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)

Q5RCH2

- PDIA2_PONAB

UniProt

Q5RCH2 - PDIA2_PONAB

Protein

Protein disulfide-isomerase A2

Gene

PDIA2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei71 – 711NucleophileBy similarity
    Sitei72 – 721Contributes to redox potential valueBy similarity
    Sitei73 – 731Contributes to redox potential valueBy similarity
    Active sitei74 – 741NucleophileBy similarity
    Sitei138 – 1381Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei418 – 4181NucleophileBy similarity
    Sitei419 – 4191Contributes to redox potential valueBy similarity
    Sitei420 – 4201Contributes to redox potential valueBy similarity
    Active sitei421 – 4211NucleophileBy similarity
    Sitei482 – 4821Lowers pKa of C-terminal Cys of second active siteBy similarity

    GO - Molecular functioni

    1. protein disulfide isomerase activity Source: UniProtKB-EC
    2. steroid binding Source: UniProtKB-KW

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro

    Keywords - Molecular functioni

    Chaperone, Isomerase

    Keywords - Ligandi

    Lipid-binding, Steroid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase A2 (EC:5.3.4.1)
    Gene namesi
    Name:PDIA2
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. 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 – 525504Protein disulfide-isomerase A2PRO_0000034223Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi18 – 18InterchainBy similarity
    Disulfide bondi71 ↔ 74Redox-activePROSITE-ProRule annotation
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi284 – 2841N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi418 ↔ 421Redox-activePROSITE-ProRule annotation
    Glycosylationi516 – 5161N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The disulfide-linked homodimer exhibits an enhanced chaperone activity.By similarity
    Glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer; predominantly as monomer under reducing conditions. Homodimer; disulfide-linked. Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5RCH2.
    SMRiQ5RCH2. Positions 389-492.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 152126Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini367 – 496130Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi522 – 5254Prevents 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.
    InParanoidiQ5RCH2.
    KOiK09581.

    Family and domain databases

    Gene3Di3.40.30.10. 4 hits.
    InterProiIPR005792. 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.
    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.

    Q5RCH2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSCQLLPVLL LLLLRASCPW GHEQGPRSPS EEPPEEEIPK EDGILVLSRH    50
    TLGLALREHP ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESSVVMLAKV 100
    DGPAQPELAE EFGVTEYPTL KFFRDGNRTH PEEYTGPREA EGIAEWLRRR 150
    VGPSAMRLED EAAAQALIDG RDLVVIGFFQ DLHDEDVATF LALAQDALDM 200
    TFGLTDRPQL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL GLDLGDLSRF 250
    LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLVGFGEA 300
    APHFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV 350
    DGGPVTTASI TAFCHAVLNG QVKPYLLSQE VPPDWDQRPV KTLVGKNFEQ 400
    VAFDETKNVF VKFYAPWCTH CKEMAPAWEA LAEKYQDHED VIIAELDATA 450
    NELDAFAVHG FPTLKYFPAG PGRKVIEYKS TRDLGTFSKF LDNGGVLPTE 500
    EPLEEPAAPF PEPPANSTMG SKEEL 525
    Length:525
    Mass (Da):58,124
    Last modified:December 21, 2004 - v1
    Checksum:i0C402549E70D3F32
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti342 – 3421E → G in CAH92649. 1 PublicationCurated
    Sequence conflicti485 – 4851G → E in CAH92649. 1 PublicationCurated
    Sequence conflicti505 – 5051E → G in CAH92649. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR858298 mRNA. Translation: CAH90535.1.
    CR860523 mRNA. Translation: CAH92649.1.
    RefSeqiNP_001125285.1. NM_001131813.1.
    UniGeneiPab.11836.
    Pab.19686.

    Genome annotation databases

    GeneIDi100172183.
    KEGGipon:100172183.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR858298 mRNA. Translation: CAH90535.1 .
    CR860523 mRNA. Translation: CAH92649.1 .
    RefSeqi NP_001125285.1. NM_001131813.1.
    UniGenei Pab.11836.
    Pab.19686.

    3D structure databases

    ProteinModelPortali Q5RCH2.
    SMRi Q5RCH2. Positions 389-492.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100172183.
    KEGGi pon:100172183.

    Organism-specific databases

    CTDi 64714.

    Phylogenomic databases

    HOVERGENi HBG005920.
    InParanoidi Q5RCH2.
    KOi K09581.

    Family and domain databases

    Gene3Di 3.40.30.10. 4 hits.
    InterProi 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.
    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: Heart.

    Entry informationi

    Entry nameiPDIA2_PONAB
    AccessioniPrimary (citable) accession number: Q5RCH2
    Secondary accession number(s): Q5R6G7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 71 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