HPH2_YEAST
ID HPH2_YEAST Reviewed; 528 AA.
AC P39734; D6VPJ0; P39733;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein HPH2;
DE AltName: Full=Functionally related to TCP1 protein 2;
DE AltName: Full=High pH protein 2;
GN Name=FRT2; Synonyms=HPH2; OrderedLocusNames=YAL028W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [2]
RP SEQUENCE REVISION.
RA Vo D.T.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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 PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [5]
RP FUNCTION, INTERACTION WITH HPH1, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Required for growth under high NaCl, alkaline pH and cell
CC wall stress. {ECO:0000269|PubMed:15189990}.
CC -!- SUBUNIT: Interacts with HPH1/FRT1. {ECO:0000269|PubMed:15189990}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15189990}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15189990}. Note=Punctate foci at the endoplasmic
CC reticulum membrane.
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
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DR EMBL; U12980; AAC05004.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06960.1; -; Genomic_DNA.
DR PIR; S70295; S70295.
DR RefSeq; NP_009374.1; NM_001178173.1.
DR AlphaFoldDB; P39734; -.
DR SMR; P39734; -.
DR BioGRID; 31738; 92.
DR DIP; DIP-1309N; -.
DR IntAct; P39734; 5.
DR MINT; P39734; -.
DR STRING; 4932.YAL028W; -.
DR MaxQB; P39734; -.
DR PaxDb; P39734; -.
DR PRIDE; P39734; -.
DR EnsemblFungi; YAL028W_mRNA; YAL028W; YAL028W.
DR GeneID; 851205; -.
DR KEGG; sce:YAL028W; -.
DR SGD; S000000026; FRT2.
DR VEuPathDB; FungiDB:YAL028W; -.
DR eggNOG; ENOG502RZP4; Eukaryota.
DR GeneTree; ENSGT00940000176734; -.
DR HOGENOM; CLU_035740_0_0_1; -.
DR InParanoid; P39734; -.
DR OMA; MEHHHAR; -.
DR BioCyc; YEAST:G3O-28839-MON; -.
DR PRO; PR:P39734; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39734; 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..528
FT /note="Protein HPH2"
FT /id="PRO_0000202415"
FT TRANSMEM 505..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 58750 MW; E5A3CC7C6D60977A CRC64;
MQNAQIKSSS KGSGIDGTDR NSKDGVEKRP LEDVKQMIDA GTPDVGHKST VETKPNVGWQ
ASHSNLAALH EKEQKYEMEH HHARHKLHRQ VIPDYTSAST AMFSDCMFNA APDKVRSLST
MKSSGLSPKH PFNVVATFKG PFPQHSVESK PLDGGYSAKD HFPSFKMLQA QQHPAHRHYK
DNDKYGLKSP SRSFVKDKKR LVHRFLKSME PSSSGQSKDS SALAPAFDPI LPNVISKPSK
RPTHHSHSSD GSSSTQTDIS LQSLLYHDLE SSPKKHVSPS RPPSVASESS PAVANPIGLS
PKDACNASFS QSSSSSLSSS SSSSSSTSFS QSVAVDPLEP PGNITYSSSN LSLNSDELDY
YQRHIGLQLQ QTEALLKHSL KDEVLKDEND LVKNIANFDK IVKELRDLRS RTIGWKELVE
EDYLMNLKQD FDKENPESFE ARLSDTINTN VAKLQDLEKR MASCKDRLAS RKEVMRKMES
LLSLENSLMI SKKNVTFASK YRNEALDIVF LIIIIVICYT FKHLVSHK
