Reviewed, UniProtKB/Swiss-Prot Q99316 (MPD2_YEAST)

Names and origin

Protein names

Recommended name:
    Protein disulfide isomerase MPD2
    EC=5.3.4.1

Gene names

Name:	MPD2
Ordered Locus Names:	YOL088C
ORF Names:	O0941

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Non essential disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. Able to fold proteins by being directly oxidized by ERO1. Ref.1
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subcellular location	Endoplasmic reticulum Ref.5.
Miscellaneous	Present with 1520 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Redox-active center Signal
Molecular function	Isomerase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro protein folding Inferred from genetic interaction. Source: SGD
Cellular component	endoplasmic reticulum Inferred from genetic interaction. Source: SGD
Molecular function	protein disulfide isomerase activity Inferred from direct assay. Source: SGD protein disulfide oxidoreductase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 277	255	Protein disulfide isomerase MPD2		PRO_0000034182
Regions
	Domain	27 – 172	146	Thioredoxin
	Motif	274 – 277	4	Prevents secretion from ER Potential
Amino acid modifications
	Disulfide bond	56 ↔ 59		Redox-active By similarity
Experimental info
	Mutagenesis	56	1	C → S: Loss of function; when associated with S-59. Ref.1
	Mutagenesis	59	1	C → S: Loss of function; when associated with S-56. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99316-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: ECCEA7C6CBB10488	FASTA	277	32,401
	10 20 30 40 50 60 MKLHGFLFSV LSTCVVILPA LAYSEAVTMV KSIEQYFDIC NRNDSYTMIK YYTSWCQHCK 70 80 90 100 110 120 TLAPVYEELG ELYAKKANKD DTPINFLEVN CEFFGPTLCT DLPGFPIIEL VKPRTKPLVL 130 140 150 160 170 180 PKLDWSSMKF HERLWQRIKT WFNNPKYQLD TSRVVRFEGS RNLKSLSNFI DTVRSKDTEE 190 200 210 220 230 240 RFIEHIFDDS RNCNEELRSQ QLLCKAGKEY YSDTLSKLYG DVNGLEKERR RLEALIKQNG 250 260 270 DDLSKEVKEK LKIIRLQLSL LSHIEDQLED TSSHDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner." Tachikawa H., Funahashi W., Takeuchi Y., Nakanishi H., Nishihara R., Katoh S., Gao X.D., Mizunaga T., Fujimoto D. Biochem. Biophys. Res. Commun. 239:710-714(1997) [PubMed: 9367834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF CYS-56 AND CYS-59.
[2]	"A 29.425 kb segment on the left arm of yeast chromosome XV contains more than twice as many unknown as known open reading frames." Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M. Yeast 11:975-986(1995) [PubMed: 8533473] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." 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 V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum." Frand A.R., Kaiser C.A. Mol. Cell 4:469-477(1999) [PubMed: 10549279] [Abstract] Cited for: OXIDATION BY ERO1.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D34634 Genomic DNA. Translation: BAA22222.1. X83121 Genomic DNA. Translation: CAA58191.1. Z74830 Genomic DNA. Translation: CAA99100.1.
PIR	S57381.
RefSeq	NP_014553.1.
3D structure databases
SMR	Q99316. Positions 37-113, 43-172.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1451N.
IntAct	Q99316. 3 interactions.
STRING	Q99316.
Genome annotation databases
Ensembl	YOL088C; YOL088C; YOL088C; Saccharomyces cerevisiae. [Genome view]
GeneID	854065.
KEGG	sce:YOL088C.
NMPDR	fig|4932.3.peg.5642.
Organism-specific databases
CYGD	YOL088c.
SGD	S000005448. MPD2.
Phylogenomic databases
eggNOG	fuNOG10906.
OMA	SHCKKLK.
OrthoDB	EOG90CK15.
PhylomeDB	Q99316.
Enzyme and pathway databases
BRENDA	5.3.4.1. 250.
Gene expression databases
ArrayExpress	Q99316.
Genevestigator	Q99316.
GermOnline	YOL088C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR017936. Thioredoxin-like. IPR012336. Thioredoxin-like_fold. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF00085. Thioredoxin. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. False negative. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	975674.

Entry information

Entry name

MPD2_YEAST

Accession

Primary (citable) accession number: Q99316

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)