ID   PALA_ASHGO              Reviewed;         631 AA.
AC   Q756C5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=pH-response regulator protein palA/RIM20;
GN   Name=RIM20; OrderedLocusNames=AER342C;
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: Required for the proteolytic cleavage of the transcription
CC       factor RIM101 in response to alkaline ambient pH. May act as a scaffold
CC       protein that recruits the calpain-like protease RIM13 via VPS32 to its
CC       substrate RIM101 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RIM101 by binding to its two YPX[LI] motifs.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the palA/RIM20 family. {ECO:0000305}.
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DR   EMBL; AE016818; AAS53022.1; -; Genomic_DNA.
DR   RefSeq; NP_985198.1; NM_210552.1.
DR   AlphaFoldDB; Q756C5; -.
DR   SMR; Q756C5; -.
DR   STRING; 33169.AAS53022; -.
DR   PRIDE; Q756C5; -.
DR   EnsemblFungi; AAS53022; AAS53022; AGOS_AER342C.
DR   GeneID; 4621412; -.
DR   KEGG; ago:AGOS_AER342C; -.
DR   eggNOG; KOG2220; Eukaryota.
DR   HOGENOM; CLU_007181_3_1_1; -.
DR   InParanoid; Q756C5; -.
DR   OMA; SAKHIDD; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR   GO; GO:0071985; P:multivesicular body sorting pathway; IEA:InterPro.
DR   GO; GO:0016485; P:protein processing; IEA:EnsemblFungi.
DR   GO; GO:0009268; P:response to pH; IEA:EnsemblFungi.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:EnsemblFungi.
DR   Gene3D; 1.25.40.280; -; 1.
DR   InterPro; IPR025304; ALIX_V_dom.
DR   InterPro; IPR045251; BRO1-like.
DR   InterPro; IPR004328; BRO1_dom.
DR   InterPro; IPR038499; BRO1_sf.
DR   PANTHER; PTHR23030; PTHR23030; 1.
DR   Pfam; PF13949; ALIX_LYPXL_bnd; 1.
DR   Pfam; PF03097; BRO1; 1.
DR   SMART; SM01041; BRO1; 1.
DR   PROSITE; PS51180; BRO1; 1.
PE   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..631
FT                   /note="pH-response regulator protein palA/RIM20"
FT                   /id="PRO_0000218873"
FT   DOMAIN          3..368
FT                   /note="BRO1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
SQ   SEQUENCE   631 AA;  72157 MW;  3816930B5E27C523 CRC64;
     MSQLSAVPLK MTLQVDMQAQ LAAIIDSTFY QVSSVFIDDL AAVNDMRNRS LMEADASVSN
     LEALLEYCKT LFALIAKFPD RQIEFTWFET LGHKAYGKTS NLWKFELFNV IYNIGAVKSL
     LASSMGNDEL KEACRYLQES AGCFQYILSA MERELESVID EKTIRAVLNL MLAQAQECCW
     ARALRDAMKH SPIARLALQV SNFYEEAHRY ARISPVIRTK LVKYINEKSF YFAAVAHYRH
     ALHFEEKQQY GNAVRSLNEA QEKIKGAGWG PEVLPFEKEL NDTLNTLQRD NDLIYLQHIP
     SQCPVINPVS MVKPILIDLL STGTQKIHLF RNLLPIDVIE SSAAFNIRQD KYVEDYVKSP
     LVALNKLLHN SLPENEALPG MKHLTEEEFD IYAKTLAGLN EFSSQLGERL TVIKSLIDGA
     TTRLPAEANH HADQDNSKDI VEEYNKRIVT LQGYLRQGEE ITRETTQIFE TVDRDLLTTQ
     LQLAATNNPT MRKVEALTKE RYDYIAEVEK KSLQNRILPS LVSNYKETGS LDFEPIFQEH
     LKMFKKDIEY VQLGKKRNAE LIAELNAEEG EESGKIKRLS PRDIQIQDFK HSLHLLEQVK
     ENIEEGQVFY EDLKESIGVL HEDVTDFLNK S