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P52555

- ERP29_RAT

UniProt

P52555 - ERP29_RAT

Protein

Endoplasmic reticulum resident protein 29

Gene

Erp29

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. intracellular protein transport Source: RGD
    2. protein folding Source: RGD
    3. protein secretion Source: InterPro
    4. response to stress Source: UniProtKB-KW

    Keywords - Biological processi

    Stress response

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmic reticulum resident protein 29
    Short name:
    ERp29
    Alternative name(s):
    Endoplasmic reticulum resident protein 31
    Short name:
    ERp31
    Gene namesi
    Name:Erp29
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 12

    Organism-specific databases

    RGDi619781. Erp29.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: RGD
    2. endoplasmic reticulum lumen Source: RGD
    3. melanosome Source: UniProtKB-SubCell
    4. smooth endoplasmic reticulum Source: UniProtKB
    5. transport vesicle Source: RGD

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi157 – 1571C → S: Loss of function. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Add
    BLAST
    Chaini33 – 260228Endoplasmic reticulum resident protein 29PRO_0000021199Add
    BLAST

    Proteomic databases

    PaxDbiP52555.
    PRIDEiP52555.

    2D gel databases

    World-2DPAGE0004:P52555.

    PTM databases

    PhosphoSiteiP52555.

    Expressioni

    Tissue specificityi

    Ubiquitous. Mostly expressed in secretory tissues.

    Inductioni

    By stress.

    Gene expression databases

    GenevestigatoriP52555.

    Interactioni

    Subunit structurei

    Homodimer. Part of a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERP29P300402EBI-917740,EBI-8762218From a different organism.

    Protein-protein interaction databases

    IntActiP52555. 4 interactions.
    MINTiMINT-4578045.

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 383
    Helixi43 – 497
    Helixi50 – 523
    Beta strandi53 – 619
    Turni67 – 704
    Helixi71 – 799
    Helixi80 – 823
    Beta strandi84 – 9310
    Helixi100 – 1089
    Beta strandi111 – 1144
    Beta strandi116 – 1249
    Beta strandi130 – 1345
    Helixi138 – 1469
    Helixi160 – 17011
    Helixi174 – 18714
    Turni188 – 1903
    Turni193 – 1953
    Helixi196 – 21116
    Helixi215 – 22915
    Turni234 – 2363
    Helixi237 – 24913
    Beta strandi252 – 2543

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G7DNMR-A155-260[»]
    1G7ENMR-A33-154[»]
    2M66NMR-A155-260[»]
    ProteinModelPortaliP52555.
    SMRiP52555. Positions 33-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52555.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi257 – 2604Prevents secretion from ER

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG82861.
    GeneTreeiENSGT00390000018566.
    HOGENOMiHOG000046371.
    HOVERGENiHBG051508.
    InParanoidiP52555.
    KOiK09586.
    OMAiPYGEKHE.
    OrthoDBiEOG7XH6RH.
    PhylomeDBiP52555.

    Family and domain databases

    Gene3Di1.20.1150.12. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR016855. ER_p29.
    IPR011679. ER_p29_C.
    IPR012883. ERp29_N.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF07749. ERp29. 1 hit.
    PF07912. ERp29_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF027352. ER_p29. 1 hit.
    SUPFAMiSSF47933. SSF47933. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P52555-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAVPGAVS LSPLLSVLLG LLLLSAPHGA SGLHTKGALP LDTVTFYKVI    50
    PKSKFVLVKF DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL 100
    NMELSEKYKL DKESYPVFYL FRDGDFENPV PYSGAVKVGA IQRWLKGQGV 150
    YLGMPGCLPA YDALAGQFIE ASSREARQAI LKQGQDGLSG VKETDKKWAS 200
    QYLKIMGKIL DQGEDFPASE LARISKLIEN KMSEGKKEEL QRSLNILTAF 250
    RKKGAEKEEL 260
    Length:260
    Mass (Da):28,575
    Last modified:November 1, 1997 - v2
    Checksum:i8D9EBAA756ED6CA2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U36482 mRNA. Translation: AAC15239.1.
    Y10264 mRNA. Translation: CAA71313.1.
    AY004254 Genomic DNA. Translation: AAF93170.1.
    BC091129 mRNA. Translation: AAH91129.1.
    RefSeqiNP_446413.1. NM_053961.2.
    UniGeneiRn.32904.

    Genome annotation databases

    EnsembliENSRNOT00000001822; ENSRNOP00000001822; ENSRNOG00000001348.
    GeneIDi117030.
    KEGGirno:117030.
    UCSCiRGD:619781. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U36482 mRNA. Translation: AAC15239.1 .
    Y10264 mRNA. Translation: CAA71313.1 .
    AY004254 Genomic DNA. Translation: AAF93170.1 .
    BC091129 mRNA. Translation: AAH91129.1 .
    RefSeqi NP_446413.1. NM_053961.2.
    UniGenei Rn.32904.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G7D NMR - A 155-260 [» ]
    1G7E NMR - A 33-154 [» ]
    2M66 NMR - A 155-260 [» ]
    ProteinModelPortali P52555.
    SMRi P52555. Positions 33-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P52555. 4 interactions.
    MINTi MINT-4578045.

    PTM databases

    PhosphoSitei P52555.

    2D gel databases

    World-2DPAGE 0004:P52555.

    Proteomic databases

    PaxDbi P52555.
    PRIDEi P52555.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000001822 ; ENSRNOP00000001822 ; ENSRNOG00000001348 .
    GeneIDi 117030.
    KEGGi rno:117030.
    UCSCi RGD:619781. rat.

    Organism-specific databases

    CTDi 10961.
    RGDi 619781. Erp29.

    Phylogenomic databases

    eggNOGi NOG82861.
    GeneTreei ENSGT00390000018566.
    HOGENOMi HOG000046371.
    HOVERGENi HBG051508.
    InParanoidi P52555.
    KOi K09586.
    OMAi PYGEKHE.
    OrthoDBi EOG7XH6RH.
    PhylomeDBi P52555.

    Miscellaneous databases

    EvolutionaryTracei P52555.
    NextBioi 619813.
    PROi P52555.

    Gene expression databases

    Genevestigatori P52555.

    Family and domain databases

    Gene3Di 1.20.1150.12. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR016855. ER_p29.
    IPR011679. ER_p29_C.
    IPR012883. ERp29_N.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF07749. ERp29. 1 hit.
    PF07912. ERp29_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF027352. ER_p29. 1 hit.
    SUPFAMi SSF47933. SSF47933. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A stress-inducible rat liver endoplasmic reticulum protein, ERp29."
      Mkrtchian S., Fang C., Hellman U., Ingelman-Sundberg M.
      Eur. J. Biochem. 251:304-313(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum."
      Demmer J., Zhou C.M., Hubbard M.J.
      FEBS Lett. 402:145-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: Wistar.
      Tissue: Enamel epithelium and Liver.
    3. "Genomic organization of the gene encoding rat endoplasmic reticulum protein ERp29."
      Mkrtchian S., Baryshev M., Sharipo A., Ingelman-Sundberg M.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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: Ovary.
    5. Lubec G., Chen W.-Q., Afjehi-Sadat L.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 113-122 AND 209-223, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus and Spinal cord.
    6. "Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells evidence for a unique role in secretory-protein synthesis."
      Hubbard M.J., McHugh N.J., Carne D.L.
      Eur. J. Biochem. 267:1945-1957(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
      Tissue: Dental pulp and Enamel epithelium.
    7. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
      Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
      Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPONENT OF A CHAPERONE COMPLEX.
    8. "Biophysical characterization of ERp29: evidence for a key structural role of cysteine-125."
      Hermann V.M., Cutfield J.F., Hubbard M.J.
      J. Biol. Chem. 280:13529-13537(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-157.
    9. "Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer."
      Liepinsh E., Baryshev M., Sharipo A., Ingelman-Sundberg M., Otting G., Mkrtchian S.
      Structure 9:457-471(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 33-260, SUBUNIT.

    Entry informationi

    Entry nameiERP29_RAT
    AccessioniPrimary (citable) accession number: P52555
    Secondary accession number(s): P80749, Q5BKC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3