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P21195

- PDIA1_RABIT

UniProt

P21195 - PDIA1_RABIT

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Protein

Protein disulfide-isomerase

Gene

P4HB

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541NucleophileBy similarity
Sitei55 – 551Contributes to redox potential valueBy similarity
Sitei56 – 561Contributes to redox potential valueBy similarity
Active sitei57 – 571NucleophileBy similarity
Sitei121 – 1211Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei398 – 3981NucleophileBy similarity
Sitei399 – 3991Contributes to redox potential valueBy similarity
Sitei400 – 4001Contributes to redox potential valueBy similarity
Active sitei401 – 4011NucleophileBy similarity
Sitei462 – 4621Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB-EC

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 PROSITE-ProRule annotation. Melanosome By similarity. Cell membrane Curated; Peripheral membrane protein Curated
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).By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 509491Protein disulfide-isomerasePRO_0000034198Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 57Redox-activePROSITE-ProRule annotation
Modified residuei223 – 2231N6-succinyllysineBy similarity
Modified residuei272 – 2721N6-succinyllysineBy similarity
Disulfide bondi398 ↔ 401Redox-activePROSITE-ProRule annotation

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).By similarity

Protein-protein interaction databases

BioGridi1173214. 2 interactions.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 135117Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini347 – 476130Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

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

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG005920.
InParanoidiP21195.

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

« Hide

        10         20         30         40         50
MLRRAVLCLA LAVTAGWAWA AEEEDNVLVL KSSNFAEELA AHKHLLVEFY
60 70 80 90 100
APWCGHCKAL APEYAKAAGK LKAEGSDIRL AKVDATEESD LAQQYGVRGY
110 120 130 140 150
PTIKFFKNGD TASPKEYTAG READDIVNWL KKRTGPAATT LADSAAAESL
160 170 180 190 200
VESSEVAVIG FFKDVESDAA KQFLLAAEAT DDIPFGLTAS SDVFSRYQVH
210 220 230 240 250
QDGVVLFKKF DEGRNNFEGE VTKEKLLDFI KHNQLPLVIE FTEQTAPKIF
260 270 280 290 300
GGEIKTHILL FLPRSAADHD GKLSGFKQAA EGFKGKILFI FIDSDHADNQ
310 320 330 340 350
RILEFFGLKK EECPAVRLIT LEEEMTKYKP ESDELTAEGI TEFCQRFLEG
360 370 380 390 400
KIKPHLMSQE LPEDWDRQPV KVLVGKNFEE VAFDEKKNVF VEFYAPWCGH
410 420 430 440 450
CKQLAPIWDK LGETYKEHQD IVIAKMDSTA NEVEAVKVHS FPTLKFFPAG
460 470 480 490 500
PGRTVIDYNG ERTLDGFKKF LESGGQDGAG DEDGLEDLEE AEEPDLEEDD

DQKAVRDEL
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...
MobiDBi 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.
InParanoidi P21195.

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: October 29, 2014
This is version 110 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