CNIH2_MOUSE
ID CNIH2_MOUSE Reviewed; 160 AA.
AC O35089;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein cornichon homolog 2;
DE Short=CNIH-2;
DE AltName: Full=Cornichon family AMPA receptor auxiliary protein 2;
DE AltName: Full=Cornichon-like protein;
GN Name=Cnih2; Synonyms=Cnil;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetal brain;
RA Fujimoto N., Kawamoto S., Matsubara K., Okubo K.;
RT "Cloning of mouse homologue of Drosophila cornichon protein from 17.5 dpc
RT fetal brain.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 40-49, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10022955; DOI=10.1007/s004270050234;
RA Hwang S.-Y., Oh B., Zhang Z., Miller W., Solter D., Knowles B.B.;
RT "The mouse cornichon gene family.";
RL Dev. Genes Evol. 209:120-125(1999).
RN [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH CACGN8.
RX PubMed=21172611; DOI=10.1016/j.neuron.2010.11.026;
RA Kato A.S., Gill M.B., Ho M.T., Yu H., Tu Y., Siuda E.R., Wang H.,
RA Qian Y.W., Nisenbaum E.S., Tomita S., Bredt D.S.;
RT "Hippocampal AMPA receptor gating controlled by both TARP and cornichon
RT proteins.";
RL Neuron 68:1082-1096(2010).
RN [5]
RP FUNCTION.
RX PubMed=20805473; DOI=10.1073/pnas.1011706107;
RA Shi Y., Suh Y.H., Milstein A.D., Isozaki K., Schmid S.M., Roche K.W.,
RA Nicoll R.A.;
RT "Functional comparison of the effects of TARPs and cornichons on AMPA
RT receptor trafficking and gating.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16315-16319(2010).
CC -!- FUNCTION: Regulates the trafficking and gating properties of AMPA-
CC selective glutamate receptors (AMPARs). Promotes their targeting to the
CC cell membrane and synapses and modulates their gating properties by
CC regulating their rates of activation, deactivation and desensitization.
CC Blocks CACNG8-mediated resensitization of AMPA receptors.
CC {ECO:0000269|PubMed:20805473, ECO:0000269|PubMed:21172611}.
CC -!- SUBUNIT: Acts as an auxiliary subunit for AMPA-selective glutamate
CC receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4,
CC CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts
CC with GRIA1 (By similarity). Interacts with CACGN8. {ECO:0000250,
CC ECO:0000269|PubMed:21172611}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Postsynaptic density
CC {ECO:0000269|PubMed:21172611}. Cell projection, dendrite
CC {ECO:0000269|PubMed:21172611}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:21172611}. Postsynaptic cell membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Also
CC localizes to the cell membrane of extrasynaptic sites (dendritic
CC shafts, spines of pyramidal cells). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain. Highest levels seen in the hippocampus,
CC intermediate levels in the cerebral cortex, striatum olfactory bulb,
CC and thalamus and lower levels in the cerebellum (at protein level).
CC Also expressed in the lung. {ECO:0000269|PubMed:10022955,
CC ECO:0000269|PubMed:21172611}.
CC -!- DEVELOPMENTAL STAGE: First detected at the eight-cell stage. Expressed
CC in eight-cell embryo, blastocyst, 6.5-day whole embryo, 7.5-day
CC primitive streak, 11.5-day limb bud and in 13.5-day whole embryo.
CC {ECO:0000269|PubMed:10022955}.
CC -!- SIMILARITY: Belongs to the cornichon family. {ECO:0000305}.
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DR EMBL; AB006191; BAA21746.2; -; mRNA.
DR CCDS; CCDS29451.1; -.
DR RefSeq; NP_034050.1; NM_009920.4.
DR PDB; 7LDD; EM; 3.40 A; E/F=1-160.
DR PDB; 7LDE; EM; 3.90 A; E/F=1-160.
DR PDB; 7LEP; EM; 3.25 A; E/F=2-160.
DR PDBsum; 7LDD; -.
DR PDBsum; 7LDE; -.
DR PDBsum; 7LEP; -.
DR AlphaFoldDB; O35089; -.
DR SMR; O35089; -.
DR STRING; 10090.ENSMUSP00000025805; -.
DR PhosphoSitePlus; O35089; -.
DR PaxDb; O35089; -.
DR PeptideAtlas; O35089; -.
DR PRIDE; O35089; -.
DR ProteomicsDB; 283402; -.
DR Antibodypedia; 30113; 141 antibodies from 23 providers.
DR DNASU; 12794; -.
DR Ensembl; ENSMUST00000025805; ENSMUSP00000025805; ENSMUSG00000024873.
DR GeneID; 12794; -.
DR KEGG; mmu:12794; -.
DR UCSC; uc008gce.2; mouse.
DR CTD; 254263; -.
DR MGI; MGI:1277225; Cnih2.
DR VEuPathDB; HostDB:ENSMUSG00000024873; -.
DR eggNOG; KOG2729; Eukaryota.
DR GeneTree; ENSGT00950000182834; -.
DR HOGENOM; CLU_112942_1_0_1; -.
DR InParanoid; O35089; -.
DR OMA; DDFINPI; -.
DR OrthoDB; 1602458at2759; -.
DR PhylomeDB; O35089; -.
DR TreeFam; TF300083; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR BioGRID-ORCS; 12794; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Cnih2; mouse.
DR PRO; PR:O35089; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O35089; protein.
DR Bgee; ENSMUSG00000024873; Expressed in cortical plate and 145 other tissues.
DR ExpressionAtlas; O35089; baseline and differential.
DR Genevisible; O35089; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0016247; F:channel regulator activity; ISO:MGI.
DR GO; GO:0051668; P:localization within membrane; ISO:MGI.
DR GO; GO:1903743; P:negative regulation of anterograde synaptic vesicle transport; ISO:MGI.
DR GO; GO:1902684; P:negative regulation of receptor localization to synapse; ISO:MGI.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IDA:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISO:MGI.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; ISO:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR003377; Cornichon.
DR InterPro; IPR033466; Cornichon_conserved.
DR Pfam; PF03311; Cornichon; 2.
DR SMART; SM01398; Cornichon; 1.
DR PROSITE; PS01340; CORNICHON; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Direct protein sequencing;
KW Endoplasmic reticulum; Membrane; Postsynaptic cell membrane;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..160
FT /note="Protein cornichon homolog 2"
FT /id="PRO_0000122226"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..72
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT HELIX 5..35
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 51..85
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 126..158
FT /evidence="ECO:0007829|PDB:7LEP"
SQ SEQUENCE 160 AA; 18931 MW; 00330E5E609B28BF CRC64;
MAFTFAAFCY MLTLVLCASL IFFVIWHIIA FDELRTDFKN PIDQGNPARA RERLKNIERI
CCLLRKLVVP EYSIHGLFCL MFLCAAEWVT LGLNIPLLFY HLWRYFHRPA DGSEVMYDAV
SIMNADILNY CQKESWCKLA FYLLSFFYYL YSMVYTLVSF
