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P21195

- PDIA1_RABIT

UniProt

P21195 - PDIA1_RABIT

Protein

Protein disulfide-isomerase

Gene

P4HB

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      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 sitei54 – 541NucleophileBy similarity
    Sitei55 – 551Contributes to redox potential valueBy similarity
    Sitei56 – 561Contributes to redox potential valueBy similarity
    Active sitei57 – 571NucleophileBy similarity
    Sitei121 – 1211Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei398 – 3981NucleophileBy similarity
    Sitei399 – 3991Contributes to redox potential valueBy similarity
    Sitei400 – 4001Contributes to redox potential valueBy similarity
    Active sitei401 – 4011NucleophileBy similarity
    Sitei462 – 4621Lowers 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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: 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 – 1818By similarityAdd
    BLAST
    Chaini19 – 509491Protein disulfide-isomerasePRO_0000034198Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 57Redox-activePROSITE-ProRule annotation
    Modified residuei223 – 2231N6-succinyllysineBy similarity
    Modified residuei272 – 2721N6-succinyllysineBy similarity
    Disulfide bondi398 ↔ 401Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP21195.

    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

    BioGridi1173214. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP21195.
    SMRiP21195. Positions 20-358, 369-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 135117Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini347 – 476130Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi506 – 5094Prevents 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

    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.

    P21195-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRRAVLCLA LAVTAGWAWA AEEEDNVLVL KSSNFAEELA AHKHLLVEFY    50
    APWCGHCKAL APEYAKAAGK LKAEGSDIRL AKVDATEESD LAQQYGVRGY 100
    PTIKFFKNGD TASPKEYTAG READDIVNWL KKRTGPAATT LADSAAAESL 150
    VESSEVAVIG FFKDVESDAA KQFLLAAEAT DDIPFGLTAS SDVFSRYQVH 200
    QDGVVLFKKF DEGRNNFEGE VTKEKLLDFI KHNQLPLVIE FTEQTAPKIF 250
    GGEIKTHILL FLPRSAADHD GKLSGFKQAA EGFKGKILFI FIDSDHADNQ 300
    RILEFFGLKK EECPAVRLIT LEEEMTKYKP ESDELTAEGI TEFCQRFLEG 350
    KIKPHLMSQE LPEDWDRQPV KVLVGKNFEE VAFDEKKNVF VEFYAPWCGH 400
    CKQLAPIWDK LGETYKEHQD IVIAKMDSTA NEVEAVKVHS FPTLKFFPAG 450
    PGRTVIDYNG ERTLDGFKKF LESGGQDGAG DEDGLEDLEE AEEPDLEEDD 500
    DQKAVRDEL 509
    Length:509
    Mass (Da):56,808
    Last modified:May 1, 1991 - v1
    Checksum:i093C8C18E209BAB5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05602 mRNA. Translation: AAA31476.1.
    PIRiA38362.
    RefSeqiNP_001164518.1. NM_001171047.1.
    UniGeneiOcu.5912.

    Genome annotation databases

    GeneIDi100328595.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05602 mRNA. Translation: AAA31476.1 .
    PIRi A38362.
    RefSeqi NP_001164518.1. NM_001171047.1.
    UniGenei Ocu.5912.

    3D structure databases

    ProteinModelPortali P21195.
    SMRi P21195. Positions 20-358, 369-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1173214. 2 interactions.

    Proteomic databases

    PRIDEi P21195.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100328595.

    Organism-specific databases

    CTDi 5034.

    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 of cDNA encoding a 55-kDa multifunctional thyroid hormone binding protein of skeletal muscle sarcoplasmic reticulum."
      Fliegel L., Newton E., Burns K., Michalak M.
      J. Biol. Chem. 265:15496-15502(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiPDIA1_RABIT
    AccessioniPrimary (citable) accession number: P21195
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 109 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