CNIH2_RAT
ID CNIH2_RAT Reviewed; 160 AA.
AC Q5BJU5;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19265014; DOI=10.1126/science.1167852;
RA Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B.,
RA Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.;
RT "Functional proteomics identify cornichon proteins as auxiliary subunits of
RT AMPA receptors.";
RL Science 323:1313-1319(2009).
RN [3]
RP FUNCTION, INTERACTION WITH GRIA1, AND TISSUE SPECIFICITY.
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:19265014, ECO:0000269|PubMed:20805473}.
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 with
CC CACGN8 (By similarity). Interacts with GRIA1. {ECO:0000250,
CC ECO:0000269|PubMed:19265014, ECO:0000269|PubMed:20805473}.
CC -!- INTERACTION:
CC Q5BJU5; P19490: Gria1; NbExp=3; IntAct=EBI-15874082, EBI-371642;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:19265014}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19265014}. Cell projection, dendrite {ECO:0000250}.
CC Cell projection, dendritic spine {ECO:0000250}. Postsynaptic density
CC {ECO:0000250}. Note=Also localizes to the cell membrane of
CC extrasynaptic sites (dendritic shafts, spines of pyramidal cells).
CC -!- TISSUE SPECIFICITY: Brain. Expressed in the neocortex, hippocampal
CC formation, and cerebellum (at protein level).
CC {ECO:0000269|PubMed:19265014, ECO:0000269|PubMed:20805473}.
CC -!- SIMILARITY: Belongs to the cornichon family. {ECO:0000305}.
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DR EMBL; BC091325; AAH91325.1; -; mRNA.
DR RefSeq; NP_001020303.1; NM_001025132.1.
DR PDB; 7OCA; EM; 3.40 A; E/G=1-160.
DR PDB; 7OCE; EM; 3.10 A; E/G=1-160.
DR PDB; 7OCF; EM; 3.60 A; E/G=1-160.
DR PDBsum; 7OCA; -.
DR PDBsum; 7OCE; -.
DR PDBsum; 7OCF; -.
DR AlphaFoldDB; Q5BJU5; -.
DR SMR; Q5BJU5; -.
DR CORUM; Q5BJU5; -.
DR DIP; DIP-59551N; -.
DR IntAct; Q5BJU5; 3.
DR STRING; 10116.ENSRNOP00000027421; -.
DR iPTMnet; Q5BJU5; -.
DR PhosphoSitePlus; Q5BJU5; -.
DR SwissPalm; Q5BJU5; -.
DR PaxDb; Q5BJU5; -.
DR GeneID; 361705; -.
DR KEGG; rno:361705; -.
DR CTD; 254263; -.
DR RGD; 1304930; Cnih2.
DR VEuPathDB; HostDB:ENSRNOG00000020247; -.
DR eggNOG; KOG2729; Eukaryota.
DR HOGENOM; CLU_112942_1_0_1; -.
DR InParanoid; Q5BJU5; -.
DR OMA; DDFINPI; -.
DR OrthoDB; 1602458at2759; -.
DR PhylomeDB; Q5BJU5; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR PRO; PR:Q5BJU5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020247; Expressed in Ammon's horn and 14 other tissues.
DR Genevisible; Q5BJU5; RN.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0051668; P:localization within membrane; IDA:MGI.
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:2000311; P:regulation of AMPA receptor activity; IDA:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:UniProtKB.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IDA:SynGO.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IDA: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; Endoplasmic reticulum;
KW Membrane; Postsynaptic cell membrane; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..160
FT /note="Protein cornichon homolog 2"
FT /id="PRO_0000122227"
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..39
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 47..66
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 88..107
FT /evidence="ECO:0007829|PDB:7OCE"
FT TURN 119..123
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 125..158
FT /evidence="ECO:0007829|PDB:7OCE"
SQ SEQUENCE 160 AA; 18931 MW; 00330E5E609B28BF CRC64;
MAFTFAAFCY MLTLVLCASL IFFVIWHIIA FDELRTDFKN PIDQGNPARA RERLKNIERI
CCLLRKLVVP EYSIHGLFCL MFLCAAEWVT LGLNIPLLFY HLWRYFHRPA DGSEVMYDAV
SIMNADILNY CQKESWCKLA FYLLSFFYYL YSMVYTLVSF
