MID1_YEAST
ID MID1_YEAST Reviewed; 548 AA.
AC P41821; D6W0Q2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Stretch-activated cation channel MID1;
DE AltName: Full=Mating pheromone-induced death protein 2;
DE Flags: Precursor;
GN Name=MID1; OrderedLocusNames=YNL291C; ORFNames=N0530;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RX PubMed=7526155; DOI=10.1128/mcb.14.12.8259-8271.1994;
RA Iida H., Nakamura H., Ono T., Okumura M.S., Anraku Y.;
RT "MID1, a novel Saccharomyces cerevisiae gene encoding a plasma membrane
RT protein, is required for Ca2+ influx and mating.";
RL Mol. Cell. Biol. 14:8259-8271(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8553702; DOI=10.1002/yea.320111311;
RA Maurer K.C.T., Urbanus J.H.M., Planta R.J.;
RT "Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV
RT carrying a ribosomal protein gene cluster, the genes encoding a plasma
RT membrane protein and a subunit of replication factor C, and a novel
RT putative serine/threonine protein kinase gene.";
RL Yeast 11:1303-1310(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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]
RP FUNCTION.
RX PubMed=10436155; DOI=10.1126/science.285.5429.882;
RA Kanzaki M., Nagasawa M., Kojima I., Sato C., Naruse K., Sokabe M., Iida H.;
RT "Molecular identification of a eukaryotic, stretch-activated nonselective
RT cation channel.";
RL Science 285:882-886(1999).
RN [6]
RP FUNCTION, INTERACTION WITH CCH1, 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 MUTAGENESIS OF CYS-417; CYS-431; CYS-434; CYS-491; CYS-498; CYS-506 AND
RP CYS-531.
RX PubMed=11796727; DOI=10.1074/jbc.m111603200;
RA Maruoka T., Nagasoe Y., Inoue S., Mori Y., Goto J., Ikeda M., Iida H.;
RT "Essential hydrophilic carboxyl-terminal regions including cysteine
RT residues of the yeast stretch-activated calcium-permeable channel Mid1.";
RL J. Biol. Chem. 277:11645-11652(2002).
RN [8]
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 [9]
RP MUTAGENESIS OF PHE-356.
RX PubMed=14697255; DOI=10.1016/j.bbrc.2003.11.166;
RA Tada T., Ohmori M., Iida H.;
RT "Phe356 in the yeast Ca2+ channel component Mid1 is a key residue for
RT viability after exposure to alpha-factor.";
RL Biochem. Biophys. Res. Commun. 313:752-757(2004).
RN [10]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=14729456; DOI=10.1016/j.yexcr.2003.09.020;
RA Yoshimura H., Tada T., Iida H.;
RT "Subcellular localization and oligomeric structure of the yeast putative
RT stretch-activated Ca2+ channel component Mid1.";
RL Exp. Cell Res. 293:185-195(2004).
RN [11]
RP DELETION MUTANTS, AND SUBCELLULAR LOCATION.
RX PubMed=16202999; DOI=10.1016/j.yexcr.2005.08.014;
RA Ozeki-Miyawaki C., Moriya Y., Tatsumi H., Iida H., Sokabe M.;
RT "Identification of functional domains of Mid1, a stretch-activated channel
RT component, necessary for localization to the plasma membrane and Ca2+
RT permeation.";
RL Exp. Cell Res. 311:84-95(2005).
RN [12]
RP FUNCTION.
RX PubMed=16223494; DOI=10.1016/j.febslet.2005.09.058;
RA Peiter E., Fischer M., Sidaway K., Roberts S.K., Sanders D.;
RT "The Saccharomyces cerevisiae Ca2+ channel Cch1pMid1p is essential for
RT tolerance to cold stress and iron toxicity.";
RL FEBS Lett. 579:5697-5703(2005).
CC -!- FUNCTION: Calcium-permeable, cation-selective stretch-activated channel
CC (SAC). Required for calcium influx and for vitality of MATa cells in a
CC late, pheromone-induced event of the mating process requiring calcium
CC induced signaling. Functions together with CCH1 to ensure that adequate
CC levels of Ca(2+) are supplied to PMR1 to sustain secretion and growth.
CC Required for growth in low-calcium environments. Together with CCH1,
CC essential for tolerance to iron stress, which leads to an increased
CC oxidative poise, and to cold stress. {ECO:0000269|PubMed:10436155,
CC ECO:0000269|PubMed:10958666, ECO:0000269|PubMed:16223494,
CC ECO:0000269|PubMed:7526155}.
CC -!- SUBUNIT: Interacts with CCH1 to form a Ca(2+) influx channel. Forms an
CC oligomer with a molecular mass of 200 kDa by disulfide bonds.
CC {ECO:0000269|PubMed:10958666, ECO:0000269|PubMed:14729456}.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Endoplasmic reticulum. Membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC Note=Trafficking to the plasma membrane is dependent on the N-
CC glycosylation and the transporter protein SEC12.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:7526155}.
CC -!- MISCELLANEOUS: Present with 3210 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Truncation mutant consisting of amino acids 1-360 is
CC fully functional. Truncation mutants consisting of amino acids 1-400
CC and 1-22 are partially functional. Truncation mutants consisting of
CC amino acids 1-455, 1-133, and a mutant in which amino acids 3-22 are
CC deleted, are not functional in Ca(2+) uptake.
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DR EMBL; D32133; BAA06859.1; -; Genomic_DNA.
DR EMBL; U23084; AAC49109.1; -; Genomic_DNA.
DR EMBL; Z71567; CAA96209.1; -; Genomic_DNA.
DR EMBL; Z71566; CAA96208.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10268.1; -; Genomic_DNA.
DR PIR; A56353; A56353.
DR RefSeq; NP_014108.1; NM_001183129.1.
DR AlphaFoldDB; P41821; -.
DR BioGRID; 35546; 131.
DR DIP; DIP-5621N; -.
DR IntAct; P41821; 2.
DR MINT; P41821; -.
DR STRING; 4932.YNL291C; -.
DR TCDB; 8.A.41.1.1; the stretch-activated calcium channel auxiliary protein, mid1 (mid1) family.
DR MaxQB; P41821; -.
DR PaxDb; P41821; -.
DR PRIDE; P41821; -.
DR EnsemblFungi; YNL291C_mRNA; YNL291C; YNL291C.
DR GeneID; 855425; -.
DR KEGG; sce:YNL291C; -.
DR SGD; S000005235; MID1.
DR VEuPathDB; FungiDB:YNL291C; -.
DR eggNOG; ENOG502QTEW; Eukaryota.
DR HOGENOM; CLU_018731_1_0_1; -.
DR InParanoid; P41821; -.
DR OMA; YEILPCI; -.
DR BioCyc; YEAST:G3O-33281-MON; -.
DR PRO; PR:P41821; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P41821; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005262; F:calcium channel activity; IMP:SGD.
DR GO; GO:0015275; F:stretch-activated, cation-selective, calcium channel activity; IDA: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 InterPro; IPR024338; Mid1/Ehs1.
DR Pfam; PF12929; Mid1; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..548
FT /note="Stretch-activated cation channel MID1"
FT /id="PRO_0000096483"
FT TOPO_DOM 21..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 356
FT /note="F->A: Significantly low viability and relatively
FT normal Ca(2+) accumulation."
FT /evidence="ECO:0000269|PubMed:14697255"
FT MUTAGEN 356
FT /note="F->H,Q,D,E,K,R: Substitution by hydrophilic amino
FT acids causes lethality and low Ca(2+) accumulation."
FT /evidence="ECO:0000269|PubMed:14697255"
FT MUTAGEN 356
FT /note="F->L,W,Y: Substitution by hydrophobic, large amino
FT acids does not cause lethality nor low Ca(2+)
FT accumulation."
FT /evidence="ECO:0000269|PubMed:14697255"
FT MUTAGEN 417
FT /note="C->A: Non-functional."
FT /evidence="ECO:0000269|PubMed:11796727"
FT MUTAGEN 431
FT /note="C->A: Non-functional."
FT /evidence="ECO:0000269|PubMed:11796727"
FT MUTAGEN 434
FT /note="C->A: Non-functional."
FT /evidence="ECO:0000269|PubMed:11796727"
FT MUTAGEN 491
FT /note="C->A: Functionally impaired."
FT /evidence="ECO:0000269|PubMed:11796727"
FT MUTAGEN 498
FT /note="C->A: Non-functional."
FT /evidence="ECO:0000269|PubMed:11796727"
FT MUTAGEN 506
FT /note="C->A: Functionally impaired."
FT /evidence="ECO:0000269|PubMed:11796727"
FT MUTAGEN 531
FT /note="C->A: Functionally impaired."
FT /evidence="ECO:0000269|PubMed:11796727"
SQ SEQUENCE 548 AA; 61575 MW; 5FCDE044C5F9ACB4 CRC64;
MIVWQALFVV YCLFTTSIHG LFQDFNPFAN KNISLKFPSL NRWEKNVMAT GQQTIINSDS
IYEWTPILSN ITAGKKDSFV FTIDAEASGY GFAPTYEVLM FISGNICQMP MNRSDVDLTI
YYSFNETVLE NPNIGQSAVF QDGYIQALAI SPVQSSSSNA TSTYSNLYVV AELVNSTTEQ
PLSSSDASEN WEYRLSISEN DLVFQWDVRP WVEVLDTDMN SALLSTGNVT ADAKVYHNYS
IYDPSLYDLY VYSYEDSVQL NQNYNLSLCA VKNGPYLVSS QNTSNATVTS NSTNPLERTD
LAIQKKITEY GGSVTEMFYV TGLNASTTYV AYLTKKISNG DGLSSVGGIL FSHVYFTTRS
TDVCSLIFGL DFCSDVAYSV PTSSFSVGNK TLMAQTYDHI AEALYANFSK ALQLISCDAD
KDARYSPVMT CDDCAEAYRD WVCAVSIPRC TTTSSQYYIH RDKSHNRNDY LNKFIKPLDD
YYEILPCIDM CYTLVRNCPS DFQFSCPNDL TTEDLLYQSY NFYMDTDYST CNYIGNSSLM
VIHPLDDT
