Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein disulfide-isomerase C17H9.14c

Gene

SPAC17H9.14c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.By similarity

Catalytic activityi

Catalyzes the rearrangement of -S-S- bonds in proteins.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei51 – 511NucleophileBy similarity
Sitei52 – 521Contributes to redox potential valueBy similarity
Sitei53 – 531Contributes to redox potential valueBy similarity
Active sitei54 – 541NucleophileBy similarity
Sitei116 – 1161Lowers pKa of C-terminal Cys of first active siteBy similarity

GO - Molecular functioni

  • protein disulfide isomerase activity Source: PomBase
  • protein disulfide oxidoreductase activity Source: PomBase

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular response to oxidative stress Source: PomBase
  • oxidation-reduction process Source: GOC
  • protein folding Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BRENDAi5.3.4.1. 5613.
ReactomeiR-SPO-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase C17H9.14c (EC:5.3.4.1)
Gene namesi
ORF Names:SPAC17H9.14c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC17H9.14c.
PomBaseiSPAC17H9.14c.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 359340Protein disulfide-isomerase C17H9.14cPRO_0000034217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 54Redox-activePROSITE-ProRule annotation
Disulfide bondi170 ↔ 173Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiO13811.

Interactioni

Protein-protein interaction databases

BioGridi278739. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliO13811.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 130111Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini134 – 250117Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

HOGENOMiHOG000176389.
InParanoidiO13811.
KOiK09584.
OMAiPQIYRKT.
OrthoDBiEOG71CFZN.
PhylomeDBiO13811.

Family and domain databases

Gene3Di1.20.1150.12. 1 hit.
3.40.30.10. 2 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR011679. ER_p29_C.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF07749. ERp29. 1 hit.
PF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 2 hits.
TIGRFAMsiTIGR01126. pdi_dom. 2 hits.
PROSITEiPS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O13811-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLPLLSFVI FALFALVFAS GVVELQSLNE LENTIRASKK GALIEFYATW
60 70 80 90 100
CGHCKSLAPV YEELGALFED HNDVLIGKID ADTHSDVADK YHITGFPTLI
110 120 130 140 150
WFPPDGSEPV QYSNARDVDS LTQFVSEKTG IKKRKIVLPS NVVELDSLNF
160 170 180 190 200
DKVVMDDKKD VLVEFYADWC GYCKRLAPTY ETLGKVFKNE PNVEIVKINA
210 220 230 240 250
DVFADIGRLH EVASFPTIKF FPKDDKDKPE LYEGDRSLES LIEYINKKSG
260 270 280 290 300
TQRSPDGTLL STAGRIPTFD EFAAEFLDMS NAAKEVVLEK VKQLALEDSS
310 320 330 340 350
RWTKYYKKVF EKILNDENWV HKEAKRLSKL LRQKSIALAS ADDFKTRLNI

LNSFLPGNH
Length:359
Mass (Da):40,692
Last modified:January 1, 1998 - v1
Checksum:iA2FB610518DA2E50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ104736 Genomic DNA. Translation: AAZ13768.1.
CU329670 Genomic DNA. Translation: CAB11223.1.
PIRiT37880.
RefSeqiNP_593584.1. NM_001019016.2.

Genome annotation databases

EnsemblFungiiSPAC17H9.14c.1; SPAC17H9.14c.1:pep; SPAC17H9.14c.
GeneIDi2542270.
KEGGispo:SPAC17H9.14c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ104736 Genomic DNA. Translation: AAZ13768.1.
CU329670 Genomic DNA. Translation: CAB11223.1.
PIRiT37880.
RefSeqiNP_593584.1. NM_001019016.2.

3D structure databases

ProteinModelPortaliO13811.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278739. 4 interactions.

Proteomic databases

MaxQBiO13811.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC17H9.14c.1; SPAC17H9.14c.1:pep; SPAC17H9.14c.
GeneIDi2542270.
KEGGispo:SPAC17H9.14c.

Organism-specific databases

EuPathDBiFungiDB:SPAC17H9.14c.
PomBaseiSPAC17H9.14c.

Phylogenomic databases

HOGENOMiHOG000176389.
InParanoidiO13811.
KOiK09584.
OMAiPQIYRKT.
OrthoDBiEOG71CFZN.
PhylomeDBiO13811.

Enzyme and pathway databases

BRENDAi5.3.4.1. 5613.
ReactomeiR-SPO-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

PROiO13811.

Family and domain databases

Gene3Di1.20.1150.12. 1 hit.
3.40.30.10. 2 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR011679. ER_p29_C.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF07749. ERp29. 1 hit.
PF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 2 hits.
TIGRFAMsiTIGR01126. pdi_dom. 2 hits.
PROSITEiPS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiPDI2_SCHPO
AccessioniPrimary (citable) accession number: O13811
Secondary accession number(s): Q4F7X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.