GPR1_YARLI
ID GPR1_YARLI Reviewed; 270 AA.
AC P41943; Q96VC8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 3.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Glyoxylate pathway regulator;
GN Name=GPR1; OrderedLocusNames=YALI0C23617g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B204-12C;
RX PubMed=8169196; DOI=10.1128/jb.176.9.2477-2482.1994;
RA Schmid-Berger N., Schmid B., Barth G.;
RT "Ylt1, a highly repetitive retrotransposon in the genome of the dimorphic
RT fungus Yarrowia lipolytica.";
RL J. Bacteriol. 176:2477-2482(1994).
RN [2]
RP SEQUENCE REVISION TO 225-229; 244 AND 248.
RA Barth G.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND MUTAGENESIS OF TYR-58 AND SER-74.
RC STRAIN=PO1d;
RX PubMed=12634328; DOI=10.1099/mic.0.25917-0;
RA Augstein A., Barth K., Gentsch M., Kohlwein S.D., Barth G.;
RT "Characterization, localization and functional analysis of Gpr1p, a protein
RT affecting sensitivity to acetic acid in the yeast Yarrowia lipolytica.";
RL Microbiology 149:589-600(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Plays a role in the adaptation of cell metabolism to the
CC utilization of acetic acid, possibly by inhibiting an anion-
CC transporting ATPase and affecting the plasma membrane H(+)-ATPase. May
CC be indirectly involved in the repression of genes encoding glyoxylate
CC cycle enzymes. {ECO:0000269|PubMed:12634328}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12634328}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:12634328}.
CC -!- INDUCTION: By acetic acid and ethanol. {ECO:0000269|PubMed:12634328}.
CC -!- SIMILARITY: Belongs to the acetate uptake transporter (AceTr) (TC
CC 2.A.96) family. {ECO:0000305}.
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DR EMBL; X74146; CAA52243.2; -; Genomic_DNA.
DR EMBL; AJ313508; CAC44466.1; -; Genomic_DNA.
DR EMBL; CR382129; CAG82510.1; -; Genomic_DNA.
DR RefSeq; XP_502188.1; XM_502188.1.
DR AlphaFoldDB; P41943; -.
DR SMR; P41943; -.
DR STRING; 284591.P41943; -.
DR TCDB; 2.A.96.1.2; the acetate uptake transporter (acetr) family.
DR EnsemblFungi; CAG82510; CAG82510; YALI0_C23617g.
DR GeneID; 2909559; -.
DR KEGG; yli:YALI0C23617g; -.
DR VEuPathDB; FungiDB:YALI0_C23617g; -.
DR HOGENOM; CLU_051062_0_0_1; -.
DR InParanoid; P41943; -.
DR OMA; VAMTWMI; -.
DR Proteomes; UP000001300; Chromosome C.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015123; F:acetate transmembrane transporter activity; IBA:GO_Central.
DR InterPro; IPR000791; Gpr1/Fun34/SatP.
DR Pfam; PF01184; Gpr1_Fun34_YaaH; 1.
DR PROSITE; PS01114; GPR1_FUN34_YAAH; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..270
FT /note="Glyoxylate pathway regulator"
FT /id="PRO_0000135702"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MUTAGEN 58
FT /note="Y->E,F: No effect on sensitivity of cells to acetic
FT acid."
FT /evidence="ECO:0000269|PubMed:12634328"
FT MUTAGEN 74
FT /note="S->A,Q: No effect on sensitivity of cells to acetic
FT acid."
FT /evidence="ECO:0000269|PubMed:12634328"
FT MUTAGEN 74
FT /note="S->H,D: No effect on sensitivity of cells to acetic
FT acid."
FT /evidence="ECO:0000269|PubMed:12634328"
FT CONFLICT 248
FT /note="G -> D (in Ref. 1; CAA52243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 29438 MW; 7F1FCBB619B2AF5B CRC64;
MNTEIPDLEK QQIDHNSGSD DPQPIHDDMA PVSRIRSSGP NHEYIHIADQ KFHRDDFYRA
FGGTLNPGGA PQPSRKFGNP APLGLSAFAL TTLVFSLCTV QARGVPNPSI AVGLALFYGG
VCQFAAGMWE FVQENTFGAA ALTSYGGFWM SWAAIEMNAF GIKDSYNDPI EVQNAVGIYL
FGWFIFTLML TLCTLKSTVA FFGLFFMLMM TFLVLACANV TQHHGTAIGG GWLGIITAFF
GFYNAYAGLA NPGNSYIVPV PLDMPFVKKD
