ID   CNIH3_RAT               Reviewed;         160 AA.
AC   D0Q0Y7;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Protein cornichon homolog 3;
DE            Short=CNIH-3;
DE   AltName: Full=Cornichon family AMPA receptor auxiliary protein 3;
GN   Name=Cnih3;
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], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Brain;
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).
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       {ECO:0000269|PubMed:19265014}.
CC   -!- SUBUNIT: Acts as an auxiliary subunit for AMPA-selective glutamate
CC       receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4,
CC       CNIH2, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8.
CC       {ECO:0000269|PubMed:19265014}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000269|PubMed:19265014}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:19265014}. Note=Also localizes to the cell membrane
CC       of 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}.
CC   -!- SIMILARITY: Belongs to the cornichon family. {ECO:0000305}.
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DR   EMBL; FJ403327; ACQ83464.1; -; mRNA.
DR   RefSeq; NP_001160050.1; NM_001166578.1.
DR   AlphaFoldDB; D0Q0Y7; -.
DR   SMR; D0Q0Y7; -.
DR   CORUM; D0Q0Y7; -.
DR   STRING; 10116.ENSRNOP00000035332; -.
DR   PaxDb; D0Q0Y7; -.
DR   PeptideAtlas; D0Q0Y7; -.
DR   GeneID; 690252; -.
DR   KEGG; rno:690252; -.
DR   UCSC; RGD:1582859; rat.
DR   CTD; 149111; -.
DR   RGD; 1582859; Cnih3.
DR   VEuPathDB; HostDB:ENSRNOG00000022724; -.
DR   eggNOG; KOG2729; Eukaryota.
DR   HOGENOM; CLU_112942_1_0_1; -.
DR   InParanoid; D0Q0Y7; -.
DR   OMA; QREAWCK; -.
DR   OrthoDB; 1602458at2759; -.
DR   PhylomeDB; D0Q0Y7; -.
DR   Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR   Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR   PRO; PR:D0Q0Y7; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000022724; Expressed in frontal cortex and 4 other tissues.
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; IBA:GO_Central.
DR   GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0016247; F:channel regulator activity; IDA:MGI.
DR   GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:RGD.
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: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   Cell membrane; Membrane; Postsynaptic cell membrane; Reference proteome;
KW   Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN           1..160
FT                   /note="Protein cornichon homolog 3"
FT                   /id="PRO_0000408978"
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"
SQ   SEQUENCE   160 AA;  18962 MW;  D9043A83D3E4A504 CRC64;
     MAFTFAAFCY MLSLVLCAAL IFFAIWHIIA FDELRTDFKS PIDQCNPVHA RERLRNIERI
     CFLLRKLVLP EYSIHSLFCV MFLCAQEWLT LGLNVPLLFY HFWRYFHCPA DSSELAYDPP
     VVMNADTLSY CQKEAWCKLA FYLLSFFYYL YCMIYTLVSS