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Q8R4U2

- PDIA1_CRIGR

UniProt

Q8R4U2 - PDIA1_CRIGR

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Protein

Protein disulfide-isomerase

Gene

P4HB

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
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.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei55 – 551NucleophileBy similarity
Sitei56 – 561Contributes to redox potential valueBy similarity
Sitei57 – 571Contributes to redox potential valueBy similarity
Active sitei58 – 581NucleophileBy similarity
Sitei122 – 1221Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei399 – 3991NucleophileBy similarity
Sitei400 – 4001Contributes to redox potential valueBy similarity
Sitei401 – 4011Contributes to redox potential valueBy similarity
Active sitei402 – 4021NucleophileBy similarity
Sitei463 – 4631Lowers pKa of C-terminal Cys of second active siteBy 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):
Prolyl 4-hydroxylase subunit beta
p58
Gene namesi
Name:P4HB
Synonyms:PDIA1
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation. Melanosome By similarity. Cell membrane Curated; Peripheral membrane protein Curated
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.By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 509490Protein disulfide-isomerasePRO_0000034194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 58Redox-activePROSITE-ProRule annotation
Modified residuei202 – 2021N6-acetyllysineBy similarity
Modified residuei224 – 2241N6-succinyllysineBy similarity
Modified residuei273 – 2731N6-succinyllysineBy similarity
Disulfide bondi399 ↔ 402Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PRIDEiQ8R4U2.

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.By similarity

Protein-protein interaction databases

MINTiMINT-4997811.

Structurei

3D structure databases

ProteinModelPortaliQ8R4U2.
SMRiQ8R4U2. Positions 20-359, 370-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 136117Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini335 – 477143Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi506 – 5094Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi482 – 4876Poly-Asp

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

HOVERGENiHBG005920.
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.

Q8R4U2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSRSLLCLA LAWVARVGAD APEEEDNVLV LKKSNFAEAL AAHNYLLVEF
60 70 80 90 100
YAPWCGHCKA LAPEYAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG
110 120 130 140 150
YPTIKFFKNG DTASPKEYTA GREADDIVNW LKKRTGPAAT TLSDTAAAET
160 170 180 190 200
LIDSSEVAVI GFFKDVESDS AKQFLLAAEA VDDIPFGITS NSGVFSKYQL
210 220 230 240 250
DKDGVVLFKK FDEGRNNFEG EVTKEKLLDF IKHNQLPLVI EFTEQTAPKI
260 270 280 290 300
FGGEIKTHIL LFLPKSVSDY DGKLGNFKKA AEGFKGKILF IFIDSDHTDN
310 320 330 340 350
QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE
360 370 380 390 400
GKIKPHLMSQ ELPEDWDKQP VKVLVGKNFE EVAFDEKKNV FVEFYAPWCG
410 420 430 440 450
HCKQLAPIWD KLGETYKDHE NIIIAKMDST ANEVEAVKVH SFPTLKFFPA
460 470 480 490 500
TADRTVIDYN GERTLDGFKK FLESGGQDGA GDDDDVDLEE ALEPDMEEDD

DQKAVKDEL
Length:509
Mass (Da):57,010
Last modified:June 1, 2002 - v1
Checksum:i9B9B7513DE918194
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF364317 mRNA. Translation: AAM00284.1.
RefSeqiNP_001233622.1. NM_001246693.1.

Genome annotation databases

GeneIDi100689433.
KEGGicge:100689433.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF364317 mRNA. Translation: AAM00284.1 .
RefSeqi NP_001233622.1. NM_001246693.1.

3D structure databases

ProteinModelPortali Q8R4U2.
SMRi Q8R4U2. Positions 20-359, 370-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4997811.

Proteomic databases

PRIDEi Q8R4U2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100689433.
KEGGi cge:100689433.

Organism-specific databases

CTDi 5034.

Phylogenomic databases

HOVERGENi HBG005920.
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. "Protein-disulfide isomerase is a component of an NBD-cholesterol monomerizing protein complex from hamster small intestine."
    Cai T.-Q., Guo Q., Wong B., Milot D., Zhang L., Wright S.D.
    Biochim. Biophys. Acta 1581:100-108(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Small intestine.

Entry informationi

Entry nameiPDIA1_CRIGR
AccessioniPrimary (citable) accession number: Q8R4U2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: June 1, 2002
Last modified: October 29, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3