CCH1_YEAST
ID CCH1_YEAST Reviewed; 2039 AA.
AC P50077; D6VV00;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Calcium-channel protein CCH1;
GN Name=CCH1; OrderedLocusNames=YGR217W; ORFNames=G8501;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1184-2039.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8701610;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 12:385-390(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1184-2039.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [5]
RP FUNCTION.
RX PubMed=9343395; DOI=10.1128/mcb.17.11.6339;
RA Paidhungat M., Garrett S.;
RT "A homolog of mammalian, voltage-gated calcium channels mediates yeast
RT pheromone-stimulated Ca2+ uptake and exacerbates the cdc1(Ts) growth
RT defect.";
RL Mol. Cell. Biol. 17:6339-6347(1997).
RN [6]
RP FUNCTION, INTERACTION WITH MID1, AND SUBCELLULAR LOCATION.
RX PubMed=10958666; DOI=10.1128/mcb.20.18.6686-6694.2000;
RA Locke E.G., Bonilla M., Liang L., Takita Y., Cunningham K.W.;
RT "A homolog of voltage-gated Ca(2+) channels stimulated by depletion of
RT secretory Ca(2+) in yeast.";
RL Mol. Cell. Biol. 20:6686-6694(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP 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).
RN [8]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Voltage-gated, high-affinity calcium channel involved in
CC calcium influx in response to some environmental stresses as well as
CC exposure to mating pheromones. Functions together with MID1 to ensure
CC that adequate levels of Ca(2+) are supplied to PMR1 to sustain
CC secretion and growth. Required for growth in low-calcium environments.
CC {ECO:0000269|PubMed:10958666, ECO:0000269|PubMed:9343395}.
CC -!- SUBUNIT: Interacts with MID1 to form a Ca(2+) influx channel.
CC {ECO:0000269|PubMed:10958666}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10958666}.
CC Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000305}.
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DR EMBL; Z73002; CAA97244.1; -; Genomic_DNA.
DR EMBL; Z73003; CAA97245.1; -; Genomic_DNA.
DR EMBL; X87941; CAA61165.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08311.1; -; Genomic_DNA.
DR PIR; S64540; S64540.
DR RefSeq; NP_011733.3; NM_001181346.3.
DR AlphaFoldDB; P50077; -.
DR BioGRID; 33470; 166.
DR IntAct; P50077; 14.
DR MINT; P50077; -.
DR STRING; 4932.YGR217W; -.
DR TCDB; 1.A.1.11.10; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; P50077; -.
DR MaxQB; P50077; -.
DR PaxDb; P50077; -.
DR PRIDE; P50077; -.
DR EnsemblFungi; YGR217W_mRNA; YGR217W; YGR217W.
DR GeneID; 853131; -.
DR KEGG; sce:YGR217W; -.
DR SGD; S000003449; CCH1.
DR VEuPathDB; FungiDB:YGR217W; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000170242; -.
DR HOGENOM; CLU_000443_2_0_1; -.
DR InParanoid; P50077; -.
DR OMA; TLFIAWN; -.
DR BioCyc; YEAST:G3O-30899-MON; -.
DR PRO; PR:P50077; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P50077; protein.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
DR GO; GO:0005262; F:calcium channel activity; IDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:SGD.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IDA:SGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 2.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF00520; Ion_trans; 4.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Stress response; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..2039
FT /note="Calcium-channel protein CCH1"
FT /id="PRO_0000054106"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 658..678
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 766..786
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 809..829
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 841..861
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 904..924
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 942..962
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1207..1227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1247..1267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1277..1297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1340..1360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1408..1428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1452..1472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1529..1549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1554..1574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1596..1616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1618..1638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1654..1674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1748..1768
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1787..1822
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2011..2039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CONFLICT 1185
FT /note="R -> Q (in Ref. 4; CAA61165)"
FT /evidence="ECO:0000305"
FT CONFLICT 1203
FT /note="I -> N (in Ref. 4; CAA61165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2039 AA; 234599 MW; 800B3825D6C6E527 CRC64;
MQGRKRTLTE PFEPNTNPFG DNAAVMTENV EDNSETDGNR LESKPQALVP PALNIVPPES
SIHSTEEKKG DEYNGNDKDS SLISNIFRTR VGRSSHENLS RPKLSLKTAS FGAAESSRRN
VSPSTKSAKS SSQYIDLNDE RLRRRSFSSY SRSSSRRVSN SPSSTDRPPR SAKVLSLIAA
DDMDDFEDLQ KGFKSAIDEE GLTWLPQLKS EKSRPVSDVG EDRGEGEQES IPDVHTPNVG
ASATPGSIHL TPEPAQNGSV SEGLEGSINN SRKKPSPKFF HHLSPQKEDK DQTEVIEYAE
DILDFETLQR KLESRPFVLY GHSLGVFSPT NPLRIKIARF LLHRRYSLLY NTLLTFYAIL
LAIRTYNPHN VVFLYRFSNW TDYFIFILSA CFTGNDIAKI IAFGFWDDSE MFKAYGREYK
SILQRSGIMK LYIYLREKYG RKLIDFIIPF RIISPGEETK YQRSSLSTSL TKPYGAKENQ
RPFGTPRAFA RSSWNRIDLV SSVSFWLGMF LSIKSYDTKT GIRIFKPLAI LRILRLVNVD
TGMPSILRGL KYGIPQLVNV SSMLVYFWIF FGILGVQIFQ GSFRRQCVWF NPEDPTDTYQ
YDMQFCGGYL DPVTKRKQNY IYEDGSEGSV SKGFLCPQYS KCVSNANPYN GRISFDNIVN
SMELVFVIMS ANTFTDLMYY TMDSDEMAAC LFFIVCIFVL TIWLLNLLIA VLVSSFEIAN
EEYKKKKFIY GSRKTGYVAR IVTGYWKYFK LKANQTKFPN WSQKGLAIYS HVEFIFVILI
ICDIGMRASV KVSTSANCNN ILLKTDRGIS IVLFIESLAR LVLYLPNMWK FLTKPSYVYD
FIISIITLVI SCLAVEGVLG HMYAWLSIFH ISRFYRVIIS FNLTKKLWKQ ILSNGVMIWN
LSSFYFFFTF LVAIIMAVYF EGVIPPEEMA DQPFGMYSLP NSFLSLFIIG STENWTDILY
ALQKHSPNIS STFFCSVFFI IWFLLSNSVI LNIFIALISE SMEVKEEEKR PQQIKHYLKF
VYPQKIQEYT HASLVARIRK KFFGGHRNED TRDFKQFLMR GTAIMNIAQN MGELADEFKE
PPSENLFKKG LSKLTIGVPS LKRLRMFANN PFYKNSDVVF TETNDINGRT YILELNEYED
EKLDYLKKYP LFNYSYYFFS PQHRFRRFCQ RLVPPSTGKR TDGSRFFEDS TDLYNKRSYF
HHIERDVFVF IFALATILLI VCSCYVTPLY RMHHKMGTWN WSSALDCAFI GAFSIEFIVK
TVADGFIYSP NAYLRNPWNF IDFCVLISMW INLIAYLKNN GNLSRIFKGL TALRALRCLT
ISNTARQTFN LVMFDGLNKI FEAGLISLSL LFPFTVWGLS IFKGRLGTCN DGSLGRADCY
NEYSNSVFQW DIMSPRVYQQ PYLHLDSFAS AFSSLYQIIS LEGWVDLLEN MMNSSGIGTP
ATVMGSAGNA LFLVLFNFLS MVFILNLFVS FIVNNQARTT GSAYFTIEEK AWLESQKLLS
QAKPKAIPNL IELSRVRQFF YQLAVEKKNF YYASFLQVVL YLHIIMLLSR SYNPGNLIGY
QGVYFMFSTS VFLIQEALHM CGEGPRLYFR QKWNSIRLSI IIIAFIMNAV AFHVPASHYW
FHNIKGFFLL VIFLFIIPQN DTLTELLETA MASLPPILSL TYTWGVLFLV YAIALNQIFG
LTRLGSNTTD NINFRTVIKS MIVLFRCSFG EGWNYIMADL TVSEPYCSSD DNSTYTDCGS
ETYAYLLLMS WNIISMYIFV NMFVSLIIGN FSYVYRSGGS RSGINRSEIK KYIEAWSKFD
TDGTGELELS YLPRIMHSFD GPLSFKIWEG RLTIKSLVEN YMEVNPDDPY DVKIDLIGLN
KELNTIDKAK IIQRKLQYRR FVQSIHYTNA YNGCIRFSDL LLQIPLYTAY SARECLGIDQ
YVHHLYILGK VDKYLENQRN FDVLEMVVTR WKFHCRMKRT IEPEWDVKDP TVSSHISNIN
VNLEPAPGIL EREPIATPRM DYGVNNFMWS PRMNQDSTME PPEEPIDNND DSANDLIDR
