2025-04-02 18:15:21, GGRNA.v2 : RefSeq release 228 (Jan, 2025)
LOCUS NM_001183342 834 bp mRNA linear PLN 17-DEC-2024 DEFINITION Saccharomyces cerevisiae S288C protein disulfide isomerase MPD2 (MPD2), partial mRNA. ACCESSION NM_001183342 VERSION NM_001183342.1 DBLINK BioProject: PRJNA128 KEYWORDS RefSeq. SOURCE Saccharomyces cerevisiae S288C ORGANISM Saccharomyces cerevisiae S288C Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. REFERENCE 1 (bases 1 to 834) AUTHORS Engel,S.R., Wong,E.D., Nash,R.S., Aleksander,S., Alexander,M., Douglass,E., Karra,K., Miyasato,S.R., Simison,M., Skrzypek,M.S., Weng,S. and Cherry,J.M. TITLE New data and collaborations at the Saccharomyces Genome Database: updated reference genome, alleles, and the Alliance of Genome Resources JOURNAL Genetics 220 (4) (2022) PUBMED 34897464 REFERENCE 2 (bases 1 to 834) AUTHORS Dujon,B., Albermann,K., Aldea,M., Alexandraki,D., Ansorge,W., Arino,J., Benes,V., Bohn,C., Bolotin-Fukuhara,M., Bordonne,R., Boyer,J., Camasses,A., Casamayor,A., Casas,C., Cheret,G., Cziepluch,C., Daignan-Fornier,B., Dang,D.V., de Haan,M., Delius,H., Durand,P., Fairhead,C., Feldmann,H., Gaillon,L., Kleine,K. et al. TITLE The nucleotide sequence of Saccharomyces cerevisiae chromosome XV JOURNAL Nature 387 (6632 SUPPL), 98-102 (1997) PUBMED 9169874 REFERENCE 3 (bases 1 to 834) AUTHORS Goffeau,A., Barrell,B.G., Bussey,H., Davis,R.W., Dujon,B., Feldmann,H., Galibert,F., Hoheisel,J.D., Jacq,C., Johnston,M., Louis,E.J., Mewes,H.W., Murakami,Y., Philippsen,P., Tettelin,H. and Oliver,S.G. TITLE Life with 6000 genes JOURNAL Science 274 (5287), 546 (1996) PUBMED 8849441 REFERENCE 4 (bases 1 to 834) CONSRTM NCBI Genome Project TITLE Direct Submission JOURNAL Submitted (17-DEC-2024) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA REFERENCE 5 (bases 1 to 834) CONSRTM Saccharomyces Genome Database TITLE Direct Submission JOURNAL Submitted (16-JAN-2015) Department of Genetics, Stanford University, Stanford, CA 94305-5120, USA REMARK Protein update by submitter REFERENCE 6 (bases 1 to 834) CONSRTM Saccharomyces Genome Database TITLE Direct Submission JOURNAL Submitted (04-MAY-2012) Department of Genetics, Stanford University, Stanford, CA 94305-5120, USA REMARK Protein update by submitter REFERENCE 7 (bases 1 to 834) CONSRTM Saccharomyces Genome Database TITLE Direct Submission JOURNAL Submitted (31-MAR-2011) Department of Genetics, Stanford University, Stanford, CA 94305-5120, USA REMARK Sequence update by submitter REFERENCE 8 (bases 1 to 834) CONSRTM Saccharomyces Genome Database TITLE Direct Submission JOURNAL Submitted (27-MAY-2010) Department of Genetics, Stanford University, Stanford, CA 94305-5120, USA REMARK Protein update by submitter REFERENCE 9 (bases 1 to 834) CONSRTM Saccharomyces Genome Database TITLE Direct Submission JOURNAL Submitted (14-DEC-2009) Department of Genetics, Stanford University, Stanford, CA 94305-5120, USA COMMENT REVIEWED REFSEQ: This record has been curated by SGD. This record is derived from an annotated genomic sequence (NC_001147). ##Genome-Annotation-Data-START## Annotation Provider :: SGD Annotation Status :: Full Annotation Annotation Version :: R64-4-1 URL :: http://www.yeastgenome.org/ ##Genome-Annotation-Data-END## COMPLETENESS: incomplete on both ends. FEATURES Location/Qualifiers source 1..834 /organism="Saccharomyces cerevisiae S288C" /mol_type="mRNA" /strain="S288C" /db_xref="taxon:559292" /chromosome="XV" gene <1..>834 /gene="MPD2" /locus_tag="YOL088C" /db_xref="GeneID:854065" CDS 1..834 /gene="MPD2" /locus_tag="YOL088C" /EC_number="5.3.4.1" /experiment="EXISTENCE:direct assay:GO:0003756 protein disulfide isomerase activity [PMID:16002399]" /experiment="EXISTENCE:direct assay:GO:0005783 endoplasmic reticulum [PMID:26928762]" /experiment="EXISTENCE:direct assay:GO:0015035 protein-disulfide reductase activity [PMID:16002399]" /experiment="EXISTENCE:genetic interaction:GO:0003756 protein disulfide isomerase activity [PMID:11157982]" /experiment="EXISTENCE:genetic interaction:GO:0005783 endoplasmic reticulum [PMID:15377672]" /experiment="EXISTENCE:genetic interaction:GO:0006457 protein folding [PMID:11157982]" /experiment="EXISTENCE:genetic interaction:GO:0015035 protein-disulfide reductase activity [PMID:11157982]" /experiment="EXISTENCE:mutant phenotype:GO:0003756 protein disulfide isomerase activity [PMID:11157982]" /note="Member of the protein disulfide isomerase (PDI) family; exhibits chaperone activity; overexpression suppresses the lethality of a pdi1 deletion but does not complement all Pdi1p functions; undergoes oxidation by Ero1p" /codon_start=1 /product="protein disulfide isomerase MPD2" /protein_id="NP_014553.1" /db_xref="GeneID:854065" /db_xref="SGD:S000005448" /translation="
MKLHGFLFSVLSTCVVILPALAYSEAVTMVKSIEQYFDICNRNDSYTMIKYYTSWCQHCKTLAPVYEELGELYAKKANKDDTPINFLEVNCEFFGPTLCTDLPGFPIIELVKPRTKPLVLPKLDWSSMKFHERLWQRIKTWFNNPKYQLDTSRVVRFEGSRNLKSLSNFIDTVRSKDTEERFIEHIFDDSRNCNEELRSQQLLCKAGKEYYSDTLSKLYGDVNGLEKERRRLEALIKQNGDDLSKEVKEKLKIIRLQLSLLSHIEDQLEDTSSHDEL"
misc_feature <142..510 /gene="MPD2" /locus_tag="YOL088C" /note="The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox...; Region: Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; cl00388" /db_xref="CDD:469754" ORIGIN
atgaaattgcacggctttttattttccgtattatcaacatgcgtcgtcattttaccagcgttggcctacagtgaagctgtcacgatggtcaagtcgattgagcagtacttcgatatctgcaataggaatgattcttacacaatgataaaatactacacttcttggtgccaacattgtaaaactctggccccagtatacgaagagcttggtgagctatacgccaaaaaagctaataaagatgataccccaattaacttccttgaagttaactgtgaattcttcgggccaactttatgtaccgacttgcctggatttccaataattgaactggtcaaacctcgtactaagcccttagttcttccgaagctcgattggtcgtctatgaaatttcatgaaagactatggcaaagaatcaagacgtggttcaacaatcctaagtaccaactggatacgtctagggttgttcgttttgaagggagtaggaacctaaagagtttaagcaactttatcgatactgtaagaagtaaagatacagaagaaagattcatagaacatattttcgatgattctaggaattgcaatgaagaattacgttctcaacagcttctgtgtaaagctggtaaagaatactactctgatactttatctaaattatacggtgacgtgaatgggctggaaaaggaaaggcgaagactagaagctttaattaagcaaaatggagatgacttgagtaaagaagttaaagaaaaactgaaaatcattcgtctacaattgagcctattatcacacatagaagaccagttagaagataccagtagtcatgacgagctttga
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Creative Commons Attribution 4.0 International License (CC BY 4.0).
If you use GGRNA in your work, please cite:
Naito Y, Bono H. (2012)
GGRNA: an ultrafast, transcript-oriented search engine for genes and transcripts.
Nucleic Acids Res., 40, W592-W596.
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