PHM7_YEAST
ID PHM7_YEAST Reviewed; 991 AA.
AC Q12252; D6W1Y4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphate metabolism protein 7;
GN Name=PHM7; OrderedLocusNames=YOL084W; ORFNames=00953;
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=8533473; DOI=10.1002/yea.320111009;
RA Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
RT "A 29.425 kb segment on the left arm of yeast chromosome XV contains more
RT than twice as many unknown as known open reading frames.";
RL Yeast 11:975-986(1995).
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 INDUCTION.
RX PubMed=11102525; DOI=10.1091/mbc.11.12.4309;
RA Ogawa N., DeRisi J.L., Brown P.O.;
RT "New components of a system for phosphate accumulation and polyphosphate
RT metabolism in Saccharomyces cerevisiae revealed by genomic expression
RT analysis.";
RL Mol. Biol. Cell 11:4309-4321(2000).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
CC -!- FUNCTION: Acts as an osmosensitive calcium-permeable cation channel.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Regulated by phosphate levels.
CC {ECO:0000269|PubMed:11102525}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
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DR EMBL; X83121; CAA58195.1; -; Genomic_DNA.
DR EMBL; Z74826; CAA99096.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10700.1; -; Genomic_DNA.
DR PIR; S57385; S57385.
DR RefSeq; NP_014557.1; NM_001183338.1.
DR AlphaFoldDB; Q12252; -.
DR SMR; Q12252; -.
DR BioGRID; 34318; 91.
DR IntAct; Q12252; 1.
DR STRING; 4932.YOL084W; -.
DR TCDB; 1.A.17.5.6; the calcium-dependent chloride channel (ca-clc) family.
DR iPTMnet; Q12252; -.
DR PaxDb; Q12252; -.
DR PRIDE; Q12252; -.
DR EnsemblFungi; YOL084W_mRNA; YOL084W; YOL084W.
DR GeneID; 854070; -.
DR KEGG; sce:YOL084W; -.
DR SGD; S000005444; PHM7.
DR VEuPathDB; FungiDB:YOL084W; -.
DR eggNOG; KOG1134; Eukaryota.
DR HOGENOM; CLU_002458_2_1_1; -.
DR InParanoid; Q12252; -.
DR OMA; NWACVAL; -.
DR BioCyc; YEAST:G3O-33487-MON; -.
DR PRO; PR:Q12252; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12252; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
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:0005227; F:calcium activated cation channel activity; IBA:GO_Central.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR032880; Csc1_N.
DR InterPro; IPR027815; PHM7_cyt.
DR InterPro; IPR022257; PHM7_ext.
DR InterPro; IPR003864; RSN1_7TM.
DR PANTHER; PTHR13018; PTHR13018; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF12621; PHM7_ext; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..991
FT /note="Phosphate metabolism protein 7"
FT /id="PRO_0000262735"
FT TOPO_DOM 1..9
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..523
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..661
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 662..682
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 683..991
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 749..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 991 AA; 112546 MW; 491FAB0BD143DC5E CRC64;
MADSSSTSAF ISTLIIYGLT AVVFVWLFLL LRPKNRRVYE PRSLKDIQTI PEEERTEPVP
EGYFGWVEYL LSKPHSFLIQ HTSVDGYFLL RYIGIVGSLS FVGCLLLLPI LLPVNATNGN
NLQGFELLSF SNVTNKNRFY AHVFLSWIFF GLFTYVIYKE LYYYVVFRHA MQTTPLYDGL
LSSRTVIVTE LHKSIAQEGE MQMRFPKASN VAFAYDLSDL QELCKERAKN AAKYEAALNK
VLNKCVKMTR NKTQKQLDKL YNNGTKPKDD LETYVPHKKR PKHRLGKLPL CLGGKKVNTL
SYSSKRIGEL NEEIHEKQAD WASNDRQPAC FIQFETQLEA QRCYQSVEAI LGKKNFGKRL
IGYSPEDVNW GSMRLSSKER HSRRAVANTI MVLLIIFWAF PVAVVGIISN VNFLTDKVPF
LRFINNMPTF LMGVITGLLP TIALVVLMSL VPPFIVMLGK LSGCVTRQET DLYSQAWYYA
FAVIQIFLVV TATSSASSTV DSIIDRPRSA MTLLANNLPK ASNFYIMYFI LKGLTGPTWT
ILQAVNLLLS KVLGRVLDST PRQKWNRYNT LATPRMGIVY PGIEILVCIY ICYSIIAPIL
LFFSTVMLTL LYVAYLYNLN YVFGFSFDLK GRNYPRALFQ IFVGIYLSEV CLLGLFIMAK
TWGPLVLEVF WIVVTALAHI YMKRKFIPLF DAVPLSAIRH ARGEPGYSYP TSDLGLQEIK
DIADEMKGKY EQDNTHGILT PVTKDDLKKA NLIPDNDGSS ENGTPSNPFE SGSERASLSG
SNAESDSIKK LNDTVIKKSS TLSSSTKDNN ESTFVPEGEK FRKFHYSDVE ALRNKRPYDE
DDHSKHGPEG AVPVNADAGV IYSDPAAVMK EPQAFPPDVL ETNTWTRRIL QFFNPRRSYP
FDSVRMRFPL VFNTSIEYDE EYLSSAYTDP CVREKDPIVW CCKDPLGVSK QQIQEARSNG
LDVRDDFTRY DEKGKVIFTY NPPDYEPEAK K
