Q12404 (MPD1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase MPD1
EC=5.3.4.1

Gene names

Name:	MPD1
Ordered Locus Names:	YOR288C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	318 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	Participates in the folding of proteins containing disulfide bonds. Ref.6
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	Interacts with CNE1 and EPS1. Ref.6
Subcellular location	Endoplasmic reticulum lumen Potential.
Miscellaneous	Present with 830 molecules/cell in log phase SD medium.
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 Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell fungal-type vacuole Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from direct assay Ref.6. Source: SGD protein disulfide oxidoreductase activity Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 318

297

Protein disulfide-isomerase MPD1

PRO_0000034220

Regions

Domain

22 – 158

137

Thioredoxin

Motif

315 – 318

4

Prevents secretion from ER Potential

Amino acid modifications

Glycosylation

47

1

N-linked (GlcNAc...) Potential

Glycosylation

307

1

N-linked (GlcNAc...) Potential

Disulfide bond

59 ↔ 62

Redox-active By similarity

Secondary structure

1

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318

Helix Strand Turn

Details...

Helix

36 – 43

8

Beta strand

45 – 48

4

Beta strand

50 – 55

6

Helix

60 – 63

4

Helix

66 – 75

10

Turn

76 – 79

4

Beta strand

80 – 86

7

Turn

90 – 92

3

Helix

93 – 98

6

Beta strand

103 – 111

9

Beta strand

132 – 135

4

Helix

142 – 150

9

Beta strand

157 – 159

3

Helix

163 – 165

3

Helix

166 – 170

5

Beta strand

174 – 186

13

Helix

189 – 197

9

Beta strand

202 – 208

7

Helix

209 – 211

3

Helix

226 – 239

14

Beta strand

246 – 251

6

Turn

252 – 255

4

Beta strand

256 – 259

4

Helix

267 – 278

12

Beta strand

283 – 285

3

Helix

289 – 299

11

Sequences

	Sequence		Length	Mass (Da)
	Q12404 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3F96477E8182DC5C	FASTA	318	36,408
	10 20 30 40 50 60 MLFLNIIKLL LGLFIMNEVK AQNFYDSDPH ISELTPKSFD KAIHNTNYTS LVEFYAPWCG 70 80 90 100 110 120 HCKKLSSTFR KAAKRLDGVV QVAAVNCDLN KNKALCAKYD VNGFPTLMVF RPPKIDLSKP 130 140 150 160 170 180 IDNAKKSFSA HANEVYSGAR TLAPIVDFSL SRIRSYVKKF VRIDTLGSLL RKSPKLSVVL 190 200 210 220 230 240 FSKQDKISPV YKSIALDWLG KFDFYSISNK KLKQLTDMNP TYEKTPEIFK YLQKVIPEQR 250 260 270 280 290 300 QSDKSKLVVF DADKDKFWEY EGNSINKNDI SKFLRDTFSI TPNEGPFSRR SEYIAYLKTG 310 KKPIKKNHSS SGNKHDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion." Tachikawa H., Takeuchi Y., Funahashi W., Miura T., Gao X.D., Fujimoto D., Mizunaga T., Onodera K. FEBS Lett. 369:212-216(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of Saccharomyces cerevisiae." Cheret G., Bernardi A., Sor F.J. Yeast 12:1059-1064(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities." Kimura T., Hosoda Y., Sato Y., Kitamura Y., Ikeda T., Horibe T., Kikuchi M. J. Biol. Chem. 280:31438-31441(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CNE1 AND EPS1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D34633 Genomic DNA. Translation: BAA07015.1.
X89633 Genomic DNA. Translation: CAA61791.1.
Z75196 Genomic DNA. Translation: CAA99515.1.
BK006948 Genomic DNA. Translation: DAA11052.1.

PIR

S67190.

RefSeq

NP_014931.3. NM_001183707.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ED3	X-ray	2.00	A/B	23-310	[»]

ProteinModelPortal

Q12404.

SMR

Q12404. Positions 22-301.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4085N.

IntAct

Q12404. 3 interactions.

MINT

MINT-479800.

STRING

4932.YOR288C.

Proteomic databases

PaxDb

Q12404.

PeptideAtlas

Q12404.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR288C; YOR288C; YOR288C.

GeneID

854462.

KEGG

sce:YOR288C.
sce:YOR290C.

Organism-specific databases

CYGD

YOR288c.

SGD

S000005814. MPD1.

Phylogenomic databases

eggNOG

COG0526.

HOGENOM

HOG000248396.

KO

K09584.
K11786.

OMA

TTLVEFY.

OrthoDB

EOG4Q5CZR.

Gene expression databases

Genevestigator

Q12404.

GermOnline

YOR288C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]

Pfam

PF00085. Thioredoxin. 1 hit.
[Graphical view]

PRINTS

PR00421. THIOREDOXIN.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q12404.

NextBio

976742.

Entry information

Entry name

MPD1_YEAST

Accession

Primary (citable) accession number: Q12404
Secondary accession number(s): D6W2Y6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program