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Calcium channel YVC1 (TRP homolog) (Yeast vacuolar conductance protein 1)

 YVC1_YEAST              Reviewed;         675 AA.
Q12324; D6W2E9; Q08500; Q7LGN3;
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 2.
20-JUN-2018, entry version 142.
RecName: Full=Calcium channel YVC1;
AltName: Full=TRP homolog;
AltName: Full=Yeast vacuolar conductance protein 1;
Name=YVC1 {ECO:0000312|SGD:S000005613}; OrderedLocusNames=YOR087W;
ORFNames=YOR088W, YOR3151W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
TOPOLOGY, AND IDENTIFICATION OF FRAMESHIFT.
STRAIN=ATCC 201389 / BY4742;
PubMed=11427713; DOI=10.1073/pnas.141036198;
Palmer C.P., Zhou X.-L., Lin J., Loukin S.H., Kung C., Saimi Y.;
"A TRP homolog in Saccharomyces cerevisiae forms an intracellular
Ca(2+)-permeable channel in the yeast vacuolar membrane.";
Proc. Natl. Acad. Sci. U.S.A. 98:7801-7805(2001).
[2] {ECO:0000312|EMBL:CAA64009.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9200815;
DOI=10.1002/(SICI)1097-0061(19970615)13:7<655::AID-YEA120>3.0.CO;2-I;
Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
Schwager C., Paces V., Sander C., Ansorge W.;
"DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
Yeast 13:655-672(1997).
[3] {ECO:0000305, ECO:0000312|EMBL:CAA99283.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11781332; DOI=10.1083/jcb.200111004;
Denis V., Cyert M.S.;
"Internal Ca(2+) release in yeast is triggered by hypertonic shock and
mediated by a TRP channel homologue.";
J. Cell Biol. 156:29-34(2002).
[6] {ECO:0000305}
IDENTIFICATION OF FRAMESHIFT.
PubMed=12748633; DOI=10.1038/nature01644;
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
"Sequencing and comparison of yeast species to identify genes and
regulatory elements.";
Nature 423:241-254(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-636, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-636, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Required for release of calcium ions from the vacuole in
response to hyperosmotic shock. {ECO:0000269|PubMed:11427713,
ECO:0000269|PubMed:11781332}.
-!- SUBCELLULAR LOCATION: Vacuole membrane
{ECO:0000269|PubMed:11427713, ECO:0000269|PubMed:11781332}; Multi-
pass membrane protein {ECO:0000269|PubMed:11427713,
ECO:0000269|PubMed:11781332}.
-!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA64009.1; Type=Frameshift; Positions=245; Evidence={ECO:0000305};
Sequence=CAA99282.1; Type=Frameshift; Positions=245; Evidence={ECO:0000305};
Sequence=CAA99283.1; Type=Frameshift; Positions=245; Evidence={ECO:0000305};
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EMBL; X94335; CAA64009.1; ALT_FRAME; Genomic_DNA.
EMBL; Z74995; CAA99282.1; ALT_FRAME; Genomic_DNA.
EMBL; Z74995; CAA99283.1; ALT_FRAME; Genomic_DNA.
EMBL; Z74997; CAA99286.1; -; Genomic_DNA.
EMBL; BK006948; DAA10865.1; -; Genomic_DNA.
PIR; S61648; S61648.
PIR; S66972; S66972.
RefSeq; NP_014730.2; NM_001183506.1.
ProteinModelPortal; Q12324; -.
BioGrid; 34486; 138.
DIP; DIP-4157N; -.
IntAct; Q12324; 2.
MINT; Q12324; -.
STRING; 4932.YOR087W; -.
TCDB; 1.A.4.4.1; the transient receptor potential ca(2+) channel (trp-cc) family.
iPTMnet; Q12324; -.
MaxQB; Q12324; -.
PaxDb; Q12324; -.
PRIDE; Q12324; -.
EnsemblFungi; YOR087W; YOR087W; YOR087W.
GeneID; 854255; -.
KEGG; sce:YOR087W; -.
EuPathDB; FungiDB:YOR087W; -.
SGD; S000005613; YVC1.
HOGENOM; HOG000199455; -.
InParanoid; Q12324; -.
OMA; RATACEV; -.
OrthoDB; EOG092C1F4Q; -.
BioCyc; YEAST:G3O-33622-MONOMER; -.
PRO; PR:Q12324; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
GO; GO:0005227; F:calcium activated cation channel activity; IDA:SGD.
GO; GO:0005262; F:calcium channel activity; IDA:SGD.
GO; GO:0005267; F:potassium channel activity; IDA:SGD.
GO; GO:0005272; F:sodium channel activity; IDA:SGD.
GO; GO:0005244; F:voltage-gated ion channel activity; IDA:SGD.
GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IMP:SGD.
GO; GO:0030003; P:cellular cation homeostasis; IDA:SGD.
InterPro; IPR024862; TRPV.
PANTHER; PTHR10582; PTHR10582; 1.
1: Evidence at protein level;
Calcium; Calcium channel; Calcium transport; Complete proteome;
Ion channel; Ion transport; Membrane; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport;
Vacuole.
CHAIN 1 675 Calcium channel YVC1.
/FTId=PRO_0000215376.
TOPO_DOM 1 236 Cytoplasmic. {ECO:0000255}.
TRANSMEM 237 257 Helical. {ECO:0000255}.
TOPO_DOM 258 295 Vacuolar. {ECO:0000255}.
TRANSMEM 296 316 Helical. {ECO:0000255}.
TOPO_DOM 317 335 Cytoplasmic. {ECO:0000255}.
TRANSMEM 336 355 Helical. {ECO:0000255}.
TOPO_DOM 356 376 Vacuolar. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TOPO_DOM 398 405 Cytoplasmic. {ECO:0000255}.
TRANSMEM 406 426 Helical. {ECO:0000255}.
TOPO_DOM 427 436 Vacuolar. {ECO:0000255}.
TRANSMEM 437 457 Helical. {ECO:0000255}.
TOPO_DOM 458 675 Cytoplasmic. {ECO:0000255}.
COMPBIAS 573 576 Poly-Asp. {ECO:0000255}.
MOD_RES 636 636 Phosphothreonine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
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


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