YVC1_YEAST
ID YVC1_YEAST Reviewed; 675 AA.
AC Q12324; D6W2E9; Q08500; Q7LGN3;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Calcium channel YVC1;
DE AltName: Full=TRP homolog;
DE AltName: Full=Yeast vacuolar conductance protein 1;
GN Name=YVC1 {ECO:0000312|SGD:S000005613}; OrderedLocusNames=YOR087W;
GN ORFNames=YOR088W, YOR3151W;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND IDENTIFICATION OF FRAMESHIFT.
RC STRAIN=ATCC 201389 / BY4742;
RX PubMed=11427713; DOI=10.1073/pnas.141036198;
RA Palmer C.P., Zhou X.-L., Lin J., Loukin S.H., Kung C., Saimi Y.;
RT "A TRP homolog in Saccharomyces cerevisiae forms an intracellular Ca(2+)-
RT permeable channel in the yeast vacuolar membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7801-7805(2001).
RN [2] {ECO:0000312|EMBL:CAA64009.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAA99283.1}
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 [4]
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 [5] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11781332; DOI=10.1083/jcb.200111004;
RA Denis V., Cyert M.S.;
RT "Internal Ca(2+) release in yeast is triggered by hypertonic shock and
RT mediated by a TRP channel homologue.";
RL J. Cell Biol. 156:29-34(2002).
RN [6] {ECO:0000305}
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-636, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-636, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Required for release of calcium ions from the vacuole in
CC response to hyperosmotic shock. {ECO:0000269|PubMed:11427713,
CC ECO:0000269|PubMed:11781332}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11427713,
CC ECO:0000269|PubMed:11781332}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11427713, ECO:0000269|PubMed:11781332}.
CC -!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA64009.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA99282.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA99283.1; Type=Frameshift; Evidence={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; X94335; CAA64009.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z74995; CAA99282.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z74995; CAA99283.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z74997; CAA99286.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10865.1; -; Genomic_DNA.
DR PIR; S61648; S61648.
DR PIR; S66972; S66972.
DR RefSeq; NP_014730.2; NM_001183506.1.
DR PDB; 6WHG; EM; 3.10 A; A/B/C/D=1-675.
DR PDBsum; 6WHG; -.
DR AlphaFoldDB; Q12324; -.
DR SMR; Q12324; -.
DR BioGRID; 34486; 143.
DR DIP; DIP-4157N; -.
DR IntAct; Q12324; 2.
DR MINT; Q12324; -.
DR STRING; 4932.YOR087W; -.
DR TCDB; 1.A.4.4.1; the transient receptor potential ca(2+) channel (trp-cc) family.
DR iPTMnet; Q12324; -.
DR MaxQB; Q12324; -.
DR PaxDb; Q12324; -.
DR PRIDE; Q12324; -.
DR EnsemblFungi; YOR087W_mRNA; YOR087W; YOR087W.
DR GeneID; 854255; -.
DR KEGG; sce:YOR087W; -.
DR SGD; S000005613; YVC1.
DR VEuPathDB; FungiDB:YOR087W; -.
DR eggNOG; ENOG502QTER; Eukaryota.
DR GeneTree; ENSGT00940000169218; -.
DR HOGENOM; CLU_014123_0_0_1; -.
DR InParanoid; Q12324; -.
DR OMA; YQKCIKY; -.
DR BioCyc; YEAST:G3O-33622-MON; -.
DR Reactome; R-SCE-3295583; TRP channels.
DR PRO; PR:Q12324; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12324; protein.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR GO; GO:0005227; F:calcium activated cation channel activity; IDA:SGD.
DR GO; GO:0005262; F:calcium channel activity; IDA:SGD.
DR GO; GO:0005216; F:ion channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; IDA:SGD.
DR GO; GO:0005272; F:sodium channel activity; IDA:SGD.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IDA:SGD.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IMP:SGD.
DR GO; GO:0030003; P:cellular cation homeostasis; IDA:SGD.
DR InterPro; IPR024862; TRPV.
DR PANTHER; PTHR10582; PTHR10582; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium channel; Calcium transport; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..675
FT /note="Calcium channel YVC1"
FT /id="PRO_0000215376"
FT TOPO_DOM 1..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..295
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..376
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..436
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 636
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 32..49
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:6WHG"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 118..142
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:6WHG"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:6WHG"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 233..252
FT /evidence="ECO:0007829|PDB:6WHG"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:6WHG"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 268..290
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 298..321
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 360..400
FT /evidence="ECO:0007829|PDB:6WHG"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 407..416
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:6WHG"
FT TURN 424..430
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 434..447
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 450..467
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 469..483
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 518..551
FT /evidence="ECO:0007829|PDB:6WHG"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:6WHG"
FT HELIX 582..599
FT /evidence="ECO:0007829|PDB:6WHG"
SQ SEQUENCE 675 AA; 77953 MW; C8CE3B092A717306 CRC64;
MVSANGDLHL PISNEQCMPE NNGSLGFEAP TPRQILRVTL NLKYLIDKVV PIVYDPNDIV
CDHSEILSPK VVKLAYEACG GNPKDKANKR KYQSVIIFSL LKVCEWYSIL ATMEVHNAKL
YETRNLASQQ LCKLLIEREE TRDLQFLFMQ LLLRRYVINE NDEDQEPLNA LELATDMHCT
TVIGSSGFQR CLKWIWRGWI VQNGLDPTTF IKDDSLAEVS LISHFNPVRL KAPVYQNYLQ
MIFSFLFLGL YTLVVNGKDS ERVQSFDLLE SIFYVFNTGF ILDELTKLYY IGYAHLSFWN
LFNDTTYLII TFAMGFRAMS VTPLNAKYSS EDWDKISYRV LSCAAPFVWS RLLLYLESQR
FIGIMLVILK HMMKESIVFF FLLFLIMIGF TQGFLGLDSA DGKRDITGPI LGNLTITVLG
LGSFDVFEEF APPYAAILYY GYYFIVSVIL LNILIALYST AYQKVIDNAD DEYMALMSQK
TLRYIRAPDE DVYVSPLNLI EVFMTPIFRI LPPKRAKDLS YTVMTIVYSP FLLLISVKET
REARRIKYNR MKRLNDDANE YDTPWDLTDG YLDDDDGLFS DNRNSGMRAT QLKNSRSLKL
QRTAEQEDVH FKVPKKWYKN VKKCSPSFEQ YDNDDTEDDA GEDKDEVKEL TKKVENLTAV
ITDLLEKLDI KDKKE
