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Q5I0H9

- PDIA5_RAT

UniProt

Q5I0H9 - PDIA5_RAT

Protein

Protein disulfide-isomerase A5

Gene

Pdia5

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. protein disulfide isomerase activity Source: RefGenome

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. protein folding Source: RefGenome
    3. response to endoplasmic reticulum stress Source: RefGenome

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    ReactomeiREACT_93415. XBP1(S) activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase A5 (EC:5.3.4.1)
    Gene namesi
    Name:Pdia5
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi1359236. Pdia5.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: RefGenome
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 517496Protein disulfide-isomerase A5PRO_0000034235Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi180 ↔ 183Redox-activePROSITE-ProRule annotation
    Disulfide bondi303 ↔ 306Redox-activePROSITE-ProRule annotation
    Disulfide bondi424 ↔ 427Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ5I0H9.
    PRIDEiQ5I0H9.

    Expressioni

    Gene expression databases

    GenevestigatoriQ5I0H9.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-4573704.
    STRINGi10116.ENSRNOP00000059945.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5I0H9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini132 – 259128Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini268 – 382115Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini376 – 504129Thioredoxin 3PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi514 – 5174Prevents secretion from ERSequence Analysis

    Sequence similaritiesi

    Belongs to the protein disulfide isomerase family.Curated
    Contains 3 thioredoxin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG0526.
    HOGENOMiHOG000039967.
    HOVERGENiHBG053547.
    InParanoidiQ5I0H9.
    KOiK09583.
    OrthoDBiEOG74TWZ6.
    PhylomeDBiQ5I0H9.
    TreeFamiTF106379.

    Family and domain databases

    Gene3Di3.40.30.10. 4 hits.
    InterProiIPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 3 hits.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 4 hits.
    PROSITEiPS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5I0H9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARAWGLLLA IGVILPTWLS STKVSSLIER ISDPKDLKKL LRTRNNVLVL    50
    YSESEVAAES HLKLLSTVAQ AVKGQGTICW VDCGDAESRK LCKKMKVDLS 100
    PKDKKIELFH YQDGAFHMQY DRAVTLKSIV AFLKDPKGPP LWEEDPGAKD 150
    VVHIDSEKDF RRLLKKEEKP LLMMFYAPWC SMCKRIMPHF QKAATQVRGH 200
    TVLAGMNVYP PEFENIKEEY NVRGYPTICY FEKGRFLFQY ENYGSTAEDI 250
    VEWLKNPQPP QPQVPETPWA DEGGSVYHLT DEDFDQFVKE HSSVLVMFHA 300
    PWCGHCKKMK PEFESAAEVL HGDAESSGVL AAVDATINEA LAERFHISAF 350
    PTLKYFKNGE QQAVPALRTK KKFIEWMQNP EAPPPPEPTW EEQQTSVLHL 400
    VGDNFRETLK KKKHTLVMFY APWCPHCKKV IPHFTATADA FKDDRKIACA 450
    AVDCVKDKNQ DLCQQESVKA YPTFHYYHYG KLVEKYESDR TELGFTSFIR 500
    TLREGDLKRL EKRREDL 517
    Length:517
    Mass (Da):59,399
    Last modified:February 15, 2005 - v1
    Checksum:i038F0B07E1C15A0A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC088305 mRNA. Translation: AAH88305.1.
    RefSeqiNP_001014147.1. NM_001014125.1.
    UniGeneiRn.162053.

    Genome annotation databases

    GeneIDi360722.
    KEGGirno:360722.
    UCSCiRGD:1359236. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC088305 mRNA. Translation: AAH88305.1 .
    RefSeqi NP_001014147.1. NM_001014125.1.
    UniGenei Rn.162053.

    3D structure databases

    ProteinModelPortali Q5I0H9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4573704.
    STRINGi 10116.ENSRNOP00000059945.

    Proteomic databases

    PaxDbi Q5I0H9.
    PRIDEi Q5I0H9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 360722.
    KEGGi rno:360722.
    UCSCi RGD:1359236. rat.

    Organism-specific databases

    CTDi 10954.
    RGDi 1359236. Pdia5.

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000039967.
    HOVERGENi HBG053547.
    InParanoidi Q5I0H9.
    KOi K09583.
    OrthoDBi EOG74TWZ6.
    PhylomeDBi Q5I0H9.
    TreeFami TF106379.

    Enzyme and pathway databases

    Reactomei REACT_93415. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    NextBioi 673887.

    Gene expression databases

    Genevestigatori Q5I0H9.

    Family and domain databases

    Gene3Di 3.40.30.10. 4 hits.
    InterProi IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 3 hits.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 4 hits.
    PROSITEi PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.

    Entry informationi

    Entry nameiPDIA5_RAT
    AccessioniPrimary (citable) accession number: Q5I0H9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 81 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