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Protein

Protein disulfide-isomerase

Gene
N/A
Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 sitei50 – 501NucleophileBy similarity
Sitei51 – 511Contributes to redox potential valueBy similarity
Sitei52 – 521Contributes to redox potential valueBy similarity
Active sitei53 – 531NucleophileBy similarity
Sitei113 – 1131Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei385 – 3851NucleophileBy similarity
Sitei386 – 3861Contributes to redox potential valueBy similarity
Sitei387 – 3871Contributes to redox potential valueBy similarity
Active sitei388 – 3881NucleophileBy similarity
Sitei451 – 4511Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BRENDAi5.3.4.1. 2710.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase (EC:5.3.4.1)
Short name:
PDI
OrganismiHumicola insolens (Soft-rot fungus)
Taxonomic identifieri34413 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 505485Protein disulfide-isomerasePRO_0000034215Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 53Redox-activePROSITE-ProRule annotation
Disulfide bondi385 ↔ 388Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP55059.

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi229 – 2324Combined sources
Turni235 – 2373Combined sources
Helixi238 – 2436Combined sources
Beta strandi248 – 2558Combined sources
Helixi256 – 27217Combined sources
Turni273 – 2764Combined sources
Beta strandi278 – 2836Combined sources
Helixi284 – 2874Combined sources
Helixi288 – 2947Combined sources
Beta strandi302 – 3087Combined sources
Turni309 – 3124Combined sources
Beta strandi313 – 3164Combined sources
Beta strandi319 – 3213Combined sources
Helixi325 – 33612Combined sources
Beta strandi355 – 3606Combined sources
Helixi362 – 3643Combined sources
Helixi365 – 3695Combined sources
Beta strandi374 – 3818Combined sources
Helixi386 – 40419Combined sources
Turni406 – 4105Combined sources
Beta strandi411 – 4177Combined sources
Turni418 – 4203Combined sources
Beta strandi429 – 4368Combined sources
Beta strandi445 – 4484Combined sources
Helixi453 – 46311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJJNMR-A354-469[»]
2DJKNMR-A228-355[»]
2KP1NMR-A354-469[»]
2KP2NMR-A228-355[»]
3WT1X-ray1.85A/B/C/D228-469[»]
3WT2X-ray3.30A/B/C228-469[»]
ProteinModelPortaliP55059.
SMRiP55059. Positions 226-469.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55059.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 128108Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini335 – 465131Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi502 – 5054Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center, Repeat, Signal

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. 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.

P55059-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHKAQKFALG LLAAAAVATA SDVVQLKKDT FDDFIKTNDL VLAEFFAPWC
60 70 80 90 100
GHCKALAPEY EEAATTLKEK NIKLAKVDCT EETDLCQQHG VEGYPTLKVF
110 120 130 140 150
RGLDNVSPYK GQRKAAAITS YMIKQSLPAV SEVTKDNLEE FKKADKAVLV
160 170 180 190 200
AYVDASDKAS SEVFTQVAEK LRDNYPFGSS SDAALAEAEG VKAPAIVLYK
210 220 230 240 250
DFDEGKAVFS EKFEVEAIEK FAKTGATPLI GEIGPETYSD YMSAGIPLAY
260 270 280 290 300
IFAETAEERK ELSDKLKPIA EAQRGVINFG TIDAKAFGAH AGNLNLKTDK
310 320 330 340 350
FPAFAIQEVA KNQKFPFDQE KEITFEAIKA FVDDFVAGKI EPSIKSEPIP
360 370 380 390 400
EKQEGPVTVV VAKNYNEIVL DDTKDVLIEF YAPWCGHCKA LAPKYEELGA
410 420 430 440 450
LYAKSEFKDR VVIAKVDATA NDVPDEIQGF PTIKLYPAGA KGQPVTYSGS
460 470 480 490 500
RTVEDLIKFI AENGKYKAAI SEDAEETSSA TETTTETATK SEEAAKETAT

EHDEL
Length:505
Mass (Da):55,114
Last modified:October 1, 1996 - v1
Checksum:i27E7C0D1A61B5F95
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74296 mRNA. Translation: AAC60578.1.
PIRiJC2291.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74296 mRNA. Translation: AAC60578.1.
PIRiJC2291.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJJNMR-A354-469[»]
2DJKNMR-A228-355[»]
2KP1NMR-A354-469[»]
2KP2NMR-A228-355[»]
3WT1X-ray1.85A/B/C/D228-469[»]
3WT2X-ray3.30A/B/C228-469[»]
ProteinModelPortaliP55059.
SMRiP55059. Positions 226-469.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP55059.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi5.3.4.1. 2710.

Miscellaneous databases

EvolutionaryTraceiP55059.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of a fungal cDNA encoding protein disulfide isomerase."
    Kajino T., Sarai K., Imaeda T., Idekoba C., Asami O., Yamada Y., Hirai M., Udaka S.
    Biosci. Biotechnol. Biochem. 58:1424-1429(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: KASI.

Entry informationi

Entry nameiPDI_HUMIN
AccessioniPrimary (citable) accession number: P55059
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 1, 2015
This is version 92 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.