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P09103 (PDIA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide-isomerase

Short name=PDI
EC=5.3.4.1
Alternative name(s):
Cellular thyroid hormone-binding protein
Endoplasmic reticulum resident protein 59
Short name=ER protein 59
Short name=ERp59
Prolyl 4-hydroxylase subunit beta
p55
Gene names
Name:P4hb
Synonyms:Pdia1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP By similarity.

Catalytic activity

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

Subunit structure

Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1 By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity. Melanosome By similarity. Cell membrane; Peripheral membrane protein Potential. Note: Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces By similarity.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Ontologies

Keywords
   Cellular componentCell membrane
Endoplasmic reticulum
Membrane
   DomainRedox-active center
Repeat
Signal
   Molecular functionChaperone
Isomerase
   PTMAcetylation
Disulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

peptidyl-proline hydroxylation to 4-hydroxy-L-proline

Inferred from sequence orthology PubMed 7753822. Source: MGI

protein folding

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to endoplasmic reticulum stress

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentendoplasmic reticulum

Inferred from direct assay PubMed 15767459PubMed 15767678PubMed 18094359PubMed 9493907PubMed 9806833. Source: MGI

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum-Golgi intermediate compartment

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

procollagen-proline 4-dioxygenase complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprocollagen-proline 4-dioxygenase activity

Inferred from electronic annotation. Source: Ensembl

protein disulfide isomerase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 509490Protein disulfide-isomerase
PRO_0000034196

Regions

Domain20 – 136117Thioredoxin 1
Domain348 – 477130Thioredoxin 2
Motif506 – 5094Prevents secretion from ER

Sites

Active site551Nucleophile By similarity
Active site581Nucleophile By similarity
Active site3991Nucleophile By similarity
Active site4021Nucleophile By similarity
Site561Contributes to redox potential value By similarity
Site571Contributes to redox potential value By similarity
Site1221Lowers pKa of C-terminal Cys of first active site By similarity
Site4001Contributes to redox potential value By similarity
Site4011Contributes to redox potential value By similarity
Site4631Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Modified residue2021N6-acetyllysine Ref.6
Modified residue2241N6-succinyllysine Ref.6
Modified residue2731N6-succinyllysine Ref.6
Disulfide bond55 ↔ 58Redox-active By similarity
Disulfide bond399 ↔ 402Redox-active By similarity

Experimental info

Sequence conflict681A → R in CAA29759. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P09103 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 1FB0AA8ACCDB13EA

FASTA50957,058
        10         20         30         40         50         60 
MLSRALLCLA LAWAARVGAD ALEEEDNVLV LKKSNFEEAL AAHKYLLVEF YAPWCGHCKA 

        70         80         90        100        110        120 
LAPEYAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG YPTIKFFKNG DTASPKEYTA 

       130        140        150        160        170        180 
GREADDIVNW LKKRTGPAAT TLSDTAAAES LVDSSEVTVI GFFKDVESDS AKQFLLAAEA 

       190        200        210        220        230        240 
IDDIPFGITS NSGVFSKYQL DKDGVVLFKK FDEGRNNFEG EITKEKLLDF IKHNQLPLVI 

       250        260        270        280        290        300 
EFTEQTAPKI FGGEIKTHIL LFLPKSVSDY DGKLSSFKRA AEGFKGKILF IFIDSDHTDN 

       310        320        330        340        350        360 
QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE GKIKPHLMSQ 

       370        380        390        400        410        420 
EVPEDWDKQP VKVLVGANFE EVAFDEKKNV FVEFYAPWCG HCKQLAPIWD KLGETYKDHE 

       430        440        450        460        470        480 
NIIIAKMDST ANEVEAVKVH SFPTLKFFPA SADRTVIDYN GERTLDGFKK FLESGGQDGA 

       490        500 
GDDEDLDLEE ALEPDMEEDD DQKAVKDEL 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a full-length cDNA clone encoding a mouse cellular thyroid hormone binding protein (p55) that is homologous to protein disulfide isomerase and the beta-subunit of prolyl-4-hydroxylase."
Gong Q.-H., Fukuda T., Parkison C., Cheng S.-Y.
Nucleic Acids Res. 16:1203-1203(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"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].
[3]"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. expand/collapse author list , 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, DBA/2 and NOD.
Tissue: Bone marrow and Stomach.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"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: Czech II and FVB/N.
Tissue: Liver and Mammary tumor.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-224 AND LYS-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06453 mRNA. Translation: CAA29759.1.
J05185 mRNA. Translation: AAA39906.1.
AK150002 mRNA. Translation: BAE29230.1.
AK150422 mRNA. Translation: BAE29545.1.
AK150805 mRNA. Translation: BAE29868.1.
AK152141 mRNA. Translation: BAE30979.1.
AK152217 mRNA. Translation: BAE31045.1.
AK159606 mRNA. Translation: BAE35225.1.
AK159965 mRNA. Translation: BAE35520.1.
AK168330 mRNA. Translation: BAE40268.1.
AK168893 mRNA. Translation: BAE40710.1.
AK170603 mRNA. Translation: BAE41907.1.
AL663030 Genomic DNA. Translation: CAM27084.1.
BC008549 mRNA. Translation: AAH08549.1.
BC093512 mRNA. Translation: AAH93512.1.
CCDSCCDS25742.1.
PIRISMSSS. A34930.
RefSeqNP_035162.1. NM_011032.2.
UniGeneMm.16660.

3D structure databases

ProteinModelPortalP09103.
SMRP09103. Positions 18-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202008. 1 interaction.
IntActP09103. 10 interactions.
MINTMINT-4122712.
STRING10090.ENSMUSP00000026122.

PTM databases

PhosphoSiteP09103.

2D gel databases

COMPLUYEAST-2DPAGEP09103.
REPRODUCTION-2DPAGEP09103.
SWISS-2DPAGEP09103.

Proteomic databases

MaxQBP09103.
PaxDbP09103.
PRIDEP09103.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026122; ENSMUSP00000026122; ENSMUSG00000025130.
GeneID18453.
KEGGmmu:18453.
UCSCuc007mti.1. mouse.

Organism-specific databases

CTD5034.
MGIMGI:97464. P4hb.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00740000115202.
HOGENOMHOG000162459.
HOVERGENHBG005920.
InParanoidQ922C8.
KOK09580.
OMAYRDHENI.
OrthoDBEOG7VHSX1.
TreeFamTF106381.

Gene expression databases

ArrayExpressP09103.
BgeeP09103.
CleanExMM_P4HB.
GenevestigatorP09103.

Family and domain databases

Gene3D3.40.30.10. 4 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSP4HB. mouse.
NextBio294144.
PROP09103.
SOURCESearch...

Entry information

Entry namePDIA1_MOUSE
AccessionPrimary (citable) accession number: P09103
Secondary accession number(s): Q922C8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot