AGC1_YEAST
ID AGC1_YEAST Reviewed; 902 AA.
AC Q12482; D6W431;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Mitochondrial aspartate-glutamate transporter AGC1;
DE AltName: Full=Aspartate-glutamate carrier 1;
GN Name=AGC1; OrderedLocusNames=YPR021C; ORFNames=YP9367.01C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=9178508;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<573::aid-yea107>3.0.co;2-i;
RA el Moualij B., Duyckaerts C., Lamotte-Brasseur J., Sluse F.E.;
RT "Phylogenetic classification of the mitochondrial carrier family of
RT Saccharomyces cerevisiae.";
RL Yeast 13:573-581(1997).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14622413; DOI=10.1046/j.1365-2958.2003.03742.x;
RA Cavero S., Vozza A., del Arco A., Palmieri L., Villa A., Blanco E.,
RA Runswick M.J., Walker J.E., Cerdan S., Palmieri F., Satrustegui J.;
RT "Identification and metabolic role of the mitochondrial aspartate-glutamate
RT transporter in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 50:1257-1269(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC -!- FUNCTION: Calcium-dependent mitochondrial aspartate and glutamate
CC carrier. Transport of glutamate in mitochondria is required for
CC mitochondrial transamination reactions and ornithine synthesis. Plays
CC also a role in malate-aspartate NADH shuttle, which is critical for
CC growth on acetate and fatty acids. {ECO:0000269|PubMed:14622413,
CC ECO:0000269|PubMed:9178508}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:14622413}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:14622413}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; Z71255; CAA95017.1; -; Genomic_DNA.
DR EMBL; Z49274; CAA89275.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11447.1; -; Genomic_DNA.
DR PIR; S54495; S54495.
DR RefSeq; NP_015346.1; NM_001184118.1.
DR AlphaFoldDB; Q12482; -.
DR BioGRID; 36198; 109.
DR DIP; DIP-8968N; -.
DR STRING; 4932.YPR021C; -.
DR TCDB; 2.A.29.14.4; the mitochondrial carrier (mc) family.
DR iPTMnet; Q12482; -.
DR MaxQB; Q12482; -.
DR PaxDb; Q12482; -.
DR PRIDE; Q12482; -.
DR EnsemblFungi; YPR021C_mRNA; YPR021C; YPR021C.
DR GeneID; 856132; -.
DR KEGG; sce:YPR021C; -.
DR SGD; S000006225; AGC1.
DR VEuPathDB; FungiDB:YPR021C; -.
DR eggNOG; KOG0751; Eukaryota.
DR HOGENOM; CLU_014931_1_0_1; -.
DR InParanoid; Q12482; -.
DR OMA; YYYKSCQ; -.
DR BioCyc; YEAST:G3O-34181-MON; -.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR Reactome; R-SCE-8963693; Aspartate and asparagine metabolism.
DR PRO; PR:Q12482; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12482; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR GO; GO:0015297; F:antiporter activity; IDA:SGD.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IDA:SGD.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015292; F:uniporter activity; IDA:SGD.
DR GO; GO:0015810; P:aspartate transmembrane transport; IDA:SGD.
DR GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IMP:SGD.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:SGD.
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 3: Inferred from homology;
KW Amino-acid transport; Calcium; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..902
FT /note="Mitochondrial aspartate-glutamate transporter AGC1"
FT /id="PRO_0000227601"
FT TRANSMEM 534..554
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 681..702
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 731..751
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..806
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 528..614
FT /note="Solcar 1"
FT REPEAT 622..710
FT /note="Solcar 2"
FT REPEAT 725..813
FT /note="Solcar 3"
SQ SEQUENCE 902 AA; 104304 MW; 07D6F831E2CD15CF CRC64;
MEQINSNSRK KKQQLEVFKY FASVLTKEDK PISISNGMLD MPTVNSSKLT AGNGKPDTEK
LTGELILTYD DFIELISSSK TIYSKFTDHS FNLNQIPKNV FGCIFFAIDE QNKGYLTLND
WFYFNNLLEY DNYHLIILYE FFRKFDVENL KAKQKKELGS SSFNLKAADD RIKSINYGNR
FLSFDDLLLN LNQFKDTIRL LHESIDDNFV KDNKLLLDWN DFRFLKFYKC YHENEEYLSL
NSLVTILQND LKNEKIFIGF DRLAQMDSQG HRLALSKNQL TYLLRLFYSH RVSADIFSSL
NLSNTELLKA DNNSIPYNVF KDIFYLFQNF DLLNQIFHKY VTENNLNEQD IREQIVTKND
FMTVLNAQYN KVNNIIEFSP SQINLLFSIV ANSKENRRLR KRNQDRDDEL LNDHHYDSDI
DFFIHNEYLH GVSRSRKNLE SFNDYYHDLS DGFDQDSGVK KASKASTGLF ESVFGGKKDK
ATMRSDLTIE DFMKILNPNY LNDLVHQMEL QKNQNESLYI NYYFYPIFDS LYNFSLGSIA
GCIGATVVYP IDFIKTRMQA QRSLAQYKNS IDCLLKIISR EGIKGLYSGL GPQLIGVAPE
KAIKLTVNDF MRNRLTDKNG KLSLFPEIIS GASAGACQVI FTNPLEIVKI RLQVQSDYVG
ENIQQANETA TQIVKKLGLR GLYNGVAACL MRDVPFSAIY FPTYAHLKKD LFDFDPNDKT
KRNRLKTWEL LTAGAIAGMP AAFLTTPFDV IKTRLQIDPR KGETKYNGIF HAIRTILKEE
SFRSFFKGGG ARVLRSSPQF GFTLAAYELF KGFIPSPDNK LKSREGRKRF CIDDDAGNEE
TVVHSNGELP QQKFYSDDRK HANYYYKSCQ IAKTFIDLDN NFSRFDSSVY KNFQEHLRSI
NG
