NEGR1_RAT
ID NEGR1_RAT Reviewed; 348 AA.
AC Q9Z0J8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Neuronal growth regulator 1;
DE AltName: Full=Kindred of IgLON;
DE Short=Kilon;
DE Flags: Precursor;
GN Name=Negr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 32-62.
RX PubMed=10075727; DOI=10.1074/jbc.274.12.8224;
RA Funatsu N., Miyata S., Kumanogoh H., Shigeta M., Hamada K., Endo Y.,
RA Sokawa Y., Maekawa S.;
RT "Characterization of a novel rat brain glycosylphosphatidylinositol-
RT anchored protein (Kilon), a member of the IgLON cell adhesion molecule
RT family.";
RL J. Biol. Chem. 274:8224-8230(1999).
CC -!- FUNCTION: May be involved in cell-adhesion. May function as a trans-
CC neural growth-promoting factor in regenerative axon sprouting in the
CC mammalian brain (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC {ECO:0000305}.
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DR EMBL; AB017139; BAA75649.1; -; mRNA.
DR RefSeq; NP_067714.1; NM_021682.1.
DR AlphaFoldDB; Q9Z0J8; -.
DR SMR; Q9Z0J8; -.
DR BioGRID; 248762; 1.
DR STRING; 10116.ENSRNOP00000035271; -.
DR GlyGen; Q9Z0J8; 6 sites, 5 N-linked glycans (5 sites).
DR iPTMnet; Q9Z0J8; -.
DR PhosphoSitePlus; Q9Z0J8; -.
DR PaxDb; Q9Z0J8; -.
DR PRIDE; Q9Z0J8; -.
DR Ensembl; ENSRNOT00000089396; ENSRNOP00000072152; ENSRNOG00000021410.
DR GeneID; 59318; -.
DR KEGG; rno:59318; -.
DR CTD; 257194; -.
DR RGD; 708416; Negr1.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000159289; -.
DR InParanoid; Q9Z0J8; -.
DR OrthoDB; 583722at2759; -.
DR PhylomeDB; Q9Z0J8; -.
DR TreeFam; TF351104; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:Q9Z0J8; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0007631; P:feeding behavior; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR GO; GO:0051963; P:regulation of synapse assembly; IMP:RGD.
DR Gene3D; 2.60.40.10; -; 3.
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 Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:10075727"
FT CHAIN 32..318
FT /note="Neuronal growth regulator 1"
FT /id="PRO_0000015041"
FT PROPEP 319..348
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015042"
FT DOMAIN 32..128
FT /note="Ig-like C2-type 1"
FT DOMAIN 133..215
FT /note="Ig-like C2-type 2"
FT DOMAIN 219..307
FT /note="Ig-like C2-type 3"
FT MOD_RES 181
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80Z24"
FT LIPID 318
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3B1"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 154..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 239..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 348 AA; 37858 MW; 37E90D1C7D24ACAB CRC64;
MVLLAQGACC SNQWLAAVLL SLCSCLPAGQ SVDFPWAAVD NMLVRKGDTA VLRCYLEDGA
SKGAWLNRSS IIFAGGDKWS VDPRVSISTL NKRDYSLQIQ NVDVTDDGPY TCSVQTQHTP
RTMQVHLTVQ VPPKIYDISN DMTINEGTNV TLTCLATGKP EPAISWRHIS PSAKPFENGQ
YLDIYGITRD QAGEYECSAE NDVSFPDVKK VRVVVNFAPT IQEIKSGTVT PGRSGLIRCE
GAGVPPPAFE WYKGEKRLFN GQQGIIIQNF STRSILTVTN VTQEHFGNYT CVAANKLGTT
NASLPLNPPS TAQYGITGSA CDLFSCWSLA LTLSSVISIF YLKNAILQ
