Reviewed, UniProtKB/Swiss-Prot P41821 (MID1_YEAST)

Names and origin

Protein names

Recommended name:
    Stretch-activated cation channel MID1
Alternative name(s):
    Mating pheromone-induced death protein 2

Gene names

Name:	MID1
Ordered Locus Names:	YNL291C
ORF Names:	N0530

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Calcium-permeable, cation-selective stretch-activated channel (SAC). Required for calcium influx and for vitality of MATa cells in a late, pheromone-induced event of the mating process requiring calcium induced signaling. Functions together with CCH1 to ensure that adequate levels of Ca2+ are supplied to PMR1 to sustain secretion and growth. Required for growth in low-calcium environments. Together with CCH1, essential for tolerance to iron stress, which leads to an increased oxidative poise, and to cold stress. Ref.1 Ref.4 Ref.5 Ref.11
Subunit structure	Interacts with CCH1 to form a Ca2+ influx channel. Forms an oligomer with a molecular mass of 200 kDa by disulfide bonds. Ref.5 Ref.9
Subcellular location	Cell membrane. Endoplasmic reticulum. Membrane; Single-pass type I membrane protein Potential. Note: Trafficking to the plasma membrane is dependent on the N-glycosylation and the transporter protein SEC12.
Post-translational modification	N-glycosylated. Ref.1
Miscellaneous	Present with 3210 molecules/cell in log phase SD medium. Ref.7 Truncation mutant consisting of amino acids 1-360 is fully functional. Truncation mutants consisting of amino acids 1-400 and 1-22 are partially functional. Truncation mutants consisting of amino acids 1-455, 1-133, and a mutant in which amino acids 3-22 are deleted, are not functional in Ca2+ uptake.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Domain	Signal Transmembrane
Ligand	Calcium
Molecular function	Calcium channel Ionic channel
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	calcium ion transport Ref.5 Inferred from direct assay. Source: SGD
Cellular component	endoplasmic reticulum Ref.9 Inferred from direct assay. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Ref.5 Inferred from direct assay. Source: SGD
Molecular function	calcium channel activity Ref.5 Inferred from mutant phenotype. Source: SGD calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.5 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCH1	P50077	1	EBI-10894,EBI-4369

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 548	528	Stretch-activated cation channel MID1		PRO_0000096483
Regions
	Topological domain	21 – 341	321	Extracellular Potential
	Transmembrane	342 – 358	17	Potential
	Topological domain	359 – 548	190	Cytoplasmic Potential
	Compositional bias	431 – 450	20	Cys-rich
	Compositional bias	487 – 506	20	Cys-rich
Amino acid modifications
	Glycosylation	32	1	N-linked (GlcNAc...) Potential
	Glycosylation	70	1	N-linked (GlcNAc...) Potential
	Glycosylation	112	1	N-linked (GlcNAc...) Potential
	Glycosylation	125	1	N-linked (GlcNAc...) Potential
	Glycosylation	159	1	N-linked (GlcNAc...) Potential
	Glycosylation	175	1	N-linked (GlcNAc...) Potential
	Glycosylation	228	1	N-linked (GlcNAc...) Potential
	Glycosylation	238	1	N-linked (GlcNAc...) Potential
	Glycosylation	265	1	N-linked (GlcNAc...) Potential
	Glycosylation	282	1	N-linked (GlcNAc...) Potential
	Glycosylation	285	1	N-linked (GlcNAc...) Potential
	Glycosylation	291	1	N-linked (GlcNAc...) Potential
	Glycosylation	324	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	356	1	F → A: Significantly low viability and relatively normal Ca(2+) accumulation. Ref.8
	Mutagenesis	356	1	F → H, Q, D, E, K or R: Substitution by hydrophilic amino acids causes lethality and low Ca(2+) accumulation. Ref.8
	Mutagenesis	356	1	F → L, W or Y: Substitution by hydrophobic, large amino acids does not cause lethality nor low Ca(2+) accumulation. Ref.8
	Mutagenesis	417	1	C → A: Non-functional. Ref.6
	Mutagenesis	431	1	C → A: Non-functional. Ref.6
	Mutagenesis	434	1	C → A: Non-functional. Ref.6
	Mutagenesis	491	1	C → A: Functionally impaired. Ref.6
	Mutagenesis	498	1	C → A: Non-functional. Ref.6
	Mutagenesis	506	1	C → A: Functionally impaired. Ref.6
	Mutagenesis	531	1	C → A: Functionally impaired. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P41821-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 5FCDE044C5F9ACB4	FASTA	548	61,575
	10 20 30 40 50 60 MIVWQALFVV YCLFTTSIHG LFQDFNPFAN KNISLKFPSL NRWEKNVMAT GQQTIINSDS 70 80 90 100 110 120 IYEWTPILSN ITAGKKDSFV FTIDAEASGY GFAPTYEVLM FISGNICQMP MNRSDVDLTI 130 140 150 160 170 180 YYSFNETVLE NPNIGQSAVF QDGYIQALAI SPVQSSSSNA TSTYSNLYVV AELVNSTTEQ 190 200 210 220 230 240 PLSSSDASEN WEYRLSISEN DLVFQWDVRP WVEVLDTDMN SALLSTGNVT ADAKVYHNYS 250 260 270 280 290 300 IYDPSLYDLY VYSYEDSVQL NQNYNLSLCA VKNGPYLVSS QNTSNATVTS NSTNPLERTD 310 320 330 340 350 360 LAIQKKITEY GGSVTEMFYV TGLNASTTYV AYLTKKISNG DGLSSVGGIL FSHVYFTTRS 370 380 390 400 410 420 TDVCSLIFGL DFCSDVAYSV PTSSFSVGNK TLMAQTYDHI AEALYANFSK ALQLISCDAD 430 440 450 460 470 480 KDARYSPVMT CDDCAEAYRD WVCAVSIPRC TTTSSQYYIH RDKSHNRNDY LNKFIKPLDD 490 500 510 520 530 540 YYEILPCIDM CYTLVRNCPS DFQFSCPNDL TTEDLLYQSY NFYMDTDYST CNYIGNSSLM VIHPLDDT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MID1, a novel Saccharomyces cerevisiae gene encoding a plasma membrane protein, is required for Ca2+ influx and mating." Iida H., Nakamura H., Ono T., Okumura M.S., Anraku Y. Mol. Cell. Biol. 14:8259-8271(1994) [PubMed: 7526155] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION.
[2]	"Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV carrying a ribosomal protein gene cluster, the genes encoding a plasma membrane protein and a subunit of replication factor C, and a novel putative serine/threonine protein kinase gene." Maurer K.C.T., Urbanus J.H.M., Planta R.J. Yeast 11:1303-1310(1995) [PubMed: 8553702] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Molecular identification of a eukaryotic, stretch-activated nonselective cation channel." Kanzaki M., Nagasawa M., Kojima I., Sato C., Naruse K., Sokabe M., Iida H. Science 285:882-886(1999) [PubMed: 10436155] [Abstract] Cited for: FUNCTION.
[5]	"A homolog of voltage-gated Ca(2+) channels stimulated by depletion of secretory Ca(2+) in yeast." Locke E.G., Bonilla M., Liang L., Takita Y., Cunningham K.W. Mol. Cell. Biol. 20:6686-6694(2000) [PubMed: 10958666] [Abstract] Cited for: FUNCTION, INTERACTION WITH CCH1, SUBCELLULAR LOCATION.
[6]	"Essential hydrophilic carboxyl-terminal regions including cysteine residues of the yeast stretch-activated calcium-permeable channel Mid1." Maruoka T., Nagasoe Y., Inoue S., Mori Y., Goto J., Ikeda M., Iida H. J. Biol. Chem. 277:11645-11652(2002) [PubMed: 11796727] [Abstract] Cited for: MUTAGENESIS OF CYS-417; CYS-431; CYS-434; CYS-491; CYS-498; CYS-506 AND CYS-531.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"Phe356 in the yeast Ca2+ channel component Mid1 is a key residue for viability after exposure to alpha-factor." Tada T., Ohmori M., Iida H. Biochem. Biophys. Res. Commun. 313:752-757(2004) [PubMed: 14697255] [Abstract] Cited for: MUTAGENESIS OF PHE-356.
[9]	"Subcellular localization and oligomeric structure of the yeast putative stretch-activated Ca2+ channel component Mid1." Yoshimura H., Tada T., Iida H. Exp. Cell Res. 293:185-195(2004) [PubMed: 14729456] [Abstract] Cited for: SUBCELLULAR LOCATION, SUBUNIT.
[10]	"Identification of functional domains of Mid1, a stretch-activated channel component, necessary for localization to the plasma membrane and Ca2+ permeation." Ozeki-Miyawaki C., Moriya Y., Tatsumi H., Iida H., Sokabe M. Exp. Cell Res. 311:84-95(2005) [PubMed: 16202999] [Abstract] Cited for: DELETION MUTANTS, SUBCELLULAR LOCATION.
[11]	"The Saccharomyces cerevisiae Ca2+ channel Cch1pMid1p is essential for tolerance to cold stress and iron toxicity." Peiter E., Fischer M., Sidaway K., Roberts S.K., Sanders D. FEBS Lett. 579:5697-5703(2005) [PubMed: 16223494] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D32133 Genomic DNA. Translation: BAA06859.1. U23084 Genomic DNA. Translation: AAC49109.1. Z71567 Genomic DNA. Translation: CAA96209.1. Z71566 Genomic DNA. Translation: CAA96208.1.
PIR	A56353.
RefSeq	NP_014108.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5621N.
IntAct	P41821. 2 interactions.
STRING	P41821.
Protein family/group databases
TCDB	1.A.16.1.1. yeast stretch-activated, cation-selective, Ca2+ channel, Mid1 family.
Proteomic databases
PeptideAtlas	P41821.
Genome annotation databases
Ensembl	YNL291C; YNL291C; YNL291C; Saccharomyces cerevisiae. [Genome view]
GeneID	855425.
KEGG	sce:YNL291C.
NMPDR	fig|4932.3.peg.5170.
Organism-specific databases
CYGD	YNL291c.
SGD	S000005235. MID1.
Phylogenomic databases
HOGENOM	P41821.
OMA	YYEILPC
OrthoDB	EOG9KPVTG
Gene expression databases
ArrayExpress	P41821.
Genevestigator	P41821.
GermOnline	YNL291C. Saccharomyces cerevisiae.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	979292.

Entry information

Entry name

MID1_YEAST

Accession

Primary (citable) accession number: P41821

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 24, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)