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Q2HWU2

- PDIA1_MACFU

UniProt

Q2HWU2 - PDIA1_MACFU

Protein

Protein disulfide-isomerase

Gene

P4HB

Organism
Macaca fuscata fuscata (Japanese macaque)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (21 Mar 2006)
      Previous versions | rss
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    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

    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
    Gene namesi
    Name:P4HB
    Synonyms:PDI, PDIA1
    OrganismiMacaca fuscata fuscata (Japanese macaque)
    Taxonomic identifieri9543 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

    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: MGI
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    3. melanosome Source: UniProtKB-SubCell
    4. 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 – 1919By similarityAdd
    BLAST
    Chaini20 – 510491Protein disulfide-isomerasePRO_0000246155Add
    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

    PRIDEiQ2HWU2.

    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

    ProteinModelPortaliQ2HWU2.
    SMRiQ2HWU2. Positions 20-359, 370-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 136117Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini351 – 477127Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi507 – 5104Prevents secretion from ERPROSITE-ProRule annotation

    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.

    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.

    Q2HWU2-1 [UniParc]FASTAAdd to Basket

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    MLRRALLCLA VAAAPGLYAD APEEEDHVLV LRKSNFAEAL AAHKYLLVEF    50
    YAPWCGHCKA LAPEYAKAAG KLKAEGSEIR LAKVDATEES DLAQQYGVRG 100
    YPTIKFFRNG DTASPKEYTA GREADDIVNW LKKRTGPAAT TLPDGAAAES 150
    LVESSEVAVI GFFKDVESDS AKQFLQAAEA IDDIPFGITS NSDVFSKYQL 200
    DKDGVVLFKK FDEGRNNFEG EVTKENLLDF IKYNQLPLVI EFTEQTAPKI 250
    FGGEIKTHIL LFLPKSVSDY DGKLSNFKTA AESFKGKILF IFIDSDHTDN 300
    QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAER ITEFCHRFLE 350
    GKIKPHLMSQ ELPEDWDKQP VKVLVGKNFE EVAFDENKNV FVEFYAPWCG 400
    HCKQLAPIWD KLGETYKDHE NIVIAKMDST ANEVEAIKVH SFPTLKFFPA 450
    SVDRTVIDYN GERTLDGFKK FLESGGQDGA GDDDDLEDLE EAEEPDMEED 500
    DDQKAVKDEL 510
    Length:510
    Mass (Da):57,304
    Last modified:March 21, 2006 - v1
    Checksum:i5F917B017F418BE2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB232156 mRNA. Translation: BAE79726.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB232156 mRNA. Translation: BAE79726.1 .

    3D structure databases

    ProteinModelPortali Q2HWU2.
    SMRi Q2HWU2. Positions 20-359, 370-473.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q2HWU2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG005920.

    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. "Molecular cloning and gene expression of endoplasmic reticulum stress proteins in Japanese monkey, Macaca fuscata."
      Higashino A., Fukuhara R., Tezuka T., Kageyama T.
      J. Med. Primatol. 35:376-383(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiPDIA1_MACFU
    AccessioniPrimary (citable) accession number: Q2HWU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 58 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