Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5R5B6

- PDIA1_PONAB

UniProt

Q5R5B6 - PDIA1_PONAB

Protein

Protein disulfide-isomerase

Gene

P4HB

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei53 – 531NucleophileBy similarity
    Sitei54 – 541Contributes to redox potential valueBy similarity
    Sitei55 – 551Contributes to redox potential valueBy similarity
    Active sitei56 – 561NucleophileBy similarity
    Sitei120 – 1201Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei397 – 3971NucleophileBy similarity
    Sitei398 – 3981Contributes to redox potential valueBy similarity
    Sitei399 – 3991Contributes to redox potential valueBy similarity
    Active sitei400 – 4001NucleophileBy similarity
    Sitei461 – 4611Lowers 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

    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 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 lumen Source: UniProtKB-SubCell
    2. melanosome Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717By similarityAdd
    BLAST
    Chaini18 – 508491Protein disulfide-isomerasePRO_0000034197Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi53 ↔ 56Redox-activePROSITE-ProRule annotation
    Modified residuei200 – 2001N6-acetyllysineBy similarity
    Modified residuei222 – 2221N6-succinyllysineBy similarity
    Modified residuei271 – 2711N6-succinyllysineBy similarity
    Disulfide bondi397 ↔ 400Redox-activePROSITE-ProRule annotation

    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.By similarity

    Structurei

    3D structure databases

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 134117Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini349 – 475127Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi505 – 5084Prevents secretion from ERPROSITE-ProRule annotation

    Compositional bias

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

    « Hide

    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: October 1, 2014
    This is version 74 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