ID   PALA_KLULA              Reviewed;         652 AA.
AC   Q6CU63;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=pH-response regulator protein palA/RIM20;
GN   Name=RIM20; OrderedLocusNames=KLLA0C07348g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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: 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; CR382123; CAH01377.1; -; Genomic_DNA.
DR   RefSeq; XP_452526.1; XM_452526.1.
DR   AlphaFoldDB; Q6CU63; -.
DR   SMR; Q6CU63; -.
DR   STRING; 28985.XP_452526.1; -.
DR   EnsemblFungi; CAH01377; CAH01377; KLLA0_C07348g.
DR   GeneID; 2892561; -.
DR   KEGG; kla:KLLA0_C07348g; -.
DR   eggNOG; KOG2220; Eukaryota.
DR   HOGENOM; CLU_007181_3_1_1; -.
DR   InParanoid; Q6CU63; -.
DR   OMA; SEWIHHM; -.
DR   Proteomes; UP000000598; Chromosome C.
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..652
FT                   /note="pH-response regulator protein palA/RIM20"
FT                   /id="PRO_0000218880"
FT   DOMAIN          3..369
FT                   /note="BRO1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
SQ   SEQUENCE   652 AA;  75582 MW;  4908C4DA934F02A2 CRC64;
     MNDIFAIPFK RALQINLKDA FTVVINNTFY QTAASVEADL TQLDKYRDVL FHLDVCQADL
     NMLKQYYMAL KAIAVKLPDD QVEFTWFNTL GLKSSGMTRN SLRFETFNVL YNIGAMYSSL
     AVEQRLESTE GLKESCRLFK LSAGCFKFIY EHEVSNNFKF FDEYTLNALV SMMLAQAQQM
     VWKKACFDDI ERHSILSRLA LQVALFYQTA SKNSNCSPYI RTDWVKSLTS KSHYFMAIAY
     YRSGLHQVQK QNYAQGICDF QYALTWINKL SLDDELTEWR GEVQALLESA ERDNDLIYLQ
     ASVQNPSKVK PVMMVQADLF DEIEKKDGNI FKNLLPIDVL ESCNAFNERV ETYVKEHISN
     PLESMNKLLI SNTPQYMDFK SYYISEQEWN SYSDSLQDLE QLRAYVAGEL KLSESILQKD
     IQENEQMIRE HGLLRWKIPS KDKKIESLLA DLTNIRNYIE NGMKVDTETA SLFKTLDHDL
     VTNVSQPPES SDPIMKEASL ILQGRKNHIL AAERKIIENR LLPKIVSYYK KTGSKDFEPV
     FQEHIRMFDG DLLQVQKEKA KNKEMLTKVT LSSPEQVQIS RNDPRTLYLE ELKHSSNVLS
     ELKENIISGK QFYQDLITAL ESKLKEIEDY VNERKLQRTE LNDTLLCDTN ES