AGP2_YEAST
ID AGP2_YEAST Reviewed; 596 AA.
AC P38090; D6VQC9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=General amino acid permease AGP2;
GN Name=AGP2; OrderedLocusNames=YBR132C; ORFNames=YBR1007;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091856; DOI=10.1002/yea.320100002;
RA Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F.,
RA Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M.,
RA Herbert C.J.;
RT "The sequence of 29.7 kb from the right arm of chromosome II reveals 13
RT complete open reading frames, of which ten correspond to new genes.";
RL Yeast 10:S1-S11(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
RP DISCUSSION OF SEQUENCE.
RX PubMed=7954890; DOI=10.1007/bf00326297;
RA Nasr F., Becam A.-M., Grzybowska E., Zagulski M., Slonimski P.P.,
RA Herbert C.J.;
RT "An analysis of the sequence of part of the right arm of chromosome II of
RT S. cerevisiae reveals new genes encoding an amino-acid permease and a
RT carboxypeptidase.";
RL Curr. Genet. 26:1-7(1994).
RN [5]
RP CHARACTERIZATION.
RA Garrett J.M., Schreve J.L.;
RL Unpublished observations (JUL-1997).
RN [6]
RP FUNCTION IN CARNITINE TRANSPORT.
RX PubMed=10545096; DOI=10.1093/emboj/18.21.5843;
RA van Roermund C.W., Hettema E.H., van den Berg M., Tabak H.F., Wanders R.J.;
RT "Molecular characterization of carnitine-dependent transport of acetyl-CoA
RT from peroxisomes to mitochondria in Saccharomyces cerevisiae and
RT identification of a plasma membrane carnitine transporter, Agp2p.";
RL EMBO J. 18:5843-5852(1999).
RN [7]
RP FUNCTION IN CARNITINE TRANSPORT.
RX PubMed=12132580;
RA Lee J., Lee B., Shin D., Kwak S.S., Bahk J.D., Lim C.O., Yun D.J.;
RT "Carnitine uptake by AGP2 in yeast Saccharomyces cerevisiae is dependent on
RT Hog1 MAP kinase pathway.";
RL Mol. Cells 13:407-412(2002).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: General amino acid permease with broad substrate specificity.
CC Can also transport carnitine. {ECO:0000269|PubMed:10545096,
CC ECO:0000269|PubMed:12132580}.
CC -!- INTERACTION:
CC P38090; P43603: LSB3; NbExp=2; IntAct=EBI-2362, EBI-22980;
CC P38090; P32793: YSC84; NbExp=2; IntAct=EBI-2362, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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DR EMBL; X75891; CAA53491.1; -; Genomic_DNA.
DR EMBL; Z36001; CAA85089.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07249.1; -; Genomic_DNA.
DR PIR; S46001; S46001.
DR RefSeq; NP_009690.1; NM_001178480.1.
DR AlphaFoldDB; P38090; -.
DR SMR; P38090; -.
DR BioGRID; 32833; 118.
DR DIP; DIP-8141N; -.
DR IntAct; P38090; 8.
DR MINT; P38090; -.
DR STRING; 4932.YBR132C; -.
DR TCDB; 2.A.3.10.19; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P38090; -.
DR MaxQB; P38090; -.
DR PaxDb; P38090; -.
DR PRIDE; P38090; -.
DR EnsemblFungi; YBR132C_mRNA; YBR132C; YBR132C.
DR GeneID; 852429; -.
DR KEGG; sce:YBR132C; -.
DR SGD; S000000336; AGP2.
DR VEuPathDB; FungiDB:YBR132C; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_1_1; -.
DR InParanoid; P38090; -.
DR OMA; NTIIHYW; -.
DR BioCyc; YEAST:G3O-29087-MON; -.
DR SABIO-RK; P38090; -.
DR PRO; PR:P38090; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38090; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:1902274; P:positive regulation of (R)-carnitine transmembrane transport; IMP:SGD.
DR GO; GO:1902269; P:positive regulation of polyamine transmembrane transport; IMP:SGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..596
FT /note="General amino acid permease AGP2"
FT /id="PRO_0000054143"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..379
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..459
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..534
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 596 AA; 67262 MW; 8658DCDA5A7D6B64 CRC64;
MTKERMTIDY ENDGDFEYDK NKYKTITTRI KSIEPSEGWL EPSGSVGHIN TIPEAGDVHV
DEHEDRGSSI DDDSRTYLLY FTETRRKLEN RHVQLIAISG VIGTALFVAI GKALYRGGPA
SLLLAFALWC VPILCITVST AEMVCFFPVS SPFLRLATKC VDDSLAVMAS WNFWFLECVQ
IPFEIVSVNT IIHYWRDDYS AGIPLAVQVV LYLLISICAV KYYGEMEFWL ASFKIILALG
LFTFTFITML GGNPEHDRYG FRNYGESPFK KYFPDGNDVG KSSGYFQGFL ACLIQASFTI
AGGEYISMLA GEVKRPRKVL PKAFKQVFVR LTFLFLGSCL CVGIVCSPND PDLTAAINEA
RPGAGSSPYV IAMNNLKIRI LPDIVNIALI TAAFSAGNAY TYCSSRTFYG MALDGYAPKI
FTRCNRHGVP IYSVAISLVW ALVSLLQLNS NSAVVLNWLI NLITASQLIN FVVLCIVYLF
FRRAYHVQQD SLPKLPFRSW GQPYTAIIGL VSCSAMILIQ GYTVFFPKLW NTQDFLFSYL
MVFINIGIYV GYKFIWKRGK DHFKNPHEID FSKELTEIEN HEIESSFEKF QYYSKA
