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Q10057 (PDI1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative protein disulfide-isomerase C1F5.02

EC=5.3.4.1
Gene names
ORF Names:SPAC1F5.02
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 492470Putative protein disulfide-isomerase C1F5.02
PRO_0000034216

Regions

Domain23 – 128106Thioredoxin 1
Domain323 – 462140Thioredoxin 2
Motif489 – 4924Prevents secretion from ER Potential

Sites

Active site511Nucleophile By similarity
Active site541Nucleophile By similarity
Active site3851Nucleophile By similarity
Active site3881Nucleophile By similarity
Site521Contributes to redox potential value By similarity
Site531Contributes to redox potential value By similarity
Site1141Lowers pKa of C-terminal Cys of first active site By similarity
Site3861Contributes to redox potential value By similarity
Site3871Contributes to redox potential value By similarity
Site4481Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2571N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 54Redox-active By similarity
Disulfide bond385 ↔ 388Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q10057 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: C50B592365666667

FASTA49254,880
        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 

« Hide

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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAA92230.1.
PIRT38093.
RefSeqNP_592871.1. NM_001018271.2.

3D structure databases

ProteinModelPortalQ10057.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277962. 3 interactions.
MINTMINT-4696595.
STRING4896.SPAC1F5.02-1.

Proteomic databases

PaxDbQ10057.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC1F5.02.1; SPAC1F5.02.1:pep; SPAC1F5.02.
GeneID2541460.
KEGGspo:SPAC1F5.02.

Organism-specific databases

PomBaseSPAC1F5.02.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
KOK09580.
OMAPAIVLYR.
OrthoDBEOG71CFZN.
PhylomeDBQ10057.

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802559.
PROQ10057.

Entry information

Entry namePDI1_SCHPO
AccessionPrimary (citable) accession number: Q10057
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names