Stretch-activated cation channel MID1

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• calcium channel activity Source: SGD

  <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

  • 12492866
  • 9343395

• stretch-activated, cation-selective, calcium channel activity Source: SGD

  <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

  • 10436155

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

• calcium ion transport Source: SGD

  <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

  • 10958666

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Molecular functionⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Biological processⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Ligandⁱ

Enzyme and pathway databases

Protein family/group databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Topology

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	21 – 341	321	ExtracellularSequence analysis			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	342 – 358	17	HelicalSequence analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	359 – 548	190	CytoplasmicSequence analysis			Add BLAST

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

• endoplasmic reticulum Source: SGD

  <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

  • 14729456

• integral component of membrane Source: UniProtKB-KW
• plasma membrane Source: SGD

  <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

  • 10958666

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componentⁱ

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	356 – 356	1	F → A: Significantly low viability and relatively normal Ca(2+) accumulation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.9 "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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF PHE-356.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	356 – 356	1	F → H, Q, D, E, K or R: Substitution by hydrophilic amino acids causes lethality and low Ca(2+) accumulation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.9 "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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF PHE-356.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	356 – 356	1	F → L, W or Y: Substitution by hydrophobic, large amino acids does not cause lethality nor low Ca(2+) accumulation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.9 "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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF PHE-356.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	417 – 417	1	C → A: Non-functional. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.7 "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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-417; CYS-431; CYS-434; CYS-491; CYS-498; CYS-506 AND CYS-531.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	431 – 431	1	C → A: Non-functional. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.7 "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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-417; CYS-431; CYS-434; CYS-491; CYS-498; CYS-506 AND CYS-531.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	434 – 434	1	C → A: Non-functional. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.7 "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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-417; CYS-431; CYS-434; CYS-491; CYS-498; CYS-506 AND CYS-531.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	491 – 491	1	C → A: Functionally impaired. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.7 "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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-417; CYS-431; CYS-434; CYS-491; CYS-498; CYS-506 AND CYS-531.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	498 – 498	1	C → A: Non-functional. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.7 "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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-417; CYS-431; CYS-434; CYS-491; CYS-498; CYS-506 AND CYS-531.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	506 – 506	1	C → A: Functionally impaired. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.7 "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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-417; CYS-431; CYS-434; CYS-491; CYS-498; CYS-506 AND CYS-531.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	531 – 531	1	C → A: Functionally impaired. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.7 "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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-417; CYS-431; CYS-434; CYS-491; CYS-498; CYS-506 AND CYS-531.

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Denotes the presence of an N-terminal signal peptide.</p><p><a href='../manual/signal' target='_top'>More...</a></p>Signal peptidei	1 – 20	20	Sequence analysis			Add BLAST
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	21 – 548	528	Stretch-activated cation channel MID1		PRO_0000096483	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	32 – 32	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	70 – 70	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	112 – 112	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	125 – 125	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	159 – 159	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	175 – 175	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	228 – 228	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	238 – 238	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	265 – 265	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	282 – 282	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	285 – 285	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	291 – 291	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	324 – 324	1	N-linked (GlcNAc...)Sequence analysis

<p>Describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.</p><p><a href='../manual/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMⁱ

Proteomic databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>Provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="/help/function_section">‘Function’</a> section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Compositional bias

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.</p><p><a href='../manual/compbias' target='_top'>More...</a></p>Compositional biasi	431 – 450	20	Cys-rich			Add BLAST
<p>Describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.</p><p><a href='../manual/compbias' target='_top'>More...</a></p>Compositional biasi	487 – 506	20	Cys-rich			Add BLAST

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the <a href="/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>Indicates if the <a href="/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.</p><p><a href='../manual/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

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

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
   Strain: ATCC 204508 / S288c.
   
4. "The reference genome sequence of Saccharomyces cerevisiae: Then and now."
   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
   G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
   Cited for: GENOME REANNOTATION.
   Strain: ATCC 204508 / S288c.
   
5. "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] [Europe PMC] [Abstract]
   Cited for: FUNCTION.
6. "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] [Europe PMC] [Abstract]
   Cited for: FUNCTION, INTERACTION WITH CCH1, SUBCELLULAR LOCATION.
7. "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] [Europe PMC] [Abstract]
   Cited for: MUTAGENESIS OF CYS-417; CYS-431; CYS-434; CYS-491; CYS-498; CYS-506 AND CYS-531.
8. "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] [Europe PMC] [Abstract]
   Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
9. "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] [Europe PMC] [Abstract]
   Cited for: MUTAGENESIS OF PHE-356.
10. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.
11. "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] [Europe PMC] [Abstract]
    Cited for: DELETION MUTANTS, SUBCELLULAR LOCATION.
12. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

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<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termⁱ

Documents

1. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
2. Yeast chromosome XIV
   Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ