MPD2_YEAST
ID MPD2_YEAST Reviewed; 277 AA.
AC Q99316; D6W1Y0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein disulfide isomerase MPD2;
DE EC=5.3.4.1;
DE Flags: Precursor;
GN Name=MPD2; OrderedLocusNames=YOL088C; ORFNames=O0941;
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], FUNCTION, AND MUTAGENESIS OF CYS-56 AND
RP CYS-59.
RX PubMed=9367834; DOI=10.1006/bbrc.1997.7426;
RA Tachikawa H., Funahashi W., Takeuchi Y., Nakanishi H., Nishihara R.,
RA Katoh S., Gao X.D., Mizunaga T., Fujimoto D.;
RT "Overproduction of Mpd2p suppresses the lethality of protein disulfide
RT isomerase depletion in a CXXC sequence dependent manner.";
RL Biochem. Biophys. Res. Commun. 239:710-714(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8533473; DOI=10.1002/yea.320111009;
RA Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
RT "A 29.425 kb segment on the left arm of yeast chromosome XV contains more
RT than twice as many unknown as known open reading frames.";
RL Yeast 11:975-986(1995).
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 OXIDATION BY ERO1.
RX PubMed=10549279; DOI=10.1016/s1097-2765(00)80198-7;
RA Frand A.R., Kaiser C.A.;
RT "Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond
RT formation in the endoplasmic reticulum.";
RL Mol. Cell 4:469-477(1999).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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).
CC -!- FUNCTION: Non essential disulfide isomerase, which participates in the
CC folding of proteins containing disulfide bonds. May be involved in
CC glycosylation, prolyl hydroxylation and triglyceride transfer. Able to
CC fold proteins by being directly oxidized by ERO1.
CC {ECO:0000269|PubMed:9367834}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1520 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; D34634; BAA22222.1; -; Genomic_DNA.
DR EMBL; X83121; CAA58191.1; -; Genomic_DNA.
DR EMBL; Z74830; CAA99100.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10696.1; -; Genomic_DNA.
DR PIR; S57381; S57381.
DR RefSeq; NP_014553.1; NM_001183342.1.
DR AlphaFoldDB; Q99316; -.
DR BioGRID; 34314; 129.
DR DIP; DIP-1451N; -.
DR IntAct; Q99316; 5.
DR MINT; Q99316; -.
DR STRING; 4932.YOL088C; -.
DR MaxQB; Q99316; -.
DR PaxDb; Q99316; -.
DR PRIDE; Q99316; -.
DR EnsemblFungi; YOL088C_mRNA; YOL088C; YOL088C.
DR GeneID; 854065; -.
DR KEGG; sce:YOL088C; -.
DR SGD; S000005448; MPD2.
DR VEuPathDB; FungiDB:YOL088C; -.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_087689_0_0_1; -.
DR InParanoid; Q99316; -.
DR OMA; CNRNDSY; -.
DR BioCyc; YEAST:YOL088C-MON; -.
DR PRO; PR:Q99316; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99316; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IGI:SGD.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:SGD.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:SGD.
DR GO; GO:0006457; P:protein folding; IGI:SGD.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..277
FT /note="Protein disulfide isomerase MPD2"
FT /id="PRO_0000034182"
FT DOMAIN 27..172
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 274..277
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT DISULFID 56..59
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MUTAGEN 56
FT /note="C->S: Loss of function; when associated with S-59."
FT /evidence="ECO:0000269|PubMed:9367834"
FT MUTAGEN 59
FT /note="C->S: Loss of function; when associated with S-56."
FT /evidence="ECO:0000269|PubMed:9367834"
SQ SEQUENCE 277 AA; 32401 MW; ECCEA7C6CBB10488 CRC64;
MKLHGFLFSV LSTCVVILPA LAYSEAVTMV KSIEQYFDIC NRNDSYTMIK YYTSWCQHCK
TLAPVYEELG ELYAKKANKD DTPINFLEVN CEFFGPTLCT DLPGFPIIEL VKPRTKPLVL
PKLDWSSMKF HERLWQRIKT WFNNPKYQLD TSRVVRFEGS RNLKSLSNFI DTVRSKDTEE
RFIEHIFDDS RNCNEELRSQ QLLCKAGKEY YSDTLSKLYG DVNGLEKERR RLEALIKQNG
DDLSKEVKEK LKIIRLQLSL LSHIEDQLED TSSHDEL
