位置:首页 > 蛋白库 > PALH_YEAST
PALH_YEAST
ID   PALH_YEAST              Reviewed;         533 AA.
AC   P48565; D6W0P9;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=pH-response regulator protein palH/RIM21;
DE   AltName: Full=Regulator of IME2 protein 21;
GN   Name=RIM21; Synonyms=PAL2; OrderedLocusNames=YNL294C; ORFNames=N0466;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8553702; DOI=10.1002/yea.320111311;
RA   Maurer K.C.T., Urbanus J.H.M., Planta R.J.;
RT   "Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV
RT   carrying a ribosomal protein gene cluster, the genes encoding a plasma
RT   membrane protein and a subunit of replication factor C, and a novel
RT   putative serine/threonine protein kinase gene.";
RL   Yeast 11:1303-1310(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
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   [5]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Required for the proteolytic cleavage of the transcription
CC       factor RIM101 in response to alkaline ambient pH (By similarity).
CC       Required for growth at alkaline pH. {ECO:0000250,
CC       ECO:0000269|PubMed:10821185}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the palH/RIM21 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U23084; AAC49105.1; -; Genomic_DNA.
DR   EMBL; Z71570; CAA96212.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10265.1; -; Genomic_DNA.
DR   PIR; S63270; S63270.
DR   RefSeq; NP_014105.1; NM_001183132.1.
DR   AlphaFoldDB; P48565; -.
DR   BioGRID; 35543; 398.
DR   MINT; P48565; -.
DR   STRING; 4932.YNL294C; -.
DR   TCDB; 9.B.213.1.1; the 7 tms ph sensor rim21/palh (rim21/palh) family.
DR   iPTMnet; P48565; -.
DR   PaxDb; P48565; -.
DR   PRIDE; P48565; -.
DR   EnsemblFungi; YNL294C_mRNA; YNL294C; YNL294C.
DR   GeneID; 855422; -.
DR   KEGG; sce:YNL294C; -.
DR   SGD; S000005238; RIM21.
DR   VEuPathDB; FungiDB:YNL294C; -.
DR   eggNOG; ENOG502QWMT; Eukaryota.
DR   HOGENOM; CLU_026111_0_0_1; -.
DR   InParanoid; P48565; -.
DR   OMA; WEWCNKF; -.
DR   BioCyc; YEAST:G3O-33283-MON; -.
DR   PRO; PR:P48565; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P48565; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR   GO; GO:0071469; P:cellular response to alkaline pH; IMP:SGD.
DR   GO; GO:0071467; P:cellular response to pH; IBA:GO_Central.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:SGD.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IMP:SGD.
DR   GO; GO:0070613; P:regulation of protein processing; IMP:SGD.
DR   GO; GO:0044088; P:regulation of vacuole organization; IGI:SGD.
DR   InterPro; IPR014844; PalH.
DR   PANTHER; PTHR35779; PTHR35779; 1.
DR   Pfam; PF08733; PalH; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..533
FT                   /note="pH-response regulator protein palH/RIM21"
FT                   /id="PRO_0000058205"
FT   TOPO_DOM        1..94
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..127
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..178
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..209
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..247
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        269..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..533
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          452..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..514
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   533 AA;  61532 MW;  9492A18512F399CC CRC64;
     MNLWRHSPEE LAAYNSCHPM KLGSGVLIQL PLYDNSAVYA EDITFRSFCC ERVPVYVSTV
     LRNSSPYRYL DEVINDWQKF IQVSDYVGGS AEYAIYAVIL SITSNFVITV FLTVICCINI
     SGRAYKRILQ LLRIASLLAS LNLTIFITKV LRRLEKEHNV YGVVRAHSIM HIFSDDMTFV
     VLDFLATLMF QFCQVGIVIR LFQRAQEKRI IFFIGVILTI TANILWVIPP FANHTTKHRN
     DWQILRPFVY LFRIAIATSY ASIVIYHIWQ KKKLWFKFNQ MGLLTLLTIL VVLLLPGFFL
     ADVSNLWISE LGEVFNTTCY VTSTVITWEW LDRLNVLERK EEAQSILGRP IFEEEQQDYR
     FAKYALRVQN ALTRRESQDA STDRHDTSSN SEVCDLQTIS RYDPEDQISV GRSIDRMHFN
     DRGTYKDVAL KKLGYARDKI LYFTDQIVQK SVGHNNSSSS KNEKTKQRKA MVRKRLGLDK
     PGIYIYSTKD VVFNSDEDDD ENAEDEDDDE YEVGSEGNNN SSATFTSDHI GHI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024