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P38660

- PDIA6_MESAU

UniProt

P38660 - PDIA6_MESAU

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Protein
Protein disulfide-isomerase A6
Gene
PDIA6
Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin 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
Sitei118 – 1181Lowers pKa of C-terminal Cys of first active site By similarity
Active sitei190 – 1901Nucleophile By similarity
Sitei191 – 1911Contributes to redox potential value By similarity
Sitei192 – 1921Contributes to redox potential value By similarity
Active sitei193 – 1931Nucleophile By similarity
Sitei256 – 2561Lowers pKa of C-terminal Cys of second active site By similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. platelet activation Source: UniProtKB
  3. platelet aggregation Source: UniProtKB
  4. protein folding Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A6 (EC:5.3.4.1)
Alternative name(s):
Protein disulfide isomerase P5
Gene namesi
Name:PDIA6
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

Endoplasmic reticulum lumen By similarity. Cell membrane By similarity. Melanosome By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 Publication
Add
BLAST
Chaini20 – 439420Protein disulfide-isomerase A6
PRO_0000034237Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 58Redox-active By similarity
Disulfide bondi190 ↔ 193Redox-active By similarity
Modified residuei427 – 4271Phosphoserine By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PRIDEiP38660.

Expressioni

Tissue specificityi

Expressed most abundantly in lung and kidney, followed by heart, liver and brain.

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. Interacts with ITGB3 following platelet stimulation By similarity.

Structurei

3D structure databases

ProteinModelPortaliP38660.
SMRiP38660. Positions 20-132, 154-280.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 133114Thioredoxin 1
Add
BLAST
Domaini151 – 287137Thioredoxin 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi436 – 4394Prevents secretion from ER By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi421 – 43515Asp/Glu-rich (acidic)
Add
BLAST

Sequence similaritiesi

Contains 2 thioredoxin domains.

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG053548.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 3 hits.
TIGRFAMsiTIGR01126. 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.

P38660-1 [UniParc]FASTAAdd to Basket

« Hide

MARLGFGLVS CTFFLAASGL YSSSDDVIEL TPSNFNREVI QSNSLWLVEF    50
YAPWCGHCQR LTPEWKKAAT ALKDVVKVGA VDADKHQSLG GQYGVQGFPT 100
IKIFGANKNK PEDYQGGRTG EAIVDAALSA LRQLVKDRLS GRSGGYSSGK 150
QGRGDSSSKK DVIELTDDTF DKNVLDSDDV WMVEFYAPWC GHCKNLEPEW 200
ATAATEVKEQ TKGKVKLAAV DATVNQVLAN RYGIRGFPTI KIFQKGEAPV 250
DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDVAKKM CEEHQLCVVA 300
VLPHILDTGA ARNSYLEILL KLADKYKKKM WGWLWTEAGA QSELENALGI 350
GGFGYPAMAR INARKMKFAL LKGSFSEQGI NEFLRELSFG RASTAPVGGG 400
SFPAITAREP WDGRDGELPV EDDIDLSDVE LDDLEKDEL 439
Length:439
Mass (Da):48,161
Last modified:February 1, 1995 - v1
Checksum:iE24CAECF5FFF5F8D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X62678 mRNA. Translation: CAA44550.1.
PIRiS19656.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X62678 mRNA. Translation: CAA44550.1 .
PIRi S19656.

3D structure databases

ProteinModelPortali P38660.
SMRi P38660. Positions 20-132, 154-280.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P38660.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG053548.

Family and domain databases

Gene3Di 3.40.30.10. 2 hits.
InterProi IPR005788. Disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 2 hits.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 3 hits.
TIGRFAMsi 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. "The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells."
    Chaudhuri M.M., Tonin P.N., Lewis W.H., Srinivasan P.R.
    Biochem. J. 281:645-650(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-43.
  2. "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
    Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
    Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPDIA6_MESAU
AccessioniPrimary (citable) accession number: P38660
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 3, 2014
This is version 95 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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