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P09103

- PDIA1_MOUSE

UniProt

P09103 - PDIA1_MOUSE

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Protein
Protein disulfide-isomerase
Gene
P4hb, Pdia1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei55 – 551Nucleophile By similarity
Sitei56 – 561Contributes to redox potential value By similarity
Sitei57 – 571Contributes to redox potential value By similarity
Active sitei58 – 581Nucleophile By similarity
Sitei122 – 1221Lowers pKa of C-terminal Cys of first active site By similarity
Active sitei399 – 3991Nucleophile By similarity
Sitei400 – 4001Contributes to redox potential value By similarity
Sitei401 – 4011Contributes to redox potential value By similarity
Active sitei402 – 4021Nucleophile By similarity
Sitei463 – 4631Lowers pKa of C-terminal Cys of second active site By similarity

GO - Molecular functioni

  1. procollagen-proline 4-dioxygenase activity Source: Ensembl
  2. protein disulfide isomerase activity Source: RefGenome

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. cellular response to hypoxia Source: Ensembl
  3. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: MGI
  4. protein folding Source: RefGenome
  5. regulation of intrinsic apoptotic signaling pathway in response to oxidative stress Source: RefGenome
  6. response to endoplasmic reticulum stress Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Enzyme and pathway databases

ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_216017. Chylomicron-mediated lipid transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase (EC:5.3.4.1)
Short name:
PDI
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 namesi
Name:P4hb
Synonyms:Pdia1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:97464. P4hb.

Subcellular locationi

Endoplasmic reticulum lumen By similarity. Melanosome By similarity. Cell membrane; Peripheral membrane protein Reviewed prediction
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.

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  3. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  4. melanosome Source: UniProtKB-SubCell
  5. plasma membrane Source: UniProtKB-SubCell
  6. procollagen-proline 4-dioxygenase complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 By similarity
Add
BLAST
Chaini20 – 509490Protein disulfide-isomerase
PRO_0000034196Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 58Redox-active By similarity
Modified residuei202 – 2021N6-acetyllysine1 Publication
Modified residuei224 – 2241N6-succinyllysine1 Publication
Modified residuei273 – 2731N6-succinyllysine1 Publication
Disulfide bondi399 ↔ 402Redox-active By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiP09103.
PaxDbiP09103.
PRIDEiP09103.

2D gel databases

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

PTM databases

PhosphoSiteiP09103.

Expressioni

Gene expression databases

ArrayExpressiP09103.
BgeeiP09103.
CleanExiMM_P4HB.
GenevestigatoriP09103.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi202008. 1 interaction.
IntActiP09103. 10 interactions.
MINTiMINT-4122712.
STRINGi10090.ENSMUSP00000026122.

Structurei

3D structure databases

ProteinModelPortaliP09103.
SMRiP09103. Positions 18-480.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 136117Thioredoxin 1
Add
BLAST
Domaini348 – 477130Thioredoxin 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi506 – 5094Prevents secretion from ER

Sequence similaritiesi

Contains 2 thioredoxin domains.

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00740000115202.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiQ922C8.
KOiK09580.
OMAiYRDHENI.
OrthoDBiEOG7VHSX1.
TreeFamiTF106381.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09103-1 [UniParc]FASTAAdd to Basket

« Hide

MLSRALLCLA LAWAARVGAD ALEEEDNVLV LKKSNFEEAL AAHKYLLVEF    50
YAPWCGHCKA LAPEYAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG 100
YPTIKFFKNG DTASPKEYTA GREADDIVNW LKKRTGPAAT TLSDTAAAES 150
LVDSSEVTVI GFFKDVESDS AKQFLLAAEA IDDIPFGITS NSGVFSKYQL 200
DKDGVVLFKK FDEGRNNFEG EITKEKLLDF IKHNQLPLVI EFTEQTAPKI 250
FGGEIKTHIL LFLPKSVSDY DGKLSSFKRA AEGFKGKILF IFIDSDHTDN 300
QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE 350
GKIKPHLMSQ EVPEDWDKQP VKVLVGANFE EVAFDEKKNV FVEFYAPWCG 400
HCKQLAPIWD KLGETYKDHE NIIIAKMDST ANEVEAVKVH SFPTLKFFPA 450
SADRTVIDYN GERTLDGFKK FLESGGQDGA GDDEDLDLEE ALEPDMEEDD 500
DQKAVKDEL 509
Length:509
Mass (Da):57,058
Last modified:July 27, 2011 - v2
Checksum:i1FB0AA8ACCDB13EA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681A → R in CAA29759. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS25742.1.
PIRiA34930. ISMSSS.
RefSeqiNP_035162.1. NM_011032.2.
UniGeneiMm.16660.

Genome annotation databases

EnsembliENSMUST00000026122; ENSMUSP00000026122; ENSMUSG00000025130.
GeneIDi18453.
KEGGimmu:18453.
UCSCiuc007mti.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS25742.1.
PIRi A34930. ISMSSS.
RefSeqi NP_035162.1. NM_011032.2.
UniGenei Mm.16660.

3D structure databases

ProteinModelPortali P09103.
SMRi P09103. Positions 18-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202008. 1 interaction.
IntActi P09103. 10 interactions.
MINTi MINT-4122712.
STRINGi 10090.ENSMUSP00000026122.

PTM databases

PhosphoSitei P09103.

2D gel databases

COMPLUYEAST-2DPAGE P09103.
REPRODUCTION-2DPAGE P09103.
SWISS-2DPAGE P09103.

Proteomic databases

MaxQBi P09103.
PaxDbi P09103.
PRIDEi P09103.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026122 ; ENSMUSP00000026122 ; ENSMUSG00000025130 .
GeneIDi 18453.
KEGGi mmu:18453.
UCSCi uc007mti.1. mouse.

Organism-specific databases

CTDi 5034.
MGIi MGI:97464. P4hb.

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00740000115202.
HOGENOMi HOG000162459.
HOVERGENi HBG005920.
InParanoidi Q922C8.
KOi K09580.
OMAi YRDHENI.
OrthoDBi EOG7VHSX1.
TreeFami TF106381.

Enzyme and pathway databases

Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_216017. Chylomicron-mediated lipid transport.

Miscellaneous databases

ChiTaRSi P4HB. mouse.
NextBioi 294144.
PROi P09103.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09103.
Bgeei P09103.
CleanExi MM_P4HB.
Genevestigatori P09103.

Family and domain databases

Gene3Di 3.40.30.10. 4 hits.
InterProi IPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 2 hits.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 4 hits.
TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiPDIA1_MOUSE
AccessioniPrimary (citable) accession number: P09103
Secondary accession number(s): Q922C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 146 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi