Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P52555 (ERP29_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoplasmic reticulum resident protein 29

Short name=ERp29
Alternative name(s):
Endoplasmic reticulum resident protein 31
Short name=ERp31
Gene names
Name:Erp29
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.9

Subcellular location

Endoplasmic reticulum lumen. Melanosome By similarity.

Tissue specificity

Ubiquitous. Mostly expressed in secretory tissues.

Induction

By stress.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERP29P300402EBI-917740,EBI-8762218From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232
Chain33 – 260228Endoplasmic reticulum resident protein 29
PRO_0000021199

Regions

Motif257 – 2604Prevents secretion from ER

Experimental info

Mutagenesis1571C → S: Loss of function. Ref.8

Secondary structure

...................................... 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52555 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 8D9EBAA756ED6CA2

FASTA26028,575
        10         20         30         40         50         60 
MAAAVPGAVS LSPLLSVLLG LLLLSAPHGA SGLHTKGALP LDTVTFYKVI PKSKFVLVKF 

        70         80         90        100        110        120 
DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL NMELSEKYKL DKESYPVFYL 

       130        140        150        160        170        180 
FRDGDFENPV PYSGAVKVGA IQRWLKGQGV YLGMPGCLPA YDALAGQFIE ASSREARQAI 

       190        200        210        220        230        240 
LKQGQDGLSG VKETDKKWAS QYLKIMGKIL DQGEDFPASE LARISKLIEN KMSEGKKEEL 

       250        260 
QRSLNILTAF RKKGAEKEEL 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U36482 mRNA. Translation: AAC15239.1.
Y10264 mRNA. Translation: CAA71313.1.
AY004254 Genomic DNA. Translation: AAF93170.1.
BC091129 mRNA. Translation: AAH91129.1.
RefSeqNP_446413.1. NM_053961.2.
UniGeneRn.32904.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G7DNMR-A155-260[»]
1G7ENMR-A33-154[»]
2M66NMR-A155-260[»]
ProteinModelPortalP52555.
SMRP52555. Positions 33-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP52555. 4 interactions.
MINTMINT-4578045.

PTM databases

PhosphoSiteP52555.

2D gel databases

World-2DPAGE0004:P52555.

Proteomic databases

PaxDbP52555.
PRIDEP52555.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001822; ENSRNOP00000001822; ENSRNOG00000001348.
GeneID117030.
KEGGrno:117030.
UCSCRGD:619781. rat.

Organism-specific databases

CTD10961.
RGD619781. Erp29.

Phylogenomic databases

eggNOGNOG82861.
GeneTreeENSGT00390000018566.
HOGENOMHOG000046371.
HOVERGENHBG051508.
InParanoidP52555.
KOK09586.
OMAPYGEKHE.
OrthoDBEOG7XH6RH.
PhylomeDBP52555.

Gene expression databases

GenevestigatorP52555.

Family and domain databases

Gene3D1.20.1150.12. 1 hit.
3.40.30.10. 1 hit.
InterProIPR016855. ER_p29.
IPR011679. ER_p29_C.
IPR012883. ERp29_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF07749. ERp29. 1 hit.
PF07912. ERp29_N. 1 hit.
[Graphical view]
PIRSFPIRSF027352. ER_p29. 1 hit.
SUPFAMSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52555.
NextBio619813.
PROP52555.

Entry information

Entry nameERP29_RAT
AccessionPrimary (citable) accession number: P52555
Secondary accession number(s): P80749, Q5BKC2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references