXETP00000035737; -.
DR   GlyCosmos; A4IIW9; 12 sites, No reported glycans.
DR   PaxDb; 8364-ENSXETP00000033400; -.
DR   DNASU; 100101739; -.
DR   Ensembl; ENSXETT00000033400; ENSXETP00000033400; ENSXETG00000015270.
DR   Ensembl; ENSXETT00000108254; ENSXETP00000106699; ENSXETG00000015270.
DR   Ensembl; ENSXETT00000111687; ENSXETP00000103263; ENSXETG00000015270.
DR   Ensembl; ENSXETT00000115070; ENSXETP00000107208; ENSXETG00000015270.
DR   Ensembl; ENSXETT00000118343; ENSXETP00000105338; ENSXETG00000015270.
DR   Ensembl; ENSXETT00000118711; ENSXETP00000114321; ENSXETG00000015270.
DR   Ensembl; ENSXETT00000121050; ENSXETP00000108744; ENSXETG00000015270.
DR   GeneID; 100101739; -.
DR   KEGG; xtr:100101739; -.
DR   AGR; Xenbase:XB-GENE-921957; -.
DR   CTD; 84894; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   HOGENOM; CLU_000288_18_24_1; -.
DR   InParanoid; A4IIW9; -.
DR   OMA; MVAREAT; -.
DR   OrthoDB; 2911036at2759; -.
DR   PhylomeDB; A4IIW9; -.
DR   TreeFam; TF334360; -.
DR   Reactome; R-XTR-193634; Axonal growth inhibition (RHOA activation).
DR   Proteomes; UP000008143; Chromosome 3.
DR   Bgee; ENSXETG00000015270; Expressed in brain and 11 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR000372; LRRNT.
DR   PANTHER; PTHR24369; ANTIGEN BSP, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR24369:SF210; CHAOPTIN-RELATED; 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; 8.
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; 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
//
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