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P38659

- PDIA4_RAT

UniProt

P38659 - PDIA4_RAT

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Protein

Protein disulfide-isomerase A4

Gene
Pdia4, Cabp2, Erp70
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 binding Source: IntAct
  2. protein disulfide isomerase activity Source: UniProt

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Calcium

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: 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 – 2020 Reviewed predictionAdd
BLAST
Chaini21 – 643623Protein disulfide-isomerase A4PRO_0000034231Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi89 ↔ 92Redox-active By similarity
Disulfide bondi204 ↔ 207Redox-active By similarity
Modified residuei364 – 3641N6-acetyllysine By similarity
Disulfide bondi553 ↔ 556Redox-active By similarity

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 – 2874
Helixi291 – 30010
Beta strandi305 – 3095
Helixi316 – 32813
Turni329 – 3313
Beta strandi334 – 3374
Helixi340 – 3467
Beta strandi350 – 3567
Helixi359 – 3613
Beta strandi370 – 3734
Helixi380 – 39011
Beta strandi395 – 3984
Turni400 – 4023
Helixi403 – 4064
Beta strandi409 – 4179
Turni423 – 4253
Helixi426 – 44015
Beta strandi446 – 4527
Turni453 – 4564
Helixi457 – 4626
Beta strandi473 – 4775
Beta strandi483 – 4853
Helixi493 – 50412

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP38659.

Family & Domainsi

Domains and Repeats

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

Motif

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

Sequence similaritiesi

Contains 3 thioredoxin domains.

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

MKLRKAWLLV LLLALTQLLA AASAEDAHED ASDSENPIED DDDEEEDEED    50
EDDLEVKEEN GVWVLNDENF DNFVADKDTV LLEFYAPWCG HCKQFAPEYE 100
KIASTLKDND PPIAVAKIDA TSASMLASKF DVSGYPTIKI LKKGQAVDYD 150
GSRTQEEIVA KVREVSQPDW TPPPEVTLTL TKENFDDVVN NADIILVEFY 200
APWCGHCKKL APEYEKAAKE LSKRSPPIPL AKVDATEQTD LAKRFDVSGY 250
PTLKIFRKGR PFDYNGPREK YGIVDYMVEQ SGPPSKEILT LKQVQEFLKD 300
GDDVVILGVF QGVGDPGYLQ YQDAANTLRE DYKFHHTFST EIAKFLKVSL 350
GKLVLMQPEK FQSKYEPRMH VMDVQGSTEA SAIKDYVVKH ALPLVGHRKT 400
SNDAKRYSKR PLVVVYYSVD FSFDYRTATQ FWRNKVLEVA KDFPEYTFAI 450
ADEEDYATEV KDLGLSESGE DVNAAILDES GKKFAMEPEE FDSDALQEFV 500
MAFKKGKLKP VIKSQPVPKN NKGPVRVVVG KTFDAIVMDP KKDVLIEFYA 550
PWCGHCKQLE PVYTSLGKKY KGQKDLVIAK MDATANDITN DRYKVEGFPT 600
IYFAPSGDKK NPIKFEGGNR DLEHLSKFID EHATKRSRTK EEL 643
Length:643
Mass (Da):72,720
Last modified:October 25, 2005 - v2
Checksum:iC5BC8536834543ED
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431D → E in AAA19217. 1 Publication
Sequence conflicti391 – 3911A → D in AAA19217. 1 Publication
Sequence conflicti497 – 4971Q → R in AAA19217. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M86870 mRNA. Translation: AAA19217.1 .
BC061535 mRNA. Translation: AAH61535.1 .
PIRi S32476.
RefSeqi NP_446301.1. NM_053849.1.
UniGenei Rn.39305.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3EC3 X-ray 1.92 A/B 283-523 [» ]
ProteinModelPortali P38659.
SMRi P38659. Positions 54-282, 521-643.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 250512. 5 interactions.
IntActi P38659. 10 interactions.
MINTi MINT-4565672.
STRINGi 10116.ENSRNOP00000008728.

Proteomic databases

PaxDbi P38659.
PRIDEi P38659.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 116598.
KEGGi rno:116598.
UCSCi RGD:619835. rat.

Organism-specific databases

CTDi 9601.
RGDi 619835. Pdia4.

Phylogenomic databases

eggNOGi COG0526.
HOGENOMi HOG000162459.
HOVERGENi HBG005920.
InParanoidi P38659.
KOi K09582.
PhylomeDBi P38659.

Miscellaneous databases

EvolutionaryTracei P38659.
NextBioi 619299.

Gene expression databases

Genevestigatori P38659.

Family and domain databases

Gene3Di 3.40.30.10. 4 hits.
InterProi IPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 3 hits.
[Graphical view ]
PIRSFi PIRSF036862. Disulphide_isom_A4. 1 hit.
SUPFAMi SSF52833. SSF52833. 5 hits.
TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 128 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

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