YVC1_CANAL
ID YVC1_CANAL Reviewed; 675 AA.
AC Q5A2J7; A0A1D8PI36;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Calcium channel YVC1 {ECO:0000305};
DE AltName: Full=Vacuolar transiant receptor potential (TPR) channel YVC1 {ECO:0000303|PubMed:25308698};
DE AltName: Full=Yeast vacuolar conductance protein 1 {ECO:0000250|UniProtKB:Q12324};
GN Name=YVC1; OrderedLocusNames=CAALFM_C207730WA;
GN ORFNames=CaO19.2209, CaO19.9754;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION, AND FUNCTION.
RX PubMed=21457451; DOI=10.1111/j.1567-1364.2011.00730.x;
RA Wang H., Liang Y., Zhang B., Zheng W., Xing L., Li M.;
RT "Alkaline stress triggers an immediate calcium fluctuation in Candida
RT albicans mediated by Rim101p and Crz1p transcription factors.";
RL FEMS Yeast Res. 11:430-439(2011).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=25308698; DOI=10.1016/j.freeradbiomed.2014.09.011;
RA Yu Q., Zhang B., Yang B., Chen J., Wang H., Jia C., Ding X., Xu N.,
RA Dong Y., Zhang B., Xing L., Li M.;
RT "Interaction between the vacuole, the mitochondria and oxidative stress
RT response is governed by the transient receptor potential channel in Candida
RT albicans.";
RL Free Radic. Biol. Med. 77:152-167(2014).
RN [6]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=24368068; DOI=10.1016/j.ijmm.2013.11.022;
RA Yu Q., Wang F., Zhao Q., Chen J., Zhang B., Ding X., Wang H., Yang B.,
RA Lu G., Zhang B., Li M.;
RT "A novel role of the vacuolar calcium channel Yvc1 in stress response,
RT morphogenesis and pathogenicity of Candida albicans.";
RL Int. J. Med. Microbiol. 304:339-350(2014).
CC -!- FUNCTION: Vacuolar calcium channel involved in the release of calcium
CC ions from the vacuole in response to hyperosmotic or alkaline stress.
CC Required for activation of CAP1-related transcription of oxidative
CC stress response (OSR) genes, but also for maintaining the stability of
CC both the mitochondria and the vacuole in a potassium- and calcium-
CC dependent manner. Contributes to pathogenicity. Plays a key role in
CC hyphal polarized growth and re-orientation to host-signals through its
CC contribution to the localization of the Spitzenkoerper to the hyphal
CC tips. {ECO:0000269|PubMed:21457451, ECO:0000269|PubMed:24368068,
CC ECO:0000269|PubMed:25308698}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:24368068};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is down-regulated in response to alkaline pH when
CC CRZ1 or RIM101 are deleted. {ECO:0000269|PubMed:21457451}.
CC -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to oxidative stress,
CC increased sensitivity to killing by macrophages, reduced ability to
CC invade epithelium cells, and attenuated virulence in a mouse model.
CC Shows defects in hyphal maintenance, hyphal growth and flocculation.
CC Prevents the localization of the Spitzenkoerper to hyphal tips.
CC Enhances mitochondrial depolarization and apoptosis.
CC {ECO:0000269|PubMed:24368068, ECO:0000269|PubMed:25308698}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC {ECO:0000305}.
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DR EMBL; CP017624; AOW27771.1; -; Genomic_DNA.
DR RefSeq; XP_716049.2; XM_710956.2.
DR AlphaFoldDB; Q5A2J7; -.
DR SMR; Q5A2J7; -.
DR STRING; 237561.Q5A2J7; -.
DR PRIDE; Q5A2J7; -.
DR GeneID; 3642303; -.
DR KEGG; cal:CAALFM_C207730WA; -.
DR CGD; CAL0000187018; YVC1.
DR VEuPathDB; FungiDB:C2_07730W_A; -.
DR eggNOG; ENOG502QTER; Eukaryota.
DR HOGENOM; CLU_014123_0_0_1; -.
DR InParanoid; Q5A2J7; -.
DR OrthoDB; 559278at2759; -.
DR PHI-base; PHI:3993; -.
DR PRO; PR:Q5A2J7; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IEA:EnsemblFungi.
DR GO; GO:0005227; F:calcium activated cation channel activity; IEA:EnsemblFungi.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005216; F:ion channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; IEA:EnsemblFungi.
DR GO; GO:0005272; F:sodium channel activity; IEA:EnsemblFungi.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:EnsemblFungi.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0030003; P:cellular cation homeostasis; IEA:EnsemblFungi.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR024862; TRPV.
DR PANTHER; PTHR10582; PTHR10582; 1.
DR Pfam; PF00520; Ion_trans; 1.
PE 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; Coiled coil; Ion channel;
KW Ion transport; Membrane; Reference proteome; Stress response;
KW Transmembrane; Transmembrane helix; Transport; Vacuole; Virulence.
FT CHAIN 1..675
FT /note="Calcium channel YVC1"
FT /id="PRO_0000431482"
FT TRANSMEM 244..264
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT COILED 644..675
FT /evidence="ECO:0000255"
SQ SEQUENCE 675 AA; 77357 MW; F38D821CF64ECC17 CRC64;
MSELDLEENN PLLPPSQIND ENYEGSIFGE DARFCPNSRQ VFRICSNLKL LIDKIIPICF
KEDEITSSNS AILSDPVIDL VYQAAGGKGD GKEGTSSYKY RGSLVFCLLK VCDWYWQQAE
FELSDNELYS LRALTAQTIA AIIIEREKRD KYLFLNMLCH RYTICVNGVD ATPVSALEMA
VDMHSTIVIG SSGYQRCIKW LWRGWIIQSS TDPHSYVLYK GAASQSFRTH FDPARIKTPL
YQNILEIFLS IIYLIIFTIV VNTHSTLTGD IDFFETVLYL FTVGYILDEF IKFYHVGWNY
LGFWNAFNDT MYCILTVAVC FRIASVNSHG ATRIKYDEIS FRVLACASPL MWSRLLLFLD
AYKFVGAMIV VLKTMMKESI LFFFLLFVVI VGFLQGFIGL DSSDGKNEAT QRILISLVKA
VIGGSSFEDM GNLVPPYASV LYYFYQFMLT VILMNILIAL YSTAYAAIVE NATDEYFALV
AHKTLRYIRA PDQNLYVPPF NLIELLITPI GWFVSTSTWK NINYYVMLVI YSPLLAYITS
DELSNARRIQ YNRFKGVPDD ANEIDTEWDL TDGYDEDSPG DGDDCWDRIR ERNSEITEEL
RIQREGERQD PEFMINTHQF SEKIDKIVKP VGQASKVGVN WQIYEVIEKI DKLTNLLEVV
VAENKELKKR LENKA
