Endoplasmic reticulum resident protein 29 precursor

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P52555 (ERP29_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Endoplasmic reticulum resident protein 29
Short name=ERp29

Alternative name(s):
Endoplasmic reticulum resident protein 31
Short name=ERp31

Gene names

Name:

Erp29

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	260 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 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.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Endoplasmic reticulum
Domain	Signal
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	intracellular protein transport Traceable author statement. Source: RGD protein folding Traceable author statement. Source: RGD protein secretion Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum lumen Traceable author statement. Source: RGD melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell transport vesicle Inferred from direct assay. Source: RGD
Molecular function	protein binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

Chain

33 – 260

228

Endoplasmic reticulum resident protein 29

PRO_0000021199

Regions

Motif

257 – 260

Prevents secretion from ER

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphotyrosine By similarity

Experimental info

Mutagenesis

157

C → S: Loss of function. Ref.8

Secondary structure

260

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P52555 [UniParc].

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

FASTA

260

28,575

        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' referencesShow '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: 9492298] [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: 9037184] [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: 15489334] [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, 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: 10727933] [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: 12475965] [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: 15572350] [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: 11435111] [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.

IPI

IPI00207184.

RefSeq

NP_446413.1. NM_053961.2.

UniGene

Rn.32904.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G7D	NMR	-	A	155-260	[»]
1G7E	NMR	-	A	33-154	[»]

ProteinModelPortal

P52555.

SMR

P52555. Positions 33-260.

ModBase

Search...

Protein-protein interaction databases

IntAct

P52555. 1 interaction.

STRING

P52555.

PTM databases

PhosphoSite

P52555.

2D gel databases

World-2DPAGE

0004:P52555.

Proteomic databases

PRIDE

P52555.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

117030.

KEGG

rno:117030.

UCSC

NM_053961. rat.

Organism-specific databases

CTD

10961.

RGD

619781. Erp29.

Phylogenomic databases

eggNOG

roNOG17758.

GeneTree

ENSGT00390000018566.

HOVERGEN

HBG051508.

InParanoid

P52555.

OMA

KIMGKVL.

OrthoDB

EOG45QHF1.

Gene expression databases

ArrayExpress

P52555.

Genevestigator

P52555.

GermOnline

ENSRNOG00000001348. Rattus norvegicus.

Family and domain databases

InterPro

IPR016855. ER_p29.
IPR011679. ER_p29_C.
IPR012883. ERp29_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1150.12. ERp29_C_type. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

K09586.

Pfam

PF07749. ERp29. 1 hit.
PF07912. ERp29_N. 1 hit.
[Graphical view]

PIRSF

PIRSF027352. ER_p29. 1 hit.

SUPFAM

SSF47933. ERP29_C. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS00014. ER_TARGET. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

619813.

Entry information

Entry name

ERP29_RAT

Accession

Primary (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:	December 14, 2011
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents