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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)DescriptionActionsGraphical viewLength
Active sitei50NucleophileBy similarity1
Sitei51Contributes to redox potential valueBy similarity1
Sitei52Contributes to redox potential valueBy similarity1
Active sitei53NucleophileBy similarity1
Sitei113Lowers pKa of C-terminal Cys of first active siteBy similarity1
Active sitei385NucleophileBy similarity1
Sitei386Contributes to redox potential valueBy similarity1
Sitei387Contributes to redox potential valueBy similarity1
Active sitei388NucleophileBy similarity1
Sitei451Lowers pKa of C-terminal Cys of second active siteBy similarity1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000003421521 – 505Protein disulfide-isomeraseAdd BLAST485

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50 ↔ 53Redox-activePROSITE-ProRule annotation
Disulfide bondi385 ↔ 388Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP55059.

Structurei

Secondary structure

1505
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi230 – 232Combined sources3
Turni235 – 237Combined sources3
Helixi238 – 243Combined sources6
Beta strandi244 – 246Combined sources3
Beta strandi248 – 255Combined sources8
Helixi256 – 272Combined sources17
Turni273 – 276Combined sources4
Beta strandi277 – 283Combined sources7
Turni284 – 287Combined sources4
Helixi288 – 294Combined sources7
Beta strandi302 – 308Combined sources7
Turni309 – 312Combined sources4
Beta strandi313 – 316Combined sources4
Beta strandi319 – 321Combined sources3
Helixi325 – 337Combined sources13
Beta strandi355 – 360Combined sources6
Helixi362 – 369Combined sources8
Beta strandi374 – 381Combined sources8
Helixi386 – 403Combined sources18
Turni406 – 410Combined sources5
Beta strandi411 – 417Combined sources7
Turni418 – 420Combined sources3
Beta strandi429 – 436Combined sources8
Beta strandi438 – 440Combined sources3
Beta strandi445 – 448Combined sources4
Helixi453 – 463Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DJJNMR-A354-469[»]
2DJKNMR-A228-355[»]
2KP1NMR-A354-469[»]
2KP2NMR-A228-355[»]
2RUENMR-A354-469[»]
2RUFNMR-A354-469[»]
3WT1X-ray1.85A/B/C/D228-469[»]
3WT2X-ray3.30A/B/C228-469[»]
5CRWX-ray1.60A228-469[»]
ProteinModelPortaliP55059.
SMRiP55059.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55059.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 128Thioredoxin 1PROSITE-ProRule annotationAdd BLAST108
Domaini335 – 465Thioredoxin 2PROSITE-ProRule annotationAdd BLAST131

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi502 – 505Prevents secretion from ERPROSITE-ProRule annotation4

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DJJNMR-A354-469[»]
2DJKNMR-A228-355[»]
2KP1NMR-A354-469[»]
2KP2NMR-A228-355[»]
2RUENMR-A354-469[»]
2RUFNMR-A354-469[»]
3WT1X-ray1.85A/B/C/D228-469[»]
3WT2X-ray3.30A/B/C228-469[»]
5CRWX-ray1.60A228-469[»]
ProteinModelPortaliP55059.
SMRiP55059.
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...

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: November 2, 2016
This is version 99 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

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.