GHC2_MOUSE
ID GHC2_MOUSE Reviewed; 320 AA.
AC Q9DB41; B2RPU3; Q14AI5;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 4.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Mitochondrial glutamate carrier 2;
DE Short=GC-2;
DE AltName: Full=Glutamate/H(+) symporter 2;
DE AltName: Full=Solute carrier family 25 member 18;
GN Name=Slc25a18; Synonyms=Gc2;
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] (ISOFORM 1).
RC TISSUE=Brain;
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 PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
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).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12865426; DOI=10.1074/jbc.m304940200;
RA Da Cruz S., Xenarios I., Langridge J., Vilbois F., Parone P.A.,
RA Martinou J.-C.;
RT "Proteomic analysis of the mouse liver mitochondrial inner membrane.";
RL J. Biol. Chem. 278:41566-41571(2003).
CC -!- FUNCTION: Responsible for the transport of glutamate from the cytosol
CC into the mitochondrial matrix with the concomitant import of a proton
CC (symport system). {ECO:0000250|UniProtKB:Q9H1K4}.
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:Q9H1K4};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:12865426}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DB41-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DB41-2; Sequence=VSP_022262;
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; BC116828; AAI16829.2; -; mRNA.
DR EMBL; BC137603; AAI37604.1; -; mRNA.
DR EMBL; AK005250; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS39614.1; -. [Q9DB41-1]
DR RefSeq; NP_001074517.1; NM_001081048.2. [Q9DB41-1]
DR RefSeq; XP_006506712.1; XM_006506649.3. [Q9DB41-1]
DR RefSeq; XP_006506713.1; XM_006506650.3. [Q9DB41-1]
DR AlphaFoldDB; Q9DB41; -.
DR SMR; Q9DB41; -.
DR BioGRID; 214940; 1.
DR IntAct; Q9DB41; 2.
DR MINT; Q9DB41; -.
DR STRING; 10090.ENSMUSP00000108302; -.
DR iPTMnet; Q9DB41; -.
DR PhosphoSitePlus; Q9DB41; -.
DR SwissPalm; Q9DB41; -.
DR jPOST; Q9DB41; -.
DR MaxQB; Q9DB41; -.
DR PaxDb; Q9DB41; -.
DR PeptideAtlas; Q9DB41; -.
DR PRIDE; Q9DB41; -.
DR ProteomicsDB; 268876; -. [Q9DB41-1]
DR ProteomicsDB; 268877; -. [Q9DB41-2]
DR Antibodypedia; 22673; 76 antibodies from 16 providers.
DR DNASU; 71803; -.
DR Ensembl; ENSMUST00000112682; ENSMUSP00000108302; ENSMUSG00000004902. [Q9DB41-1]
DR GeneID; 71803; -.
DR KEGG; mmu:71803; -.
DR UCSC; uc009dnq.1; mouse. [Q9DB41-1]
DR CTD; 83733; -.
DR MGI; MGI:1919053; Slc25a18.
DR VEuPathDB; HostDB:ENSMUSG00000004902; -.
DR eggNOG; KOG0750; Eukaryota.
DR GeneTree; ENSGT00940000162050; -.
DR HOGENOM; CLU_015166_3_4_1; -.
DR InParanoid; Q9DB41; -.
DR OMA; LMTQVHS; -.
DR OrthoDB; 945010at2759; -.
DR PhylomeDB; Q9DB41; -.
DR TreeFam; TF313209; -.
DR Reactome; R-MMU-428643; Organic anion transporters.
DR BioGRID-ORCS; 71803; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q9DB41; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9DB41; protein.
DR Bgee; ENSMUSG00000004902; Expressed in lumbar subsegment of spinal cord and 84 other tissues.
DR Genevisible; Q9DB41; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
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; IBA:GO_Central.
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 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 Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome; Repeat;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..320
FT /note="Mitochondrial glutamate carrier 2"
FT /id="PRO_0000090622"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..128
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 11..97
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 105..215
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 224..313
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1K4"
FT VAR_SEQ 1..17
FT /note="MIACRMSSQDLSISAKL -> TPSSCRTKI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_022262"
SQ SEQUENCE 320 AA; 34166 MW; 1FC0AD760C44E6FE CRC64;
MIACRMSSQD LSISAKLING GIAGLVGVTC VFPIDLAKTR LQNQQGKDVY RGMTDCLMKT
ARAEGFLGMY RGAAVNLTLV TPEKAIKLAA NDFLRQLLMQ DGTQRNLKME MLAGCGAGIC
QVVITCPMEM LKIQLQDAGR LAVCHQASAS ATPTSRPYST GSTSTHRRPS ATLIARELLR
TQGLSGLYRG LGATLLRDIP FSIIYFPLFA NLNQLGVSEL TGKASFTHSF VAGCTAGSVA
AVAVTPLDVL KTRIQTLKKG LGEDTYSGVT DCARKLWTQE GPAAFMKGAG CRALVIAPLF
GIAQGVYFIG IGERILKCFE
