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PALH_KLULA
ID   PALH_KLULA              Reviewed;         519 AA.
AC   Q6CXK7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=pH-response regulator protein palH/RIM21;
GN   Name=RIM21; OrderedLocusNames=KLLA0A07469g;
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. {ECO:0000250}.
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; CR382121; CAH02920.1; -; Genomic_DNA.
DR   RefSeq; XP_451332.1; XM_451332.1.
DR   AlphaFoldDB; Q6CXK7; -.
DR   STRING; 28985.XP_451332.1; -.
DR   EnsemblFungi; CAH02920; CAH02920; KLLA0_A07469g.
DR   GeneID; 2896424; -.
DR   KEGG; kla:KLLA0_A07469g; -.
DR   eggNOG; ENOG502QWMT; Eukaryota.
DR   HOGENOM; CLU_026111_0_0_1; -.
DR   InParanoid; Q6CXK7; -.
DR   OMA; WEWCNKF; -.
DR   Proteomes; UP000000598; Chromosome A.
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:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR   GO; GO:0071469; P:cellular response to alkaline pH; IEA:EnsemblFungi.
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..519
FT                   /note="pH-response regulator protein palH/RIM21"
FT                   /id="PRO_0000058201"
FT   TOPO_DOM        1..96
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..126
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        148..176
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..209
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..243
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        265..279
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301..309
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        331..519
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   519 AA;  59667 MW;  DD3F3497A20A7243 CRC64;
     MTGRSRWRYH FPSEDYSSCQ GVQLDEGVLI WNKLPDKFAY IKSLVFTSNC QDGTPLYSSF
     VELEDECPYL PIVAFDWNSY INNDGYTGPF KYSIYSVIYS VTANFIITVF LTVIVFINVP
     TKPSRKASYI LKLGALLASL NLSIFVIRVW KNIAENYTYN GYVSSTSFLN LLWGDKVFAG
     IDLVVVFLLQ ISQVQIVMRF FDRMQEKRMV FYFGLFLILV TQILWVIPTL SPVPTKDSDS
     DIDILPPFVY LFRIALSTCY ASVICFHVLT KKSLCFRGRM IFLTLLTIFT VFLHPTFFIV
     DVSNLWIDDL SEIFNTTCYL ASTVIVLEWT NRIHTMERKI HAASVLGRPI YEDEEQNFHF
     AIYALRMQNA MKMHRDGHVH DHGHTCDSND NANVSLQNAN TNDSSSIITD NSSQRTSTFG
     TMATDQVTLH TQQGERNITQ FKRAETFWNK CHHVLESIVY YTDNVMVNAL AGSKTFDSFT
     NDAEKLLKTE RLRKTVGLDE PEDVYLYRKT TMSSDSVME
 
 
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