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P21195

- PDIA1_RABIT

UniProt

P21195 - PDIA1_RABIT

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Protein
Protein disulfide-isomerase
Gene
P4HB, PDIA1
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript 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 sitei54 – 541Nucleophile By similarity
Sitei55 – 551Contributes to redox potential value By similarity
Sitei56 – 561Contributes to redox potential value By similarity
Active sitei57 – 571Nucleophile By similarity
Sitei121 – 1211Lowers pKa of C-terminal Cys of first active site By similarity
Active sitei398 – 3981Nucleophile By similarity
Sitei399 – 3991Contributes to redox potential value By similarity
Sitei400 – 4001Contributes to redox potential value By similarity
Active sitei401 – 4011Nucleophile By similarity
Sitei462 – 4621Lowers pKa of C-terminal Cys of second active site By similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

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
Prolyl 4-hydroxylase subunit beta
p55
Gene namesi
Name:P4HB
Synonyms:PDIA1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

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 lumen Source: UniProtKB-SubCell
  2. melanosome Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 By similarity
Add
BLAST
Chaini19 – 509491Protein disulfide-isomerase
PRO_0000034198Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 57Redox-active By similarity
Modified residuei223 – 2231N6-succinyllysine By similarity
Modified residuei272 – 2721N6-succinyllysine By similarity
Disulfide bondi398 ↔ 401Redox-active By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP21195.

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

BioGridi1173214. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP21195.
SMRiP21195. Positions 20-358, 369-472.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 135117Thioredoxin 1
Add
BLAST
Domaini347 – 476130Thioredoxin 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

HOVERGENiHBG005920.

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.

P21195-1 [UniParc]FASTAAdd to Basket

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MLRRAVLCLA LAVTAGWAWA AEEEDNVLVL KSSNFAEELA AHKHLLVEFY    50
APWCGHCKAL APEYAKAAGK LKAEGSDIRL AKVDATEESD LAQQYGVRGY 100
PTIKFFKNGD TASPKEYTAG READDIVNWL KKRTGPAATT LADSAAAESL 150
VESSEVAVIG FFKDVESDAA KQFLLAAEAT DDIPFGLTAS SDVFSRYQVH 200
QDGVVLFKKF DEGRNNFEGE VTKEKLLDFI KHNQLPLVIE FTEQTAPKIF 250
GGEIKTHILL FLPRSAADHD GKLSGFKQAA EGFKGKILFI FIDSDHADNQ 300
RILEFFGLKK EECPAVRLIT LEEEMTKYKP ESDELTAEGI TEFCQRFLEG 350
KIKPHLMSQE LPEDWDRQPV KVLVGKNFEE VAFDEKKNVF VEFYAPWCGH 400
CKQLAPIWDK LGETYKEHQD IVIAKMDSTA NEVEAVKVHS FPTLKFFPAG 450
PGRTVIDYNG ERTLDGFKKF LESGGQDGAG DEDGLEDLEE AEEPDLEEDD 500
DQKAVRDEL 509
Length:509
Mass (Da):56,808
Last modified:May 1, 1991 - v1
Checksum:i093C8C18E209BAB5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05602 mRNA. Translation: AAA31476.1.
PIRiA38362.
RefSeqiNP_001164518.1. NM_001171047.1.
UniGeneiOcu.5912.

Genome annotation databases

GeneIDi100328595.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05602 mRNA. Translation: AAA31476.1 .
PIRi A38362.
RefSeqi NP_001164518.1. NM_001171047.1.
UniGenei Ocu.5912.

3D structure databases

ProteinModelPortali P21195.
SMRi P21195. Positions 20-358, 369-472.
ModBasei Search...

Protein-protein interaction databases

BioGridi 1173214. 2 interactions.

Proteomic databases

PRIDEi P21195.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100328595.

Organism-specific databases

CTDi 5034.

Phylogenomic databases

HOVERGENi HBG005920.

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

  1. "Molecular cloning of cDNA encoding a 55-kDa multifunctional thyroid hormone binding protein of skeletal muscle sarcoplasmic reticulum."
    Fliegel L., Newton E., Burns K., Michalak M.
    J. Biol. Chem. 265:15496-15502(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPDIA1_RABIT
AccessioniPrimary (citable) accession number: P21195
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: September 3, 2014
This is version 108 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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