ASG7_YEAS7
ID ASG7_YEAS7 Reviewed; 209 AA.
AC A6ZQG3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Protein ASG7;
DE AltName: Full=A-specific gene 7 protein;
GN Name=ASG7; ORFNames=SCY_3124;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Required for receptor inhibition of inappropriately expressed
CC a-factor receptor (STE3) in MAT a cells. Inhibits signaling by
CC relocalizing the G protein beta-gamma (STE4-STE18) subunit to
CC intracellular membranes. May also be a mechanism for the down-
CC regulation of the mating pheromone response after the zygotic fusion
CC event, promoting the transition of the new diploid cell to vegetative
CC growth (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: Induced by alpha-pheromone. Repressed by the ALPHA2-MCM1
CC repressor (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN63215.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AAFW02000044; EDN63215.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A6ZQG3; -.
DR SMR; A6ZQG3; -.
DR EnsemblFungi; EDN63215; EDN63215; SCY_3124.
DR HOGENOM; CLU_114202_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT CHAIN 1..209
FT /note="Protein ASG7"
FT /id="PRO_0000330044"
FT TOPO_DOM 1..49
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..209
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46993"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46993"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46993"
FT MOD_RES 153
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46993"
SQ SEQUENCE 209 AA; 24949 MW; 52CCE840B71DB7AC CRC64;
MTTLASSIEH KTKHLAAPFE NDENTWMKKY CCQCKSCKMS VPVQPWLPRF FVFGILCPVF
WLVNLLAWWF LQYWQPHELE FHDLQEDEYP GFYEYEAITK RTVIPLKEEV LQEIRVMQNF
SDSNSEEYYE SKDGMPSSFL NVNTEQVEDE NDTLKKYRYA FLKKVAHDVL ESHDLLRKTF
RNWNLRSLLG LLIDSILIIF VVLLCKKSR