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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
//

by @meso_cacase at DBCLS
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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. [Full Text]