PALH_YARLI
ID PALH_YARLI Reviewed; 632 AA.
AC Q9UVF6; Q6C1Y3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=pH-response regulator protein palH/RIM21;
GN Name=RIM21; Synonyms=PAL2; OrderedLocusNames=YALI0F12397g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX PubMed=10821185; DOI=10.1007/s004380051195;
RA Treton B., Blanchin-Roland S., Lambert M., Lepingle A., Gaillardin C.;
RT "Ambient pH signalling in ascomycetous yeasts involves homologues of the
RT Aspergillus nidulans genes palF and palH.";
RL Mol. Gen. Genet. 263:505-513(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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.
CC {ECO:0000269|PubMed:10821185}.
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; AJ133771; CAB59339.1; -; Genomic_DNA.
DR EMBL; CR382132; CAG78136.1; -; Genomic_DNA.
DR RefSeq; XP_505329.1; XM_505329.1.
DR AlphaFoldDB; Q9UVF6; -.
DR STRING; 4952.CAG78136; -.
DR EnsemblFungi; CAG78136; CAG78136; YALI0_F12397g.
DR GeneID; 2908960; -.
DR KEGG; yli:YALI0F12397g; -.
DR VEuPathDB; FungiDB:YALI0_F12397g; -.
DR HOGENOM; CLU_432938_0_0_1; -.
DR InParanoid; Q9UVF6; -.
DR Proteomes; UP000001300; Chromosome F.
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:0071467; P:cellular response to pH; IBA:GO_Central.
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..632
FT /note="pH-response regulator protein palH/RIM21"
FT /id="PRO_0000058204"
FT TOPO_DOM 1..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..330
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..632
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 380..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 248
FT /note="L -> F (in Ref. 1; CAB59339)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="H -> N (in Ref. 1; CAB59339)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 69998 MW; 0AACB03A7C3FC68E CRC64;
MHSDAPTPVA NELSEVSHLA EGDNASFSAG NFTVLQLPSD PSHCIDYAIP AGTLVIVDPN
NPDNNRTVKL QAPAVFRPQC ALGGTRAPAP RPEESFPDWS EYQKYHHNDR RDPFYGSVTP
IAYTIAASTV TAWMLLIILF LSRKPSPLFQ KIAVLITAVS LTVFLAQATD TLESQYNEGY
QNAYELRHKI MGGWAFRILQ VITCVITWLA RLQVVIRLFD VPKINTRLAV VGSTLIFTNA
TIWACLNLIP PWSQYVRNAK SVLPVFGALC SLLLEVFYLV VVVIYSISKR KYAYSRTSIV
MAAISWLAMI LPMVFIVFDI AHYWIAGWSD FIRWTADAAA SVVVWEWTNV IVYQERREQR
QSVLGRQVYR DEILDFKGDN GGGTVGGGRT KYPSRMEEDD VPFRSSPNDH HFTSNIPTSA
GEGQSFQFFK RARLPMYSRK IWKIARGESA ASNNTHYEHA IIEEEEEESI ERNRRTPTVQ
ENGEEDDEET YDEENDQYSQ DNHSSVHSFE SSRPSQHPVP SSGGTRAVGH THFPLPGQSE
GAHTTSPAAA AAAAEPEPEP VAGPSGGAAA HGDSDDDSDN SDDSSLASFT VIQQTGFSVD
NQGVPEYDAD SAPPTFEPIP GFHRQDYSDA KG
