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P52555

- ERP29_RAT

UniProt

P52555 - ERP29_RAT

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Protein

Endoplasmic reticulum resident protein 29

Gene

Erp29

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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 - 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
Complete GO annotation...

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. smooth endoplasmic reticulum Source: UniProtKB
  4. transport vesicle Source: RGD
Complete GO annotation...

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Phosphotyrosine; by PKDCCBy similarity
Modified residuei66 – 661Phosphotyrosine; by PKDCCBy similarity

Keywords - PTMi

Phosphoprotein

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 – 383Combined sources
Helixi43 – 497Combined sources
Helixi50 – 523Combined sources
Beta strandi53 – 619Combined sources
Turni67 – 704Combined sources
Helixi71 – 799Combined sources
Helixi80 – 823Combined sources
Beta strandi84 – 9310Combined sources
Helixi100 – 1089Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi116 – 1249Combined sources
Beta strandi130 – 1345Combined sources
Helixi138 – 1469Combined sources
Helixi160 – 17011Combined sources
Helixi174 – 18714Combined sources
Turni188 – 1903Combined sources
Turni193 – 1953Combined sources
Helixi196 – 21116Combined sources
Helixi215 – 22915Combined sources
Turni234 – 2363Combined sources
Helixi237 – 24913Combined sources
Beta strandi252 – 2543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MAAAVPGAVS LSPLLSVLLG LLLLSAPHGA SGLHTKGALP LDTVTFYKVI
60 70 80 90 100
PKSKFVLVKF DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL
110 120 130 140 150
NMELSEKYKL DKESYPVFYL FRDGDFENPV PYSGAVKVGA IQRWLKGQGV
160 170 180 190 200
YLGMPGCLPA YDALAGQFIE ASSREARQAI LKQGQDGLSG VKETDKKWAS
210 220 230 240 250
QYLKIMGKIL DQGEDFPASE LARISKLIEN KMSEGKKEEL QRSLNILTAF
260
RKKGAEKEEL
Length:260
Mass (Da):28,575
Last modified:November 1, 1997 - v2
Checksum:i8D9EBAA756ED6CA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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 29, 2014
This is version 130 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