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Protein

Protein disulfide-isomerase A4

Gene

Pdia4

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

Functioni

Catalytic activityi

Catalyzes the rearrangement of -S-S- bonds in proteins.

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. chaperone-mediated protein folding Source: UniProtKB
  3. response to endoplasmic reticulum stress Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BRENDAi5.3.4.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A4 (EC:5.3.4.1)
Alternative name(s):
Calcium-binding protein 2
Short name:
CaBP2
Endoplasmic reticulum resident protein 70
Short name:
ER protein 70
Short name:
ERp70
Endoplasmic reticulum resident protein 72
Short name:
ER protein 72
Short name:
ERp-72
Short name:
ERp72
Gene namesi
Name:Pdia4
Synonyms:Cabp2, Erp70
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619835. Pdia4.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  2. melanosome Source: UniProtKB-SubCell
  3. smooth endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 643623Protein disulfide-isomerase A4PRO_0000034231Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi89 ↔ 92Redox-activePROSITE-ProRule annotation
Disulfide bondi204 ↔ 207Redox-activePROSITE-ProRule annotation
Modified residuei364 – 3641N6-acetyllysineBy similarity
Disulfide bondi553 ↔ 556Redox-activePROSITE-ProRule annotation

Post-translational modificationi

O-glycosylated.

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP38659.
PRIDEiP38659.

Expressioni

Inductioni

Upon glucose starvation, as well as treatment with tunicamycin.

Gene expression databases

GenevestigatoriP38659.

Interactioni

Subunit structurei

Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.

Binary interactionsi

WithEntry#Exp.IntActNotes
Dmel_CG7484Q9VVJ72EBI-917435,EBI-128899From a different organism.
PpibP243682EBI-917435,EBI-916926
TgP068823EBI-917435,EBI-1549657

Protein-protein interaction databases

BioGridi250512. 5 interactions.
IntActiP38659. 10 interactions.
MINTiMINT-4565672.
STRINGi10116.ENSRNOP00000008728.

Structurei

Secondary structure

1
643
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi284 – 2874Combined sources
Helixi291 – 30010Combined sources
Beta strandi305 – 3095Combined sources
Helixi316 – 32813Combined sources
Turni329 – 3313Combined sources
Beta strandi334 – 3374Combined sources
Helixi340 – 3467Combined sources
Beta strandi350 – 3567Combined sources
Helixi359 – 3613Combined sources
Beta strandi370 – 3734Combined sources
Helixi380 – 39011Combined sources
Beta strandi395 – 3984Combined sources
Turni400 – 4023Combined sources
Helixi403 – 4064Combined sources
Beta strandi409 – 4179Combined sources
Turni423 – 4253Combined sources
Helixi426 – 44015Combined sources
Beta strandi446 – 4527Combined sources
Turni453 – 4564Combined sources
Helixi457 – 4626Combined sources
Beta strandi473 – 4775Combined sources
Beta strandi483 – 4853Combined sources
Helixi493 – 50412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EC3X-ray1.92A/B283-523[»]
ProteinModelPortaliP38659.
SMRiP38659. Positions 54-282, 521-643.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38659.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 167147Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini167 – 299133Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST
Domaini503 – 634132Thioredoxin 3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi640 – 6434Prevents secretion from ER

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 3 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP38659.
KOiK09582.
PhylomeDBiP38659.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFiPIRSF036862. Disulphide_isom_A4. 1 hit.
SUPFAMiSSF52833. SSF52833. 5 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38659-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLRKAWLLV LLLALTQLLA AASAEDAHED ASDSENPIED DDDEEEDEED
60 70 80 90 100
EDDLEVKEEN GVWVLNDENF DNFVADKDTV LLEFYAPWCG HCKQFAPEYE
110 120 130 140 150
KIASTLKDND PPIAVAKIDA TSASMLASKF DVSGYPTIKI LKKGQAVDYD
160 170 180 190 200
GSRTQEEIVA KVREVSQPDW TPPPEVTLTL TKENFDDVVN NADIILVEFY
210 220 230 240 250
APWCGHCKKL APEYEKAAKE LSKRSPPIPL AKVDATEQTD LAKRFDVSGY
260 270 280 290 300
PTLKIFRKGR PFDYNGPREK YGIVDYMVEQ SGPPSKEILT LKQVQEFLKD
310 320 330 340 350
GDDVVILGVF QGVGDPGYLQ YQDAANTLRE DYKFHHTFST EIAKFLKVSL
360 370 380 390 400
GKLVLMQPEK FQSKYEPRMH VMDVQGSTEA SAIKDYVVKH ALPLVGHRKT
410 420 430 440 450
SNDAKRYSKR PLVVVYYSVD FSFDYRTATQ FWRNKVLEVA KDFPEYTFAI
460 470 480 490 500
ADEEDYATEV KDLGLSESGE DVNAAILDES GKKFAMEPEE FDSDALQEFV
510 520 530 540 550
MAFKKGKLKP VIKSQPVPKN NKGPVRVVVG KTFDAIVMDP KKDVLIEFYA
560 570 580 590 600
PWCGHCKQLE PVYTSLGKKY KGQKDLVIAK MDATANDITN DRYKVEGFPT
610 620 630 640
IYFAPSGDKK NPIKFEGGNR DLEHLSKFID EHATKRSRTK EEL
Length:643
Mass (Da):72,720
Last modified:October 25, 2005 - v2
Checksum:iC5BC8536834543ED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431D → E in AAA19217 (PubMed:8477750).Curated
Sequence conflicti391 – 3911A → D in AAA19217 (PubMed:8477750).Curated
Sequence conflicti497 – 4971Q → R in AAA19217 (PubMed:8477750).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86870 mRNA. Translation: AAA19217.1.
BC061535 mRNA. Translation: AAH61535.1.
PIRiS32476.
RefSeqiNP_446301.1. NM_053849.1.
UniGeneiRn.39305.

Genome annotation databases

GeneIDi116598.
KEGGirno:116598.
UCSCiRGD:619835. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86870 mRNA. Translation: AAA19217.1.
BC061535 mRNA. Translation: AAH61535.1.
PIRiS32476.
RefSeqiNP_446301.1. NM_053849.1.
UniGeneiRn.39305.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EC3X-ray1.92A/B283-523[»]
ProteinModelPortaliP38659.
SMRiP38659. Positions 54-282, 521-643.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250512. 5 interactions.
IntActiP38659. 10 interactions.
MINTiMINT-4565672.
STRINGi10116.ENSRNOP00000008728.

Proteomic databases

PaxDbiP38659.
PRIDEiP38659.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi116598.
KEGGirno:116598.
UCSCiRGD:619835. rat.

Organism-specific databases

CTDi9601.
RGDi619835. Pdia4.

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP38659.
KOiK09582.
PhylomeDBiP38659.

Enzyme and pathway databases

BRENDAi5.3.4.1. 5301.

Miscellaneous databases

EvolutionaryTraceiP38659.
NextBioi619299.
PROiP38659.

Gene expression databases

GenevestigatoriP38659.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFiPIRSF036862. Disulphide_isom_A4. 1 hit.
SUPFAMiSSF52833. SSF52833. 5 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase activity."
    Van P.N., Rupp K., Lampen A., Soeling H.-D.
    Eur. J. Biochem. 213:789-795(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  2. "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: Pituitary.
  3. "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.

Entry informationi

Entry nameiPDIA4_RAT
AccessioniPrimary (citable) accession number: P38659
Secondary accession number(s): Q6P7S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 25, 2005
Last modified: April 29, 2015
This is version 136 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.