Reviewed, UniProtKB/Swiss-Prot O13811 (PDI2_SCHPO)

Names and origin

Protein names

Recommended name:
    Protein disulfide-isomerase C17H9.14c
    EC=5.3.4.1

Gene names

ORF Names:

SPAC17H9.14c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer By similarity.
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Domain	Redox-active center Repeat 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 cellular response to oxidative stress Inferred from mutant phenotype. Source: GeneDB_SPombe protein folding Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: InterPro
Molecular function	protein disulfide isomerase activity Inferred from mutant phenotype. Source: GeneDB_SPombe protein disulfide oxidoreductase activity Inferred from mutant phenotype. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 359	340	Protein disulfide-isomerase C17H9.14c		PRO_0000034217
Regions
	Domain	20 – 130	111	Thioredoxin 1
	Domain	134 – 250	117	Thioredoxin 2
Sites
	Active site	51	1	Nucleophile By similarity
	Active site	54	1	Nucleophile By similarity
	Site	52	1	Contributes to redox potential value By similarity
	Site	53	1	Contributes to redox potential value By similarity
	Site	116	1	Lowers pKa of C-terminal Cys of first active site By similarity
Amino acid modifications
	Disulfide bond	51 ↔ 54		Redox-active By similarity
	Disulfide bond	170 ↔ 173		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13811-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: A2FB610518DA2E50	FASTA	359	40,692
	10 20 30 40 50 60 MRLPLLSFVI FALFALVFAS GVVELQSLNE LENTIRASKK GALIEFYATW CGHCKSLAPV 70 80 90 100 110 120 YEELGALFED HNDVLIGKID ADTHSDVADK YHITGFPTLI WFPPDGSEPV QYSNARDVDS 130 140 150 160 170 180 LTQFVSEKTG IKKRKIVLPS NVVELDSLNF DKVVMDDKKD VLVEFYADWC GYCKRLAPTY 190 200 210 220 230 240 ETLGKVFKNE PNVEIVKINA DVFADIGRLH EVASFPTIKF FPKDDKDKPE LYEGDRSLES 250 260 270 280 290 300 LIEYINKKSG TQRSPDGTLL STAGRIPTFD EFAAEFLDMS NAAKEVVLEK VKQLALEDSS 310 320 330 340 350 RWTKYYKKVF EKILNDENWV HKEAKRLSKL LRQKSIALAS ADDFKTRLNI LNSFLPGNH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Physiological roles and regulation of protein disulfide isomerase in the fission yeast Schizosaccharomyces pombe." Choi Y.-S., Kim H.-G., Lim H.-W., Lim C.-J. Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ104736 Genomic DNA. Translation: AAZ13768.1. CU329670 Genomic DNA. Translation: CAB11223.1.
PIR	T37880.
RefSeq	NP_593584.1.
3D structure databases
HSSP	HSSP built from PDB template 1MEK based on UniProtKB P07237.
ModBase	Search...
Genome annotation databases
GeneID	2542270.
KEGG	spo:SPAC17H9.14c.
NMPDR	fig|4896.1.peg.3554.
Organism-specific databases
GeneDB_Spombe	SPAC17H9.14c.
Phylogenomic databases
OMA	GFPTLKW.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001258-MON.
BRENDA	5.3.4.1. 653.
Gene expression databases
ArrayExpress	O13811.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR011679. ER_p29_C. IPR017936. Thioredoxin-like. IPR006662. Thioredoxin-like_subdom. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:1.20.1150.12. ERp29_C_type. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.
Pfam	PF07749. ERp29. 1 hit. PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
TIGRFAMs	TIGR01126. pdi_dom. 2 hits.
PROSITE	PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDI2_SCHPO

Accession

Primary (citable) accession number: O13811
Secondary accession number(s): Q4F7X2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)