CNIH2_HUMAN
ID CNIH2_HUMAN Reviewed; 160 AA.
AC Q6PI25;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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, AND INTERACTION WITH GRIA1.
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).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=23103966; DOI=10.1097/wnr.0b013e32835ad229;
RA Drummond J.B., Simmons M., Haroutunian V., Meador-Woodruff J.H.;
RT "Upregulation of cornichon transcripts in the dorsolateral prefrontal
RT cortex in schizophrenia.";
RL NeuroReport 23:1031-1034(2012).
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}.
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 (By
CC similarity). Interacts with CACGN8 (By similarity). Interacts with
CC GRIA1. {ECO:0000250, ECO:0000269|PubMed:20805473}.
CC -!- INTERACTION:
CC Q6PI25; P19397: CD53; NbExp=3; IntAct=EBI-12815321, EBI-6657396;
CC Q6PI25; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12815321, EBI-6942903;
CC Q6PI25; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-12815321, EBI-3917143;
CC Q6PI25; P31937: HIBADH; NbExp=3; IntAct=EBI-12815321, EBI-11427100;
CC Q6PI25; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-12815321, EBI-8638294;
CC Q6PI25; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-12815321, EBI-12345267;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
CC projection, dendrite {ECO:0000250}. Cell projection, dendritic spine
CC {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Also localizes
CC to the cell membrane of extrasynaptic sites (dendritic shafts, spines
CC of pyramidal cells). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expression is up-regulated in dorsolateral
CC prefrontal cortex of patients with schizophrenia (postmortem brain
CC study). {ECO:0000269|PubMed:23103966}.
CC -!- SIMILARITY: Belongs to the cornichon family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC047953; AAH47953.1; -; mRNA.
DR CCDS; CCDS8131.1; -.
DR RefSeq; NP_872359.1; NM_182553.2.
DR AlphaFoldDB; Q6PI25; -.
DR SMR; Q6PI25; -.
DR BioGRID; 129026; 6.
DR IntAct; Q6PI25; 6.
DR STRING; 9606.ENSP00000310003; -.
DR TCDB; 8.A.61.1.8; the endoplasmic reticulum-derived vesicle protein, erv14 (erv14) family.
DR PhosphoSitePlus; Q6PI25; -.
DR BioMuta; CNIH2; -.
DR DMDM; 61563951; -.
DR MassIVE; Q6PI25; -.
DR PaxDb; Q6PI25; -.
DR PeptideAtlas; Q6PI25; -.
DR PRIDE; Q6PI25; -.
DR ProteomicsDB; 67134; -.
DR Antibodypedia; 30113; 141 antibodies from 23 providers.
DR DNASU; 254263; -.
DR Ensembl; ENST00000311445.7; ENSP00000310003.6; ENSG00000174871.11.
DR GeneID; 254263; -.
DR KEGG; hsa:254263; -.
DR MANE-Select; ENST00000311445.7; ENSP00000310003.6; NM_182553.3; NP_872359.1.
DR UCSC; uc001ohi.3; human.
DR CTD; 254263; -.
DR DisGeNET; 254263; -.
DR GeneCards; CNIH2; -.
DR HGNC; HGNC:28744; CNIH2.
DR HPA; ENSG00000174871; Tissue enriched (brain).
DR MIM; 611288; gene.
DR neXtProt; NX_Q6PI25; -.
DR OpenTargets; ENSG00000174871; -.
DR PharmGKB; PA134887358; -.
DR VEuPathDB; HostDB:ENSG00000174871; -.
DR eggNOG; KOG2729; Eukaryota.
DR GeneTree; ENSGT00950000182834; -.
DR InParanoid; Q6PI25; -.
DR OMA; DDFINPI; -.
DR OrthoDB; 1602458at2759; -.
DR PhylomeDB; Q6PI25; -.
DR TreeFam; TF300083; -.
DR PathwayCommons; Q6PI25; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR SignaLink; Q6PI25; -.
DR BioGRID-ORCS; 254263; 22 hits in 1063 CRISPR screens.
DR GenomeRNAi; 254263; -.
DR Pharos; Q6PI25; Tbio.
DR PRO; PR:Q6PI25; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6PI25; protein.
DR Bgee; ENSG00000174871; Expressed in cortical plate and 109 other tissues.
DR ExpressionAtlas; Q6PI25; baseline and differential.
DR Genevisible; Q6PI25; HS.
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; ISS:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0051668; P:localization within membrane; IEA:Ensembl.
DR GO; GO:1903743; P:negative regulation of anterograde synaptic vesicle transport; IEA:Ensembl.
DR GO; GO:1902684; P:negative regulation of receptor localization to synapse; IEA:Ensembl.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IDA:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IEA:Ensembl.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IEA:Ensembl.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
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; Cell projection; Endoplasmic reticulum; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..160
FT /note="Protein cornichon homolog 2"
FT /id="PRO_0000122225"
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; 18931 MW; 00330E5E609B28BF CRC64;
MAFTFAAFCY MLTLVLCASL IFFVIWHIIA FDELRTDFKN PIDQGNPARA RERLKNIERI
CCLLRKLVVP EYSIHGLFCL MFLCAAEWVT LGLNIPLLFY HLWRYFHRPA DGSEVMYDAV
SIMNADILNY CQKESWCKLA FYLLSFFYYL YSMVYTLVSF
