P52555 (ERP29_RAT) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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 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.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Endoplasmic reticulum
Domain	Signal
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intracellular protein transport Traceable author statement PubMed 12039039. Source: RGD protein folding Traceable author statement PubMed 12039039. 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 PubMed 11884402. Source: RGD melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell transport vesicle Inferred from direct assay PubMed 11884402. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Chain

33 – 260

228

Endoplasmic reticulum resident protein 29

PRO_0000021199

Regions

Motif

257 – 260

4

Prevents secretion from ER

Experimental info

Mutagenesis

157

1

C → S: Loss of function. Ref.8

Secondary structure

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260

Helix Strand Turn

Details...

Beta strand

36 – 38

3

Helix

43 – 49

7

Helix

50 – 52

3

Beta strand

53 – 61

9

Turn

67 – 70

4

Helix

71 – 79

9

Helix

80 – 82

3

Beta strand

84 – 93

10

Helix

100 – 108

9

Beta strand

111 – 114

4

Beta strand

116 – 124

9

Beta strand

130 – 134

5

Helix

138 – 146

9

Helix

160 – 170

11

Helix

174 – 187

14

Turn

188 – 190

3

Turn

193 – 195

3

Helix

196 – 211

16

Helix

215 – 229

15

Turn

234 – 236

3

Helix

237 – 249

13

Beta strand

252 – 254

3

Sequences

	Sequence		Length	Mass (Da)
	P52555 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 8D9EBAA756ED6CA2	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

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] [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, 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.

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.

PTM databases

PhosphoSite

P52555.

2D gel databases

World-2DPAGE

0004:P52555.

Proteomic databases

PaxDb

P52555.

PRIDE

P52555.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000001822; ENSRNOP00000001822; ENSRNOG00000001348.

GeneID

117030.

KEGG

rno:117030.

UCSC

RGD:619781. rat.

Organism-specific databases

CTD

10961.

RGD

619781. Erp29.

Phylogenomic databases

eggNOG

NOG82861.

GeneTree

ENSGT00390000018566.

HOGENOM

HOG000046371.

HOVERGEN

HBG051508.

InParanoid

P52555.

KO

K09586.

OMA

TITFYKV.

OrthoDB

EOG45QHF1.

Gene expression databases

Genevestigator

P52555.

GermOnline

ENSRNOG00000001348. Rattus norvegicus.

Family and domain databases

Gene3D

1.20.1150.12. 1 hit.
3.40.30.10. 1 hit.

InterPro

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

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

EvolutionaryTrace

P52555.

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:	April 3, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program