Reviewed, UniProtKB/Swiss-Prot Q10057 (PDI1_SCHPO)

Names and origin

Protein names

Recommended name:
    Putative protein disulfide-isomerase C1F5.02
    EC=5.3.4.1

Gene names

ORF Names:

SPAC1F5.02

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	492 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.
Subcellular location	Endoplasmic reticulum lumen By similarity.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: GeneDB_SPombe endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein disulfide isomerase activity Inferred from electronic annotation. Source: EC
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 – 492	470	Putative protein disulfide-isomerase C1F5.02		PRO_0000034216
Regions
	Domain	23 – 128	106	Thioredoxin 1
	Domain	323 – 462	140	Thioredoxin 2
	Motif	489 – 492	4	Prevents secretion from ER Potential
Sites
	Active site	51	1	Nucleophile By similarity
	Active site	54	1	Nucleophile By similarity
	Active site	385	1	Nucleophile By similarity
	Active site	388	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	114	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	386	1	Contributes to redox potential value By similarity
	Site	387	1	Contributes to redox potential value By similarity
	Site	448	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	257	1	N-linked (GlcNAc...) Potential
	Disulfide bond	51 ↔ 54		Redox-active By similarity
	Disulfide bond	385 ↔ 388		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q10057-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: C50B592365666667	FASTA	492	54,880
	10 20 30 40 50 60 MKISNLLAAF LAFSGGFFCA SAEVPKVNKE GLNELITADK VLMVKFYAPW CGHCKALAPE 70 80 90 100 110 120 YESAADELEK DGISLVEVDC TEEGDLCSEY SIRGYPTLNV FKNGKQISQY SGPRKHDALV 130 140 150 160 170 180 KYMRKQLLPT VKPISKDTLE NFVEKADDLA VVAFFKDQKL NDTYTEVAEV MKDDFVFAAS 190 200 210 220 230 240 DDKELAKSLG SNFPGIVAFT KDAAQDSDKL VYTGDWDPAS IADFIGVSSI PLLDELNQMT 250 260 270 280 290 300 FGKYQQSGLP LGIIFYNSTE SRDELYDVFQ PLAKKYQDTL RFAFLDAVRY GAVAKQMNVE 310 320 330 340 350 360 SDWPAFVIAN LKSMLKYPFP TTELTAKAMT KFVGDFVDGK LQPKIKSQPI PESQEDLVVL 370 380 390 400 410 420 VADNFDDIVM DETKDVLVEF YAPWCGHCKN LAPTYEKLAE EYSDDSNVVV AKIDATENDI 430 440 450 460 470 480 SVSISGFPTI MFFKANDKVN PVRYEGDRTL EDLSAFIDKH ASFEPIKKEK ESVPAPDLED 490 QVAVEDEMAD EL

References

[1]

"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	CU329670 Genomic DNA. Translation: CAA92230.1.
PIR	T38093.
RefSeq	NP_592871.1.
3D structure databases
HSSP	HSSP built from PDB template 1MEK based on UniProtKB P07237.
ModBase	Search...
Genome annotation databases
GeneID	2541460.
KEGG	spo:SPAC1F5.02.
NMPDR	fig|4896.1.peg.2841.
Organism-specific databases
GeneDB_Spombe	SPAC1F5.02.
Phylogenomic databases
OMA	Q10057. EETINGN.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000606-MON.
BRENDA	5.3.4.1. 653.
Gene expression databases
ArrayExpress	Q10057.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR000886. ER_targeting_sequence. IPR005792. Prot_disulphide_isomerase. IPR017936. Thioredoxin-like. IPR006662. Thioredoxin-like_subdom. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 3 hits.
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
TIGRFAMs	TIGR01130. ER_PDI_fam. 1 hit. TIGR01126. pdi_dom. 2 hits.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDI1_SCHPO

Accession

Primary (citable) accession number: Q10057

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)