GHC1_MOUSE
ID GHC1_MOUSE Reviewed; 323 AA.
AC Q9D6M3; Q3TRY1;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Mitochondrial glutamate carrier 1;
DE Short=GC-1;
DE AltName: Full=Glutamate/H(+) symporter 1;
DE AltName: Full=Solute carrier family 25 member 22;
GN Name=Slc25a22; Synonyms=Gc1;
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, and NOD;
RC TISSUE=Diencephalon, Head, Medulla oblongata, and Tongue;
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].
RC TISSUE=Eye;
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 [3]
RP PROTEIN SEQUENCE OF 12-33; 59-80; 84-91; 129-136; 180-196; 259-273 AND
RP 278-286, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mitochondrial glutamate/H(+) symporter. Responsible for the
CC transport of glutamate from the cytosol into the mitochondrial matrix
CC with the concomitant import of a proton (By similarity). Plays a role
CC in the control of glucose-stimulated insulin secretion (By similarity).
CC {ECO:0000250|UniProtKB:A0A0G2K5L2, ECO:0000250|UniProtKB:Q9H936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-glutamate(in) = H(+)(out) + L-glutamate(out);
CC Xref=Rhea:RHEA:70955, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985;
CC Evidence={ECO:0000250|UniProtKB:Q9H936};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:A0A0G2K5L2}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AK010193; BAB26760.1; -; mRNA.
DR EMBL; AK046874; BAC32903.1; -; mRNA.
DR EMBL; AK048389; BAC33318.1; -; mRNA.
DR EMBL; AK049313; BAC33676.1; -; mRNA.
DR EMBL; AK155276; BAE33159.1; -; mRNA.
DR EMBL; AK162400; BAE36895.1; -; mRNA.
DR EMBL; BC037949; AAH37949.1; -; mRNA.
DR CCDS; CCDS22013.1; -.
DR RefSeq; NP_001171047.1; NM_001177576.1.
DR RefSeq; NP_080922.1; NM_026646.3.
DR RefSeq; XP_006536295.1; XM_006536232.1.
DR RefSeq; XP_006536296.1; XM_006536233.3.
DR AlphaFoldDB; Q9D6M3; -.
DR SMR; Q9D6M3; -.
DR BioGRID; 212770; 15.
DR IntAct; Q9D6M3; 7.
DR MINT; Q9D6M3; -.
DR STRING; 10090.ENSMUSP00000019226; -.
DR iPTMnet; Q9D6M3; -.
DR PhosphoSitePlus; Q9D6M3; -.
DR SwissPalm; Q9D6M3; -.
DR EPD; Q9D6M3; -.
DR jPOST; Q9D6M3; -.
DR MaxQB; Q9D6M3; -.
DR PeptideAtlas; Q9D6M3; -.
DR PRIDE; Q9D6M3; -.
DR ProteomicsDB; 271218; -.
DR Antibodypedia; 9992; 68 antibodies from 21 providers.
DR DNASU; 68267; -.
DR Ensembl; ENSMUST00000019226; ENSMUSP00000019226; ENSMUSG00000019082.
DR Ensembl; ENSMUST00000106007; ENSMUSP00000101629; ENSMUSG00000019082.
DR Ensembl; ENSMUST00000201710; ENSMUSP00000144231; ENSMUSG00000019082.
DR GeneID; 68267; -.
DR KEGG; mmu:68267; -.
DR UCSC; uc009kkz.2; mouse.
DR CTD; 79751; -.
DR MGI; MGI:1915517; Slc25a22.
DR VEuPathDB; HostDB:ENSMUSG00000019082; -.
DR eggNOG; KOG0750; Eukaryota.
DR GeneTree; ENSGT00940000161196; -.
DR InParanoid; Q9D6M3; -.
DR OMA; WQREGPT; -.
DR OrthoDB; 945010at2759; -.
DR PhylomeDB; Q9D6M3; -.
DR TreeFam; TF313209; -.
DR Reactome; R-MMU-428643; Organic anion transporters.
DR BioGRID-ORCS; 68267; 13 hits in 76 CRISPR screens.
DR ChiTaRS; Slc25a22; mouse.
DR PRO; PR:Q9D6M3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D6M3; protein.
DR Bgee; ENSMUSG00000019082; Expressed in dentate gyrus of hippocampal formation granule cell and 247 other tissues.
DR ExpressionAtlas; Q9D6M3; baseline and differential.
DR Genevisible; Q9D6M3; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005280; F:amino acid:proton symporter activity; ISS:UniProtKB.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015810; P:aspartate transmembrane transport; IBA:GO_Central.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0043490; P:malate-aspartate shuttle; IBA:GO_Central.
DR GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..323
FT /note="Mitochondrial glutamate carrier 1"
FT /id="PRO_0000090620"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 6..93
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 101..214
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 223..312
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 323 AA; 34670 MW; CCAED09AB4CF73AE CRC64;
MADKQISLPA KLINGGIAGL IGVTCVFPID LAKTRLQNQQ NGQRMYASMS DCLIKTIRSE
GYFGMYRGAA VNLTLVTPEK AIKLAANDFF RHQLSKDGQK LTLPKEMLAG CGAGTCQVIV
TTPMEMLKIQ LQDAGRIAAQ RKILAAQAQL SAQGGAQPSV EAPAPPRPTA TQLTRDLLRN
HGIAGLYKGL GATLLRDVPF SIVYFPLFAN LNQLGRPSSE EKSPFYVSFL AGCVAGSAAA
VAVNPCDVVK TRLQSLERGV NEDTYSGFLD CARKIWRHEG PSAFLKGAYC RALVIAPLFG
IAQVVYFLGI AESLLGLLQE PQA
