CNIH3_MOUSE
ID CNIH3_MOUSE Reviewed; 160 AA.
AC Q6ZWS4; Q14BS0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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 (By similarity). {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Note=Also localizes to the cell
CC membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal
CC cells). {ECO:0000250}.
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; AK033911; BAC28511.1; -; mRNA.
DR EMBL; BC115640; AAI15641.1; -; mRNA.
DR EMBL; BC115641; AAI15642.1; -; mRNA.
DR CCDS; CCDS48470.1; -.
DR RefSeq; NP_001153683.1; NM_001160211.1.
DR RefSeq; NP_001153684.1; NM_001160212.1.
DR RefSeq; NP_082684.1; NM_028408.3.
DR PDB; 6PEQ; EM; 2.97 A; E/F/G/H=1-160.
DR PDB; 6UCB; EM; 3.28 A; E/F/G/H=1-160.
DR PDB; 6UD4; EM; 3.30 A; E/F/G/H=1-160.
DR PDB; 6UD8; EM; 3.20 A; E/F/G/H=1-160.
DR PDBsum; 6PEQ; -.
DR PDBsum; 6UCB; -.
DR PDBsum; 6UD4; -.
DR PDBsum; 6UD8; -.
DR AlphaFoldDB; Q6ZWS4; -.
DR SMR; Q6ZWS4; -.
DR SwissPalm; Q6ZWS4; -.
DR PRIDE; Q6ZWS4; -.
DR ProteomicsDB; 283450; -.
DR Antibodypedia; 34640; 126 antibodies from 21 providers.
DR DNASU; 72978; -.
DR Ensembl; ENSMUST00000027795; ENSMUSP00000027795; ENSMUSG00000026514.
DR GeneID; 72978; -.
DR KEGG; mmu:72978; -.
DR UCSC; uc007dxi.2; mouse.
DR CTD; 149111; -.
DR MGI; MGI:1920228; Cnih3.
DR VEuPathDB; HostDB:ENSMUSG00000026514; -.
DR GeneTree; ENSGT00950000182834; -.
DR HOGENOM; CLU_112942_1_0_1; -.
DR InParanoid; Q6ZWS4; -.
DR OMA; QREAWCK; -.
DR OrthoDB; 1602458at2759; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR BioGRID-ORCS; 72978; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q6ZWS4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6ZWS4; protein.
DR Bgee; ENSMUSG00000026514; Expressed in cortical plate and 59 other tissues.
DR ExpressionAtlas; Q6ZWS4; baseline and differential.
DR Genevisible; Q6ZWS4; 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; IBA:GO_Central.
DR GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
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:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; 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; Membrane; Postsynaptic cell membrane;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..160
FT /note="Protein cornichon homolog 3"
FT /id="PRO_0000122229"
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 6..34
FT /evidence="ECO:0007829|PDB:6PEQ"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:6PEQ"
FT HELIX 69..84
FT /evidence="ECO:0007829|PDB:6PEQ"
FT HELIX 88..106
FT /evidence="ECO:0007829|PDB:6PEQ"
FT HELIX 128..157
FT /evidence="ECO:0007829|PDB:6PEQ"
SQ SEQUENCE 160 AA; 18976 MW; CF7E8645A9587504 CRC64;
MAFTFAAFCY MLSLVLCAAL IFFAIWHIIA FDELRTDFKS PIDQCNPVHA RERLRNIERI
CFLLRKLVLP EYSIHSLFCI MFLCAQEWLT LGLNVPLLFY HFWRYFHCPA DSSELAYDPP
VVMNADTLSY CQKEAWCKLA FYLLSFFYYL YCMIYTLVSS
