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PMP3_ASHGO
ID   PMP3_ASHGO              Reviewed;          55 AA.
AC   Q75C38;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Plasma membrane proteolipid 3;
GN   Name=PMP3; OrderedLocusNames=ACR079W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Plays a role in the regulation of membrane potential. Could
CC       mediate a proton leak (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the UPF0057 (PMP3) family. {ECO:0000305}.
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DR   EMBL; AE016816; AAS51305.1; -; Genomic_DNA.
DR   RefSeq; NP_983481.1; NM_208834.1.
DR   AlphaFoldDB; Q75C38; -.
DR   STRING; 33169.AAS51305; -.
DR   EnsemblFungi; AAS51305; AAS51305; AGOS_ACR079W.
DR   GeneID; 4619606; -.
DR   KEGG; ago:AGOS_ACR079W; -.
DR   eggNOG; KOG1773; Eukaryota.
DR   HOGENOM; CLU_107649_6_2_1; -.
DR   InParanoid; Q75C38; -.
DR   OMA; GWGRECI; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070300; F:phosphatidic acid binding; IEA:EnsemblFungi.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0046625; F:sphingolipid binding; IEA:EnsemblFungi.
DR   GO; GO:0006812; P:cation transport; IEA:EnsemblFungi.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:EnsemblFungi.
DR   GO; GO:0042391; P:regulation of membrane potential; IEA:EnsemblFungi.
DR   InterPro; IPR000612; PMP3.
DR   PANTHER; PTHR21659; PTHR21659; 1.
DR   Pfam; PF01679; Pmp3; 1.
DR   PROSITE; PS01309; UPF0057; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..55
FT                   /note="Plasma membrane proteolipid 3"
FT                   /id="PRO_0000247907"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   55 AA;  6138 MW;  B7604EF6B480CAD7 CRC64;
     MNSTKVVNVI IAIFLPPVAV FLARGWGVEC IVDLLLTIFF FFPGMLYALY IVLTS
 
 
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