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 07-OCT-2020, entry version 128. 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}. Cell junction, synapse, CC postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein CC {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell CC projection, dendritic spine {ECO:0000250}. Cell junction, synapse, CC postsynaptic density {ECO:0000250}. Note=Also localizes to the cell CC membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal CC 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 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; 131 antibodies. DR DNASU; 254263; -. DR Ensembl; ENST00000311445; ENSP00000310003; ENSG00000174871. DR GeneID; 254263; -. DR KEGG; hsa:254263; -. DR UCSC; uc001ohi.3; human. DR CTD; 254263; -. DR DisGeNET; 254263; -. DR EuPathDB; HostDB:ENSG00000174871.10; -. 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 eggNOG; KOG2729; Eukaryota. DR GeneTree; ENSGT00950000182834; -. DR InParanoid; Q6PI25; -. DR KO; K20368; -. DR OMA; LAWNANK; -. 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 BioGRID-ORCS; 254263; 18 hits in 869 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 134 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: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:0000139; C:Golgi membrane; IEA:GOC. 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:0048208; P:COPII vesicle coating; TAS:Reactome. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:Reactome. 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 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 junction; 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_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 //