ID   MPD1_YEAST              Reviewed;         318 AA.
AC   Q12404;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 74.
DE   RecName: Full=Protein disulfide-isomerase MPD1;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=MPD1; OrderedLocusNames=YOR288C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95377403; PubMed=7649260; DOI=10.1016/0014-5793(95)00750-4;
RA   Tachikawa H., Takeuchi Y., Funahashi W., Miura T., Gao X.D.,
RA   Fujimoto D., Mizunaga T., Onodera K.;
RT   "Isolation and characterization of a yeast gene, MPD1, the
RT   overexpression of which suppresses inviability caused by protein
RT   disulfide isomerase depletion.";
RL   FEBS Lett. 369:212-216(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97051594; PubMed=8896271;
RX   DOI=10.1002/(SICI)1097-0061(199609)12:10B<1059::AID-YEA994>3.0.CO;2-7;
RA   Cheret G., Bernardi A., Sor F.J.;
RT   "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT   Saccharomyces cerevisiae.";
RL   Yeast 12:1059-1064(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97313270; PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
RA   Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
RA   Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
RA   Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
RA   Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
RA   Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
RA   Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
RA   Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
RA   Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
RA   Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
RA   Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
RA   Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
RA   Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
RA   Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
RA   Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Participates in the folding of proteins containing
CC       disulfide bonds.
CC   -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC       proteins.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (Potential).
CC   -!- MISCELLANEOUS: Present with 830 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; D34633; BAA07015.1; -; Genomic_DNA.
DR   EMBL; X89633; CAA61791.1; -; Genomic_DNA.
DR   EMBL; Z75196; CAA99515.1; -; Genomic_DNA.
DR   PIR; S67190; S67190.
DR   RefSeq; NP_014931.1; -.
DR   PDB; 3ED3; X-ray; 2.00 A; A/B=23-310.
DR   PDBsum; 3ED3; -.
DR   DIP; DIP:4085N; -.
DR   IntAct; Q12404; 1.
DR   PeptideAtlas; Q12404; -.
DR   Ensembl; YOR288C; Saccharomyces cerevisiae.
DR   GeneID; 854462; -.
DR   GenomeReviews; Y13140_GR; YOR288C.
DR   KEGG; sce:YOR288C; -.
DR   NMPDR; fig|4932.3.peg.6043; -.
DR   CYGD; YOR288c; -.
DR   SGD; S000005814; MPD1.
DR   HOGENOM; Q12404; -.
DR   OMA; Q12404; TTLVEFY.
DR   BRENDA; 5.3.4.1; 250.
DR   NextBio; 976742; -.
DR   GermOnline; YOR288C; Saccharomyces cerevisiae.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IDA:SGD.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IDA:SGD.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IGI:SGD.
DR   InterPro; IPR000886; ER_targeting_sequence.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR006662; Thioredoxin-like_subdom.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Disulfide bond;
KW   Endoplasmic reticulum; Glycoprotein; Isomerase; Redox-active center;
KW   Signal.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    318       Protein disulfide-isomerase MPD1.
FT                                /FTId=PRO_0000034220.
FT   DOMAIN       22    158       Thioredoxin.
FT   MOTIF       315    318       Prevents secretion from ER (Potential).
FT   CARBOHYD     47     47       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    307    307       N-linked (GlcNAc...) (Potential).
FT   DISULFID     59     62       Redox-active (By similarity).
SQ   SEQUENCE   318 AA;  36408 MW;  3F96477E8182DC5C CRC64;
     MLFLNIIKLL LGLFIMNEVK AQNFYDSDPH ISELTPKSFD KAIHNTNYTS LVEFYAPWCG
     HCKKLSSTFR KAAKRLDGVV QVAAVNCDLN KNKALCAKYD VNGFPTLMVF RPPKIDLSKP
     IDNAKKSFSA HANEVYSGAR TLAPIVDFSL SRIRSYVKKF VRIDTLGSLL RKSPKLSVVL
     FSKQDKISPV YKSIALDWLG KFDFYSISNK KLKQLTDMNP TYEKTPEIFK YLQKVIPEQR
     QSDKSKLVVF DADKDKFWEY EGNSINKNDI SKFLRDTFSI TPNEGPFSRR SEYIAYLKTG
     KKPIKKNHSS SGNKHDEL
//