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Q5R5B6

- PDIA1_PONAB

UniProt

Q5R5B6 - PDIA1_PONAB

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Protein
Protein disulfide-isomerase
Gene
P4HB, PDIA1
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP By similarity.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei53 – 531Nucleophile By similarity
Sitei54 – 541Contributes to redox potential value By similarity
Sitei55 – 551Contributes to redox potential value By similarity
Active sitei56 – 561Nucleophile By similarity
Sitei120 – 1201Lowers pKa of C-terminal Cys of first active site By similarity
Active sitei397 – 3971Nucleophile By similarity
Sitei398 – 3981Contributes to redox potential value By similarity
Sitei399 – 3991Contributes to redox potential value By similarity
Active sitei400 – 4001Nucleophile By similarity
Sitei461 – 4611Lowers pKa of C-terminal Cys of second active site By similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase (EC:5.3.4.1)
Short name:
PDI
Alternative name(s):
Cellular thyroid hormone-binding protein
Prolyl 4-hydroxylase subunit beta
p55
Gene namesi
Name:P4HB
Synonyms:PDIA1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Endoplasmic reticulum lumen By similarity. Melanosome By similarity. Cell membrane; Peripheral membrane protein Reviewed prediction
Note: Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces By similarity.

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  2. melanosome Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 By similarity
Add
BLAST
Chaini18 – 508491Protein disulfide-isomerase
PRO_0000034197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 56Redox-active By similarity
Modified residuei200 – 2001N6-acetyllysine By similarity
Modified residuei222 – 2221N6-succinyllysine By similarity
Modified residuei271 – 2711N6-succinyllysine By similarity
Disulfide bondi397 ↔ 400Redox-active By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PRIDEiQ5R5B6.

Interactioni

Subunit structurei

Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5R5B6.
SMRiQ5R5B6. Positions 18-357, 368-471.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 134117Thioredoxin 1
Add
BLAST
Domaini349 – 475127Thioredoxin 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi505 – 5084Prevents secretion from ER By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi480 – 4834Poly-Asp

Sequence similaritiesi

Contains 2 thioredoxin domains.

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG005920.
InParanoidiQ5R5B6.
KOiK09580.

Family and domain databases

Gene3Di3.40.30.10. 4 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.

Q5R5B6-1 [UniParc]FASTAAdd to Basket

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MLRRALLCLA VAGLVCADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA    50
PWCGHCKALA PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP 100
TIKFFRNGDT ASPKEYTAGR EADDIVNWLK KRTGPAATIL PDGAAAESLV 150
ESSEVAVVGF FKDVESDSAK QFLQAAEAID DIPFGITSNS DVFSKYQLDK 200
DGVVLFKKFD EGRNNFEGEV TKENLLDFIK HNQLPLVIEF TEQTAPKIFG 250
GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR 300
ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK 350
IKPHLMSQEL PDDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC 400
KQLAPIWDKL GETYKDHENI VIAKMDSTAN EVEAVKVHSF PTLKFFPASA 450
DRTVIDYNGE RTLDGFKKFL ESGGQDGAGD DDDLEDLEEA EEPDMEEDDD 500
QKAVKDEL 508
Length:508
Mass (Da):57,033
Last modified:December 21, 2004 - v1
Checksum:i114D79D9BC740400
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR860947 mRNA. Translation: CAH93050.1.
RefSeqiNP_001126805.1. NM_001133333.1.

Genome annotation databases

GeneIDi100173809.
KEGGipon:100173809.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR860947 mRNA. Translation: CAH93050.1 .
RefSeqi NP_001126805.1. NM_001133333.1.

3D structure databases

ProteinModelPortali Q5R5B6.
SMRi Q5R5B6. Positions 18-357, 368-471.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5R5B6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100173809.
KEGGi pon:100173809.

Organism-specific databases

CTDi 5034.

Phylogenomic databases

HOVERGENi HBG005920.
InParanoidi Q5R5B6.
KOi K09580.

Family and domain databases

Gene3Di 3.40.30.10. 4 hits.
InterProi IPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 2 hits.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 4 hits.
TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiPDIA1_PONAB
AccessioniPrimary (citable) accession number: Q5R5B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 21, 2004
Last modified: September 3, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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