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P08003

- PDIA4_MOUSE

UniProt

P08003 - PDIA4_MOUSE

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Protein

Protein disulfide-isomerase A4

Gene

Pdia4

Organism
Mus musculus (Mouse)
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. poly(A) RNA binding Source: Ensembl
  2. protein disulfide isomerase activity Source: UniProt

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A4 (EC:5.3.4.1)
Alternative name(s):
Endoplasmic reticulum resident protein 72
Short name:
ER protein 72
Short name:
ERp-72
Short name:
ERp72
Gene namesi
Name:Pdia4
Synonyms:Cai, Erp72
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:104864. Pdia4.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: MGI
  2. endoplasmic reticulum Source: MGI
  3. endoplasmic reticulum lumen Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 638618Protein disulfide-isomerase A4PRO_0000034230Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi84 ↔ 87Redox-activePROSITE-ProRule annotation
Disulfide bondi199 ↔ 202Redox-activePROSITE-ProRule annotation
Modified residuei359 – 3591N6-acetyllysineBy similarity
Disulfide bondi548 ↔ 551Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP08003.
PaxDbiP08003.
PRIDEiP08003.

PTM databases

PhosphoSiteiP08003.

Expressioni

Gene expression databases

BgeeiP08003.
CleanExiMM_PDIA4.
GenevestigatoriP08003.

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.

Protein-protein interaction databases

BioGridi198446. 1 interaction.
IntActiP08003. 5 interactions.
MINTiMINT-4106888.

Structurei

Secondary structure

1
638
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 543
Beta strandi57 – 593
Turni62 – 643
Helixi65 – 695
Beta strandi73 – 797
Helixi85 – 884
Helixi91 – 10212
Beta strandi103 – 1064
Beta strandi109 – 1135
Turni115 – 1173
Helixi119 – 1246
Beta strandi129 – 1379
Beta strandi140 – 1434
Helixi150 – 16112
Beta strandi162 – 1643
Beta strandi171 – 1733
Turni177 – 1793
Turni181 – 1833
Helixi184 – 1863
Beta strandi188 – 1958
Helixi200 – 21819
Beta strandi219 – 2213
Beta strandi225 – 2295
Turni230 – 2323
Helixi234 – 2396
Beta strandi244 – 25411
Beta strandi256 – 2583
Helixi265 – 27713
Beta strandi519 – 5224
Turni525 – 5273
Helixi528 – 5325
Beta strandi537 – 5437
Helixi550 – 56516
Beta strandi568 – 5769
Turni578 – 5803
Beta strandi591 – 5999
Helixi619 – 6279
Beta strandi628 – 6303

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJ1NMR-A46-172[»]
2DJ2NMR-A171-277[»]
2DJ3NMR-A519-638[»]
ProteinModelPortaliP08003.
SMRiP08003. Positions 47-507, 516-638.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08003.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 162142Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 294133Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST
Domaini498 – 629132Thioredoxin 3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi635 – 6384Prevents secretion from ER

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 5012Asp/Glu-rich (acidic)Add
BLAST

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.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP08003.
KOiK09582.
OrthoDBiEOG7VHSX1.
PhylomeDBiP08003.
TreeFamiTF106382.

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.

P08003-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLRKAWLLV LLLALTQLLA AASAGDAHED TSDTENATEE EEEEDDDDLE
60 70 80 90 100
VKEENGVWVL NDGNFDNFVA DKDTVLLEFY APWCGHCKQF APEYEKIAST
110 120 130 140 150
LKDNDPPIAV AKIDATSASM LASKFDVSGY PTIKILKKGQ AVDYDGSRTQ
160 170 180 190 200
EEIVAKVREV SQPDWTPPPE VTLSLTKDNF DDVVNNADII LVEFYAPWCG
210 220 230 240 250
HCKKLAPEYE KAAKELSKRS PPIPLAKVDA TEQTDLAKRF DVSGYPTLKI
260 270 280 290 300
FRKGRPFDYN GPREKYGIVD YMIEQSGPPS KEILTLKQVQ EFLKDGDDVV
310 320 330 340 350
IIGLFQGDGD PAYLQYQDAA NNLREDYKFH HTFSPEIAKF LKVSLGKLVL
360 370 380 390 400
THPEKFQSKY EPRFHVMDVQ GSTEASAIKD YVVKHALPLV GHRKTSNDAK
410 420 430 440 450
RYSKRPLVVV YYSVDFSFDY RAATQFWRNK VLEVAKDFPE YTFAIADEED
460 470 480 490 500
YATEVKDLGL SESGEDVNAA ILDESGKKFA MEPEEFDSDT LREFVTAFKK
510 520 530 540 550
GKLKPVIKSQ PVPKNNKGPV KVVVGKTFDA IVMDPKKDVL IEFYAPWCGH
560 570 580 590 600
CKQLEPIYTS LGKKYKGQKD LVIAKMDATA NDITNDQYKV EGFPTIYFAP
610 620 630
SGDKKNPIKF EGGNRDLEHL SKFIDEHATK RSRTKEEL
Length:638
Mass (Da):71,982
Last modified:November 30, 2010 - v3
Checksum:i2DDE2CE80BD77F6E
GO

Sequence cautioni

The sequence CAA68777.1 differs from that shown. Reason: Frameshift at position 544.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281H → Q in AAA39907. (PubMed:2295602)Curated
Sequence conflicti28 – 281H → Q in BAE27045. (PubMed:16141072)Curated
Sequence conflicti28 – 281H → Q in AAI41079. (PubMed:15489334)Curated
Sequence conflicti39 – 391E → EEEE in BAC25863. (PubMed:16141072)Curated
Sequence conflicti39 – 391E → EEEE in BAE41134. (PubMed:16141072)Curated
Sequence conflicti39 – 391E → EEEE in BAE36446. (PubMed:16141072)Curated
Sequence conflicti39 – 391E → EEEE in BAE29664. (PubMed:16141072)Curated
Sequence conflicti468 – 4681N → S in BAC25863. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05186 mRNA. Translation: AAA39907.1.
AK028292 mRNA. Translation: BAC25863.1.
AK146288 mRNA. Translation: BAE27045.1.
AK150566 mRNA. Translation: BAE29664.1.
AK161534 mRNA. Translation: BAE36446.1.
AK169387 mRNA. Translation: BAE41134.1.
BC066857 mRNA. Translation: AAH66857.1.
BC141078 mRNA. Translation: AAI41079.1.
Y00884 mRNA. Translation: CAA68777.1. Frameshift.
PIRiB34930. ISMSER.
S06318.
RefSeqiNP_033917.2. NM_009787.2.
UniGeneiMm.2442.

Genome annotation databases

EnsembliENSMUST00000077290; ENSMUSP00000076521; ENSMUSG00000025823.
GeneIDi12304.
KEGGimmu:12304.
UCSCiuc009btf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05186 mRNA. Translation: AAA39907.1 .
AK028292 mRNA. Translation: BAC25863.1 .
AK146288 mRNA. Translation: BAE27045.1 .
AK150566 mRNA. Translation: BAE29664.1 .
AK161534 mRNA. Translation: BAE36446.1 .
AK169387 mRNA. Translation: BAE41134.1 .
BC066857 mRNA. Translation: AAH66857.1 .
BC141078 mRNA. Translation: AAI41079.1 .
Y00884 mRNA. Translation: CAA68777.1 . Frameshift.
PIRi B34930. ISMSER.
S06318.
RefSeqi NP_033917.2. NM_009787.2.
UniGenei Mm.2442.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DJ1 NMR - A 46-172 [» ]
2DJ2 NMR - A 171-277 [» ]
2DJ3 NMR - A 519-638 [» ]
ProteinModelPortali P08003.
SMRi P08003. Positions 47-507, 516-638.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198446. 1 interaction.
IntActi P08003. 5 interactions.
MINTi MINT-4106888.

PTM databases

PhosphoSitei P08003.

Proteomic databases

MaxQBi P08003.
PaxDbi P08003.
PRIDEi P08003.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000077290 ; ENSMUSP00000076521 ; ENSMUSG00000025823 .
GeneIDi 12304.
KEGGi mmu:12304.
UCSCi uc009btf.1. mouse.

Organism-specific databases

CTDi 9601.
MGIi MGI:104864. Pdia4.

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00760000119201.
HOGENOMi HOG000162459.
HOVERGENi HBG005920.
InParanoidi P08003.
KOi K09582.
OrthoDBi EOG7VHSX1.
PhylomeDBi P08003.
TreeFami TF106382.

Miscellaneous databases

ChiTaRSi PDIA4. mouse.
EvolutionaryTracei P08003.
NextBioi 280830.
PROi P08003.
SOURCEi Search...

Gene expression databases

Bgeei P08003.
CleanExi MM_PDIA4.
Genevestigatori P08003.

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. "ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase."
    Mazzarella R.A., Srinivasan M., Haugejorden S.M., Green M.
    J. Biol. Chem. 265:1094-1101(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Amnion, Bone marrow, Head, Ovary and Uterus.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Brain and Embryonic germ cell.
  4. "An mRNA sharing sequences with a variant granulocyte-macrophage colony stimulating factor cDNA clone."
    Gough N.M., King J.A., Dunn A.R.
    Nucleic Acids Res. 15:10584-10584(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-638.
    Strain: BALB/c.
    Tissue: T-cell.
  5. "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.
  6. "The solution structure of thioredoxin domains of mouse protein disulfide-isomerase A4."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 46-277 AND 516-638.

Entry informationi

Entry nameiPDIA4_MOUSE
AccessioniPrimary (citable) accession number: P08003
Secondary accession number(s): P15841
, Q3TT79, Q3UJW0, Q6NXW4, Q8BMT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 30, 2010
Last modified: October 29, 2014
This is version 149 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3