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PALH_ASHGO
ID   PALH_ASHGO              Reviewed;         502 AA.
AC   Q758G4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=pH-response regulator protein palH/RIM21;
GN   Name=RIM21; Synonyms=PAL2; OrderedLocusNames=AEL202C;
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], AND FUNCTION.
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: Required for the proteolytic cleavage of the transcription
CC       factor RIM101 in response to alkaline ambient pH.
CC       {ECO:0000269|PubMed:15001715}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the palH/RIM21 family. {ECO:0000305}.
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DR   EMBL; AE016818; AAS52483.1; -; Genomic_DNA.
DR   RefSeq; NP_984659.1; NM_210012.1.
DR   AlphaFoldDB; Q758G4; -.
DR   STRING; 33169.AAS52483; -.
DR   PRIDE; Q758G4; -.
DR   EnsemblFungi; AAS52483; AAS52483; AGOS_AEL202C.
DR   GeneID; 4620841; -.
DR   KEGG; ago:AGOS_AEL202C; -.
DR   eggNOG; ENOG502QWMT; Eukaryota.
DR   HOGENOM; CLU_026111_0_0_1; -.
DR   InParanoid; Q758G4; -.
DR   OMA; WEWCNKF; -.
DR   Proteomes; UP000000591; Chromosome V.
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:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR   GO; GO:0071469; P:cellular response to alkaline pH; IEA:EnsemblFungi.
DR   GO; GO:0071467; P:cellular response to pH; IBA:GO_Central.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:EnsemblFungi.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0070613; P:regulation of protein processing; IEA:EnsemblFungi.
DR   GO; GO:0044088; P:regulation of vacuole organization; IEA:EnsemblFungi.
DR   InterPro; IPR014844; PalH.
DR   PANTHER; PTHR35779; PTHR35779; 1.
DR   Pfam; PF08733; PalH; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..502
FT                   /note="pH-response regulator protein palH/RIM21"
FT                   /id="PRO_0000058195"
FT   TOPO_DOM        1..95
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        117..131
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..165
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..206
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        228..250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..283
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..313
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        332..502
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          379..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  55880 MW;  22353EF0B5C8924C CRC64;
     MVQRTRWRYS AIAHNYNSCR PMELGAGIAV GAWDGVWARA RSAEFVAATD MGDPVYSAFM
     RYDDSAPLHA AVAADWATYV AADFNGGPFK YSIFPILYSF TASLVVTMGL TVIVFFNVRT
     KPHRGVPKLL RVAAVLACGN LLTFVVRAMM QLGRDHAEGV VPMNHILDML WTDTAFNTVD
     ILAVLILQLC QVQTVMRFFT RFQEKRLISL CGILLAVLSQ VLWAIPPYSE AVSNHFMPLD
     DDKDMDVLPP FVYLVRIAQA GSYASFVLMH VFAKKKLCVQ SVQMFLLTVL TVVVVVLQPA
     FFITDVTNVW IDNLSEIFST TCYMGSTVIV WEWSNRLSIL EARRQAQSIL GRPVYEDEEQ
     GYNFARYALK IQTALTSKSD EGDTTSATTF AAPRSARFEG KGGPQSPVYV QEGEQQAVMA
     FNKRMGTRAL AHHVLDSIIY YTDKVVVKGL GNLSASLPSK TSSATSVRGR VRKRIGLEGA
     NDVFVYRTKD LVFDSDEDIP RT
 
 
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