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Protein

Protein disulfide-isomerase A6

Gene

Pdia6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei55 – 551NucleophileBy similarity
Sitei56 – 561Contributes to redox potential valueBy similarity
Sitei57 – 571Contributes to redox potential valueBy similarity
Active sitei58 – 581NucleophileBy similarity
Sitei118 – 1181Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei190 – 1901NucleophileBy similarity
Sitei191 – 1911Contributes to redox potential valueBy similarity
Sitei192 – 1921Contributes to redox potential valueBy similarity
Active sitei193 – 1931NucleophileBy similarity
Sitei256 – 2561Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: RGD
  2. protein disulfide isomerase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic cell clearance Source: GO_Central
  2. cell redox homeostasis Source: InterPro
  3. platelet activation Source: UniProtKB
  4. platelet aggregation Source: UniProtKB
  5. protein folding Source: GO_Central
  6. response to endoplasmic reticulum stress Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_93415. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A6 (EC:5.3.4.1)
Alternative name(s):
Calcium-binding protein 1
Short name:
CaBP1
Protein disulfide isomerase P5
Thioredoxin domain-containing protein 7
Gene namesi
Name:Pdia6
Synonyms:Cabp1, Txndc7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 6

Organism-specific databases

RGDi628688. Pdia6.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation. Cell membrane By similarity. Melanosome By similarity

GO - Cellular componenti

  1. endoplasmic reticulum-Golgi intermediate compartment Source: RGD
  2. endoplasmic reticulum lumen Source: HGNC
  3. melanosome Source: UniProtKB
  4. plasma membrane Source: UniProtKB
  5. smooth endoplasmic reticulum 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 – 1919By similarityAdd
BLAST
Chaini20 – 440421Protein disulfide-isomerase A6PRO_0000034240Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 58Redox-activePROSITE-ProRule annotation
Modified residuei129 – 1291PhosphoserineBy similarity
Disulfide bondi190 ↔ 193Redox-activePROSITE-ProRule annotation
Modified residuei428 – 4281PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PRIDEiQ63081.

PTM databases

PhosphoSiteiQ63081.

Expressioni

Gene expression databases

GenevestigatoriQ63081.

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).By similarity

Protein-protein interaction databases

BioGridi251898. 2 interactions.
IntActiQ63081. 5 interactions.
MINTiMINT-1775443.

Structurei

3D structure databases

ProteinModelPortaliQ63081.
SMRiQ63081. Positions 20-132, 154-280.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 133113Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini151 – 287137Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi437 – 4404Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi422 – 43615Asp/Glu-rich (acidic)Add
BLAST

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

HOVERGENiHBG053548.
InParanoidiQ63081.
KOiK09584.
OrthoDBiEOG7XDBFV.
PhylomeDBiQ63081.

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.

Q63081-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLVLGLVS CTFFLAVSAL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF
60 70 80 90 100
YAPWCGHCQR LTPEWKKAAS ALKDVVKVGA VNADKHQSLG GQYGVQGFPT
110 120 130 140 150
IKIFGANKNK PEDYQGGRTG EAIVDAALSA LRQLVKDRLG GRSGGYSSGK
160 170 180 190 200
QGRGDSSSKK DVVELTDDTF DKNVLDSEDV WMVEFYAPWC GHCKNLEPEW
210 220 230 240 250
AAAATEVKEQ TKGKVKLAAV DATVNQVLAS RYGIKGFPTI KIFQKGESPV
260 270 280 290 300
DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKKT CEEHQLCVVA
310 320 330 340 350
VLPHILDTGA TGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQYELENALG
360 370 380 390 400
IGGFGYPAMA AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG
410 420 430 440
GSFPNITPRE PWDGKDGELP VEDDIDLSDV ELDDLEKDEL
Length:440
Mass (Da):48,173
Last modified:March 29, 2005 - v2
Checksum:i8D388E4FFD743719
GO

Sequence cautioni

The sequence AAH82063.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC082063 mRNA. Translation: AAH82063.1. Different initiation.
X79328 mRNA. Translation: CAA55891.1.
PIRiS45038.
RefSeqiNP_001004442.1. NM_001004442.1.
UniGeneiRn.2685.

Genome annotation databases

GeneIDi286906.
KEGGirno:286906.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC082063 mRNA. Translation: AAH82063.1. Different initiation.
X79328 mRNA. Translation: CAA55891.1.
PIRiS45038.
RefSeqiNP_001004442.1. NM_001004442.1.
UniGeneiRn.2685.

3D structure databases

ProteinModelPortaliQ63081.
SMRiQ63081. Positions 20-132, 154-280.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251898. 2 interactions.
IntActiQ63081. 5 interactions.
MINTiMINT-1775443.

PTM databases

PhosphoSiteiQ63081.

Proteomic databases

PRIDEiQ63081.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi286906.
KEGGirno:286906.

Organism-specific databases

CTDi10130.
RGDi628688. Pdia6.

Phylogenomic databases

HOVERGENiHBG053548.
InParanoidiQ63081.
KOiK09584.
OrthoDBiEOG7XDBFV.
PhylomeDBiQ63081.

Enzyme and pathway databases

ReactomeiREACT_93415. XBP1(S) activates chaperone genes.

Miscellaneous databases

NextBioi625007.

Gene expression databases

GenevestigatoriQ63081.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Testis.
  2. "CaBP1, a calcium binding protein of the thioredoxin family, is a resident KDEL protein of the ER and not of the intermediate compartment."
    Fuellekrug J., Soennichsen B., Wuensch U., Arseven K., Van P.N., Soeling H.-D., Mieskes G.
    J. Cell Sci. 107:2719-2727(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-440.
    Strain: Wistar.
    Tissue: Liver.
  3. Lubec G., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 119-132; 217-231 AND 314-322, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.

Entry informationi

Entry nameiPDIA6_RAT
AccessioniPrimary (citable) accession number: Q63081
Secondary accession number(s): Q641Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 29, 2005
Last modified: March 4, 2015
This is version 122 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.