MPD1_YEAST
ID MPD1_YEAST Reviewed; 318 AA.
AC Q12404; D6W2Y6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Protein disulfide-isomerase MPD1;
DE EC=5.3.4.1;
DE Flags: Precursor;
GN Name=MPD1; OrderedLocusNames=YOR288C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7649260; DOI=10.1016/0014-5793(95)00750-4;
RA Tachikawa H., Takeuchi Y., Funahashi W., Miura T., Gao X.D., Fujimoto D.,
RA Mizunaga T., Onodera K.;
RT "Isolation and characterization of a yeast gene, MPD1, the overexpression
RT of which suppresses inviability caused by protein disulfide isomerase
RT depletion.";
RL FEBS Lett. 369:212-216(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8896271;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.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 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., 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., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., 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 GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, AND INTERACTION WITH CNE1 AND EPS1.
RX PubMed=16002399; DOI=10.1074/jbc.m503377200;
RA Kimura T., Hosoda Y., Sato Y., Kitamura Y., Ikeda T., Horibe T.,
RA Kikuchi M.;
RT "Interactions among yeast protein-disulfide isomerase proteins and
RT endoplasmic reticulum chaperone proteins influence their activities.";
RL J. Biol. Chem. 280:31438-31441(2005).
CC -!- FUNCTION: Participates in the folding of proteins containing disulfide
CC bonds. {ECO:0000269|PubMed:16002399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBUNIT: Interacts with CNE1 and EPS1. {ECO:0000269|PubMed:16002399}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- MISCELLANEOUS: Present with 830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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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 EMBL; BK006948; DAA11052.1; -; Genomic_DNA.
DR PIR; S67190; S67190.
DR RefSeq; NP_014931.3; NM_001183707.3.
DR PDB; 3ED3; X-ray; 2.00 A; A/B=23-310.
DR PDBsum; 3ED3; -.
DR AlphaFoldDB; Q12404; -.
DR SMR; Q12404; -.
DR BioGRID; 34675; 79.
DR DIP; DIP-4085N; -.
DR IntAct; Q12404; 3.
DR STRING; 4932.YOR288C; -.
DR MaxQB; Q12404; -.
DR PaxDb; Q12404; -.
DR PRIDE; Q12404; -.
DR EnsemblFungi; YOR288C_mRNA; YOR288C; YOR288C.
DR GeneID; 854462; -.
DR KEGG; sce:YOR288C; -.
DR SGD; S000005814; MPD1.
DR VEuPathDB; FungiDB:YOR288C; -.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_059951_0_0_1; -.
DR InParanoid; Q12404; -.
DR OMA; QVASVNC; -.
DR BioCyc; YEAST:YOR288C-MON; -.
DR EvolutionaryTrace; Q12404; -.
DR PRO; PR:Q12404; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12404; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:SGD.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IDA:SGD.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:SGD.
DR GO; GO:0006457; P:protein folding; IGI:SGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR InterPro; IPR044569; PDIA6-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45815; PTHR45815; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
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; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Isomerase; Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..318
FT /note="Protein disulfide-isomerase MPD1"
FT /id="PRO_0000034220"
FT DOMAIN 22..158
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 315..318
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..62
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:3ED3"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:3ED3"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:3ED3"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:3ED3"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:3ED3"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:3ED3"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:3ED3"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3ED3"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:3ED3"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:3ED3"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:3ED3"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:3ED3"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3ED3"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3ED3"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:3ED3"
FT STRAND 174..186
FT /evidence="ECO:0007829|PDB:3ED3"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:3ED3"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:3ED3"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3ED3"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:3ED3"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:3ED3"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:3ED3"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:3ED3"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:3ED3"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:3ED3"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:3ED3"
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
