Basic Information

NameCalcium channel YVC1 (TRP homolog) (Yeast vacuolar conductance protein 1)
Uniprot IDQ12324
Systematic gene nameYOR087W
Standard gene nameYVC1
Gene namesYVC1 YOR087W YOR088W YOR3151W
Description from SGDYOR087W YVC1 SGDID:S000005613, Chr XV from 487707-489734, Genome Release 64-3-1, Verified ORF, "Vacuolar cation channel; mediates release of Ca(2+) from the vacuole in response to hyperosmotic shock"
Protein length675
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

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

Legend

  • X Phoshorylation
  • X Glutathionylation

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


Use imported representation

Loading structure from server... It may take a while.

If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.

References

[3, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[13, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[13, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[17, Glut]Chandel, A., Das, K.K., Bachhawat, A.K. (2016). Glutathione depletion activates the yeast vacuolar transient receptor potential channel, Yvc1p, by reversible glutathionylation of specific cysteines. Mol Biol Cell 27: 3913-3925. (Publication) (All modifications)
[79, Glut]Chandel, A., Das, K.K., Bachhawat, A.K. (2016). Glutathione depletion activates the yeast vacuolar transient receptor potential channel, Yvc1p, by reversible glutathionylation of specific cysteines. Mol Biol Cell 27: 3913-3925. (Publication) (All modifications)
[191, Glut]Chandel, A., Das, K.K., Bachhawat, A.K. (2016). Glutathione depletion activates the yeast vacuolar transient receptor potential channel, Yvc1p, by reversible glutathionylation of specific cysteines. Mol Biol Cell 27: 3913-3925. (Publication) (All modifications)
[244, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[244, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[631, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[636, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[636, Phos]Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications)
[636, Phos]Studer RA, Rodriguez-Mias RA, Haas KM, et al (2016) Evolution of protein phosphorylation across 18 fungal species. Science 354:229–232. (Publication) (All modifications)
[636, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[636, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[636, Phos]Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications)
[636, Phos]Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[636, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)