HPH1_YEAST
ID HPH1_YEAST Reviewed; 602 AA.
AC Q99332; D6W322;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein HPH1;
DE AltName: Full=Functionally related to TCP1 protein 1;
DE AltName: Full=High pH protein 1;
GN Name=FRT1; Synonyms=HPH1; OrderedLocusNames=YOR324C; ORFNames=O6159;
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=8896266;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1021::aid-yea981>3.0.co;2-7;
RA Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
RA Schweizer M.;
RT "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome
RT XV reveals regions of similarity to chromosomes I and XIII.";
RL Yeast 12:1021-1031(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 SUBCELLULAR LOCATION.
RX PubMed=12514182; DOI=10.1074/jbc.m212725200;
RA Beilharz T., Egan B., Silver P.A., Hofmann K., Lithgow T.;
RT "Bipartite signals mediate subcellular targeting of tail-anchored membrane
RT proteins in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:8219-8223(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, INTERACTION WITH CNA1; CMP2 AND HPH2, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RX PubMed=15189990; DOI=10.1128/ec.3.3.695-704.2004;
RA Heath V.L., Shaw S.L., Roy S., Cyert M.S.;
RT "Hph1p and Hph2p, novel components of calcineurin-mediated stress responses
RT in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 3:695-704(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, 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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND SER-342, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Calcineurin-dependent protein required for growth under high
CC NaCl, alkaline pH and cell wall stress. {ECO:0000269|PubMed:15189990}.
CC -!- SUBUNIT: Interacts with the 2 calcineurin A subunits CNA1 and CMP2, and
CC with HPH2/FRT2. {ECO:0000269|PubMed:15189990}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12514182, ECO:0000269|PubMed:15189990}; Single-pass
CC membrane protein {ECO:0000269|PubMed:12514182,
CC ECO:0000269|PubMed:15189990}. Note=Punctate foci at the endoplasmic
CC reticulum membrane. The distribution of FRT1 on the endoplasmic
CC reticulum membrane depends on CaCl2 and calcineurin activity.
CC -!- PTM: Phosphorylated. Is dephosphorylated by calcineurin.
CC {ECO:0000269|PubMed:15189990}.
CC -!- MISCELLANEOUS: Present with 251 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; X90565; CAA62181.1; -; Genomic_DNA.
DR EMBL; Z75232; CAA99644.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11088.1; -; Genomic_DNA.
DR PIR; S58336; S58336.
DR RefSeq; NP_014969.3; NM_001183744.3.
DR AlphaFoldDB; Q99332; -.
DR SMR; Q99332; -.
DR BioGRID; 34710; 100.
DR DIP; DIP-2719N; -.
DR ELM; Q99332; -.
DR IntAct; Q99332; 7.
DR MINT; Q99332; -.
DR STRING; 4932.YOR324C; -.
DR iPTMnet; Q99332; -.
DR MaxQB; Q99332; -.
DR PaxDb; Q99332; -.
DR PRIDE; Q99332; -.
DR EnsemblFungi; YOR324C_mRNA; YOR324C; YOR324C.
DR GeneID; 854503; -.
DR KEGG; sce:YOR324C; -.
DR SGD; S000005851; FRT1.
DR VEuPathDB; FungiDB:YOR324C; -.
DR eggNOG; ENOG502SD1S; Eukaryota.
DR GeneTree; ENSGT00940000176734; -.
DR HOGENOM; CLU_035740_0_0_1; -.
DR InParanoid; Q99332; -.
DR OMA; ERRMEVC; -.
DR BioCyc; YEAST:G3O-33802-MON; -.
DR PRO; PR:Q99332; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99332; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071469; P:cellular response to alkaline pH; IMP:SGD.
DR GO; GO:0071472; P:cellular response to salt stress; IMP:SGD.
DR InterPro; IPR025752; HPH_family.
DR Pfam; PF13694; Hph; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..602
FT /note="Protein HPH1"
FT /id="PRO_0000227934"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 31..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 602 AA; 67293 MW; 1F39BCD1DAD25AC4 CRC64;
MNLLIDRMEN PGSRNCTLLP PSFPRGFCKG RRASSGDAVK IKESGLQPQP QPEPLQAKTN
VAHFSKSSSR LPVIAVNDNP VVPRPSTEVN LGSLLQKERE KEKEEQPALH DRRHLYVTKN
RAHGVRQRSL EMTSLPVLGS TKTGKFSDFL FEDDIDNRVG RHSRSYSGAS SLDDPFRVSP
KTDFNSNRAR LSCLSKGRRG SMSVFQSCHT GLAFNQIQGS SSSQRRSSAG SFDYERKRLV
NQFLQPSLGN SDPFDTLRES VVFEPSSTAG GIKLGNMHSQ SQISVNSSPS TSLFYHDLDG
SAVNDSSSFL YSRSNVPAFL SSSAFSSTSS TSSDSEDVDR RSLNGVYPSL GYLTNQRKPR
NSSGSSTAPG TDTLGFKYLL NRQKSADSST RFKSVLKVNN NNGSAATPDS SSNSISKSNS
NLNDNIDELN YYQNHISTLL VKIENEMRRN LNDTIIKNEN NVQKTIQKYD LLSGELTLLL
DEMTTLRTTV INQFLVKLKS DFDEDDNKAF INELKISVEE SVAQLQGLER RMEVCQERLN
KQKSSLREMD SLIELKNVLN KSKNNTKSIY LYRYFIIDII AFLLMGGFIV YVKNLLTRFF
TR
