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Protein

Endoplasmic reticulum resident protein 29

Gene

Erp29

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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 - Molecular functioni

  • chaperone binding Source: ParkinsonsUK-UCL
  • protein homodimerization activity Source: ParkinsonsUK-UCL

GO - Biological processi

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
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi619781. Erp29.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: Ensembl
  • endoplasmic reticulum Source: RGD
  • endoplasmic reticulum lumen Source: RGD
  • extracellular exosome Source: Ensembl
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: Ensembl
  • smooth endoplasmic reticulum Source: UniProtKB
  • transport vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi157C → S: Loss of function. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Add BLAST32
ChainiPRO_000002119933 – 260Endoplasmic reticulum resident protein 29Add BLAST228

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei64Phosphotyrosine; by PKDCCBy similarity1
Modified residuei66Phosphotyrosine; by PKDCCBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP52555.
PRIDEiP52555.

2D gel databases

World-2DPAGE0004:P52555.

PTM databases

iPTMnetiP52555.
PhosphoSitePlusiP52555.

Expressioni

Tissue specificityi

Ubiquitous. Mostly expressed in secretory tissues.

Inductioni

By stress.

Gene expression databases

BgeeiENSRNOG00000001348.
GenevisibleiP52555. RN.

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.

GO - Molecular functioni

  • chaperone binding Source: ParkinsonsUK-UCL
  • protein homodimerization activity Source: ParkinsonsUK-UCL

Protein-protein interaction databases

IntActiP52555. 4 interactors.
MINTiMINT-4578045.
STRINGi10116.ENSRNOP00000001822.

Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 38Combined sources3
Helixi43 – 49Combined sources7
Helixi50 – 52Combined sources3
Beta strandi53 – 61Combined sources9
Turni67 – 70Combined sources4
Helixi71 – 79Combined sources9
Helixi80 – 82Combined sources3
Beta strandi84 – 93Combined sources10
Helixi100 – 108Combined sources9
Beta strandi111 – 114Combined sources4
Beta strandi116 – 124Combined sources9
Beta strandi130 – 134Combined sources5
Helixi138 – 146Combined sources9
Helixi160 – 170Combined sources11
Helixi174 – 187Combined sources14
Turni188 – 190Combined sources3
Turni193 – 195Combined sources3
Helixi196 – 211Combined sources16
Helixi215 – 229Combined sources15
Turni234 – 236Combined sources3
Helixi237 – 249Combined sources13
Beta strandi252 – 254Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G7DNMR-A155-260[»]
1G7ENMR-A33-154[»]
2M66NMR-A155-260[»]
ProteinModelPortaliP52555.
SMRiP52555.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52555.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi257 – 260Prevents secretion from ER4

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IX2F. Eukaryota.
ENOG4111I8S. LUCA.
GeneTreeiENSGT00390000018566.
HOGENOMiHOG000046371.
HOVERGENiHBG051508.
InParanoidiP52555.
KOiK09586.
OMAiDGCIKEF.
PhylomeDBiP52555.

Family and domain databases

CDDicd00238. ERp29c. 1 hit.
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.
ENSRNOT00000081016; ENSRNOP00000072413; 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.
RefSeqiNP_446413.1. NM_053961.2.
UniGeneiRn.32904.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G7DNMR-A155-260[»]
1G7ENMR-A33-154[»]
2M66NMR-A155-260[»]
ProteinModelPortaliP52555.
SMRiP52555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP52555. 4 interactors.
MINTiMINT-4578045.
STRINGi10116.ENSRNOP00000001822.

PTM databases

iPTMnetiP52555.
PhosphoSitePlusiP52555.

2D gel databases

World-2DPAGE0004:P52555.

Proteomic databases

PaxDbiP52555.
PRIDEiP52555.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001822; ENSRNOP00000001822; ENSRNOG00000001348.
ENSRNOT00000081016; ENSRNOP00000072413; ENSRNOG00000001348.
GeneIDi117030.
KEGGirno:117030.
UCSCiRGD:619781. rat.

Organism-specific databases

CTDi10961.
RGDi619781. Erp29.

Phylogenomic databases

eggNOGiENOG410IX2F. Eukaryota.
ENOG4111I8S. LUCA.
GeneTreeiENSGT00390000018566.
HOGENOMiHOG000046371.
HOVERGENiHBG051508.
InParanoidiP52555.
KOiK09586.
OMAiDGCIKEF.
PhylomeDBiP52555.

Miscellaneous databases

EvolutionaryTraceiP52555.
PROiP52555.

Gene expression databases

BgeeiENSRNOG00000001348.
GenevisibleiP52555. RN.

Family and domain databases

CDDicd00238. ERp29c. 1 hit.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 142 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.