CNI1_CAEEL
ID CNI1_CAEEL Reviewed; 145 AA.
AC Q22361;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein cornichon homolog 1 {ECO:0000312|WormBase:T09E8.3};
GN Name=cni-1 {ECO:0000312|WormBase:T09E8.3};
GN Synonyms=cnih-2 {ECO:0000303|PubMed:22213799};
GN ORFNames=T09E8.3 {ECO:0000312|WormBase:T09E8.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=22213799; DOI=10.1083/jcb.201104141;
RA Zhang D., Isack N.R., Glodowski D.R., Liu J., Chen C.C., Xu X.Z.,
RA Grant B.D., Rongo C.;
RT "RAB-6.2 and the retromer regulate glutamate receptor recycling through a
RT retrograde pathway.";
RL J. Cell Biol. 196:85-101(2012).
RN [3]
RP FUNCTION, INTERACTION WITH GLR-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=24094107; DOI=10.1016/j.neuron.2013.07.028;
RA Brockie P.J., Jensen M., Mellem J.E., Jensen E., Yamasaki T., Wang R.,
RA Maxfield D., Thacker C., Hoerndli F., Dunn P.J., Tomita S., Madsen D.M.,
RA Maricq A.V.;
RT "Cornichons control ER export of AMPA receptors to regulate synaptic
RT excitability.";
RL Neuron 80:129-142(2013).
CC -!- FUNCTION: Negatively regulates export of glr-1 from the endoplasmic
CC reticulum to synapses. {ECO:0000269|PubMed:24094107}.
CC -!- SUBUNIT: Interacts with glr-1. {ECO:0000269|PubMed:24094107}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24094107}; Multi-pass membrane protein
CC {ECO:0000255}. Synapse {ECO:0000269|PubMed:24094107}. Cell projection,
CC dendrite {ECO:0000269|PubMed:22213799}.
CC -!- TISSUE SPECIFICITY: Widely expressed in the nervous system including in
CC the AVA interneurons. {ECO:0000269|PubMed:24094107}.
CC -!- DISRUPTION PHENOTYPE: Hyperreversal phenotype with considerably shorter
CC average forward time than wild-type and a corresponding increase in
CC frequency of reversals. Increased anterograde transport of glr-1 with
CC corresponding increases in synaptic glr-1 expression and glr-1-mediated
CC currents. Altered pattern of glr-1 glycosylation, indicative of
CC increased export from the endoplasmic reticulum.
CC {ECO:0000269|PubMed:24094107}.
CC -!- SIMILARITY: Belongs to the cornichon family. {ECO:0000305}.
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DR EMBL; Z78065; CAB01516.2; -; Genomic_DNA.
DR PIR; A89261; A89261.
DR PIR; T24750; T24750.
DR RefSeq; NP_506278.1; NM_073877.4.
DR AlphaFoldDB; Q22361; -.
DR SMR; Q22361; -.
DR BioGRID; 44819; 1.
DR STRING; 6239.T09E8.3; -.
DR EPD; Q22361; -.
DR PaxDb; Q22361; -.
DR PeptideAtlas; Q22361; -.
DR EnsemblMetazoa; T09E8.3.1; T09E8.3.1; WBGene00011648.
DR GeneID; 179801; -.
DR KEGG; cel:CELE_T09E8.3; -.
DR UCSC; T09E8.3; c. elegans.
DR CTD; 179801; -.
DR WormBase; T09E8.3; CE23961; WBGene00011648; cni-1.
DR eggNOG; KOG2729; Eukaryota.
DR GeneTree; ENSGT00950000182834; -.
DR HOGENOM; CLU_112942_1_0_1; -.
DR InParanoid; Q22361; -.
DR OMA; WIAFLLN; -.
DR OrthoDB; 1602458at2759; -.
DR PhylomeDB; Q22361; -.
DR Reactome; R-CEL-204005; COPII-mediated vesicle transport.
DR Reactome; R-CEL-5694530; Cargo concentration in the ER.
DR PRO; PR:Q22361; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00011648; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IMP:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:1903743; P:negative regulation of anterograde synaptic vesicle transport; IMP:UniProtKB.
DR GO; GO:1902684; P:negative regulation of receptor localization to synapse; IMP:UniProtKB.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; IMP:UniProtKB.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IMP:UniProtKB.
DR GO; GO:0050795; P:regulation of behavior; IMP:UniProtKB.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:UniProtKB.
DR InterPro; IPR003377; Cornichon.
DR InterPro; IPR033466; Cornichon_conserved.
DR Pfam; PF03311; Cornichon; 1.
DR SMART; SM01398; Cornichon; 1.
DR PROSITE; PS01340; CORNICHON; 1.
PE 1: Evidence at protein level;
KW Cell projection; Endoplasmic reticulum; Membrane; Reference proteome;
KW Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..145
FT /note="Protein cornichon homolog 1"
FT /id="PRO_0000122239"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 145 AA; 16830 MW; 5C1C032B25DCE73C CRC64;
MAFTFAAFCY LLALIAVGFC IFFAIYTVIC VDELRTDYKN PIEQCRNLNQ LILPEYIIHG
TFTVLFIFSW QLISILANLP LAFYHIYTYA KRPVMSGPGI YDPTTILNRS TLSSTLRISW
IKLAFYLVSF FYYLYAMIYT LVTSN
