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Protein

Protein disulfide-isomerase

Gene

P4HB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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. procollagen-proline 4-dioxygenase activity Source: AgBase
  2. protein disulfide isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15199.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

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: AgBase
  2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  3. melanosome Source: UniProtKB-SubCell
  4. 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 – 20202 PublicationsAdd
BLAST
Chaini21 – 510490Protein disulfide-isomerasePRO_0000034193Add
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

PaxDbiP05307.
PRIDEiP05307.

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

Structurei

3D structure databases

ProteinModelPortaliP05307.
SMRiP05307. Positions 21-359, 370-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 136110Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini351 – 477127Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi507 – 5104Prevents secretion from ER

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

eggNOGiCOG0526.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP05307.
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.

P05307-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRRALLCLA LTALFRAGAG APDEEDHVLV LHKGNFDEAL AAHKYLLVEF
60 70 80 90 100
YAPWCGHCKA LAPEYAKAAG KLKAEGSEIR LAKVDATEES DLAQQYGVRG
110 120 130 140 150
YPTIKFFKNG DTASPKEYTA GREADDIVNW LKKRTGPAAS TLSDGAAAEA
160 170 180 190 200
LVESSEVAVI GFFKDMESDS AKQFFLAAEV IDDIPFGITS NSDVFSKYQL
210 220 230 240 250
DKDGVVLFKK FDEGRNNFEG EVTKEKLLDF IKHNQLPLVI EFTEQTAPKI
260 270 280 290 300
FGGEIKTHIL LFLPKSVSDY EGKLSNFKKA AESFKGKILF IFIDSDHTDN
310 320 330 340 350
QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE
360 370 380 390 400
GKIKPHLMSQ ELPDDWDKQP VKVLVGKNFE EVAFDEKKNV FVEFYAPWCG
410 420 430 440 450
HCKQLAPIWD KLGETYKDHE NIVIAKMDST ANEVEAVKVH SFPTLKFFPA
460 470 480 490 500
SADRTVIDYN GERTLDGFKK FLESGGQDGA GDDDDLEDLE EAEEPDLEED
510
DDQKAVKDEL
Length:510
Mass (Da):57,266
Last modified:November 1, 1988 - v1
Checksum:iF19BEC892E03C4CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17596 mRNA. Translation: AAA30690.1.
PIRiA26829. ISBOSS.
RefSeqiNP_776560.1. NM_174135.3.
UniGeneiBt.106831.

Genome annotation databases

GeneIDi281373.
KEGGibta:281373.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17596 mRNA. Translation: AAA30690.1.
PIRiA26829. ISBOSS.
RefSeqiNP_776560.1. NM_174135.3.
UniGeneiBt.106831.

3D structure databases

ProteinModelPortaliP05307.
SMRiP05307. Positions 21-359, 370-473.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiP05307.
PRIDEiP05307.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281373.
KEGGibta:281373.

Organism-specific databases

CTDi5034.

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP05307.
KOiK09580.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15199.

Miscellaneous databases

NextBioi20805377.

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]
ProtoNetiSearch...

Publicationsi

  1. "Sequence of membrane-associated thyroid hormone binding protein from bovine liver: its identity with protein disulphide isomerase."
    Yamauchi K., Yamamoto T., Hayashi H., Koya S., Takikawa H., Toyoshima K., Horiuchi R.
    Biochem. Biophys. Res. Commun. 146:1485-1492(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex."
    Wetterau J.R., Combs K.A., Spinner S.N., Joiner B.J.
    J. Biol. Chem. 265:9800-9807(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-45, INTERACTION WITH MTTP.
  3. Parkinson D.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 21-32.

Entry informationi

Entry nameiPDIA1_BOVIN
AccessioniPrimary (citable) accession number: P05307
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: January 7, 2015
This is version 128 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, Direct protein sequencing, Reference proteome

Documents

  1. 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.