LIGO1_CHICK
ID LIGO1_CHICK Reviewed; 613 AA.
AC Q50L44;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1;
DE Short=cLINGO-1;
DE Flags: Precursor;
GN Name=LINGO1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=16024296; DOI=10.1016/j.modgep.2005.04.016;
RA Okafuji T., Tanaka H.;
RT "Expression pattern of LINGO-1 in the developing nervous system of the
RT chick embryo.";
RL Gene Expr. Patterns 6:57-62(2005).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. Forms ternary complex with RTN4R/NGFR and
CC RTN4R/TNFRSF19 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed broadly in the spinal cord, including
CC the ventral portion of the ventricular zone, and motor neurons.
CC Expressed also in the dorsal root ganglion and boundary cap cells at
CC dorsal and ventral roots. In the early embryonic brain, is first
CC expressed in the prosencephalon and the ventral mesencephalon, and
CC later in the telencephalon, the rostral part of the mesencephalon and
CC some parts of the hindbrain. Expressed also in the ventral part of the
CC neural retina and trigeminal and facial nerves.
CC {ECO:0000269|PubMed:16024296}.
CC -!- PTM: N-glycosylated. Contains predominantly high-mannose glycans (By
CC similarity). {ECO:0000250}.
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DR EMBL; AB195262; BAD97693.1; -; mRNA.
DR RefSeq; NP_001019748.1; NM_001024577.1.
DR RefSeq; XP_015134353.1; XM_015278867.1.
DR RefSeq; XP_015134354.1; XM_015278868.1.
DR AlphaFoldDB; Q50L44; -.
DR SMR; Q50L44; -.
DR STRING; 9031.ENSGALP00000004263; -.
DR PaxDb; Q50L44; -.
DR GeneID; 415344; -.
DR KEGG; gga:415344; -.
DR CTD; 84894; -.
DR VEuPathDB; HostDB:geneid_415344; -.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; Q50L44; -.
DR OrthoDB; 399926at2759; -.
DR PhylomeDB; Q50L44; -.
DR TreeFam; TF334360; -.
DR PRO; PR:Q50L44; -.
DR Proteomes; UP000000539; Unplaced.
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 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; 10.
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; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..613
FT /note="Leucine-rich repeat and immunoglobulin-like domain-
FT containing nogo receptor-interacting protein 1"
FT /id="PRO_0000328646"
FT TOPO_DOM 35..554
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 576..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..64
FT /note="LRRNT"
FT REPEAT 65..86
FT /note="LRR 1"
FT REPEAT 89..110
FT /note="LRR 2"
FT REPEAT 113..134
FT /note="LRR 3"
FT REPEAT 137..158
FT /note="LRR 4"
FT REPEAT 161..182
FT /note="LRR 5"
FT REPEAT 185..206
FT /note="LRR 6"
FT REPEAT 209..230
FT /note="LRR 7"
FT REPEAT 257..278
FT /note="LRR 8"
FT REPEAT 281..302
FT /note="LRR 9"
FT REPEAT 305..326
FT /note="LRR 10"
FT REPEAT 329..350
FT /note="LRR 11"
FT DOMAIN 362..416
FT /note="LRRCT"
FT DOMAIN 404..508
FT /note="Ig-like C2-type"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 39..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 366..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 368..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 439..490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 613 AA; 69580 MW; D6005E781EDCBCB8 CRC64;
MLAGEASMRS PILACWQPIL LLMLGSILSG SATGCPPRCE CSAQERAVLC HRKRFMVVPE
GIPTETRQLD LGKNRIKTLN QDEFANYPHL EELELNENII SAIEPGAFNN LFNLRTLGLR
SNRLKLIPLG VFTGLSNLTK LDISENKIVI LLDYMFQDLY NLKSLEVGDN DLVYISHRAF
SGLNSLEQLT LEKCNLTSIP TEALSHLHGL IVLRLRHLNI NAIRDYSFKR LYRLKVLEIS
HWPYLDTMTS NCLYGLNLTS LSITHCNLTS IPYVSVRHLV YLRFLNLSYN PIVTIEGSML
HDLLRLQEIQ LVGGQLTTVE PFAFRGLNYL RILNVSGNLL TTLEESAFHS VGNLETLILD
NNPLACDCRL LWVFRRRWRL NFNKQQPTCS TPEFVQGKEF KDFPDVLLPN YFTCRRARIR
DRKPQQIFVD EGHTVHFVCR ADGDPPPAIM WLSPRKHLIS TKTNGRLTVF PDGTLEVRYA
QIQDNGTYLC IASNAGGNDT MLAHLHVRSY SPDWPHQPNK TFAFISNQPN ESDANSTRAT
VPFPFDIKTL IIATTMGFIS FLGVVLFCLV LLFLWSRGKG NTKHNIEIEY VPRKSDAGIS
SADAPRKFNM KMI
