Protein disulfide-isomerase A6 precursor

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Q63081 (PDIA6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Pdia6
Synonyms:	Cabp1, Txndc7

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	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.
Subcellular location	Endoplasmic reticulum lumen By similarity. Cell membrane By similarity. Melanosome By similarity.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.
Sequence caution	The sequence AAH82063.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Domain	Redox-active center Repeat Signal
Ligand	Calcium
Molecular function	Chaperone Isomerase
PTM	Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro platelet aggregation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	endoplasmic reticulum lumen Inferred from direct assay PubMed 14561759. Source: HGNC endoplasmic reticulum-Golgi intermediate compartment Traceable author statement Ref.2. Source: RGD melanosome Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	calcium ion binding Traceable author statement Ref.2. Source: RGD electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from sequence or structural similarity. Source: UniProtKB protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

By similarity

Chain

20 – 440

421

Protein disulfide-isomerase A6

PRO_0000034240

Regions

Domain

21 – 133

113

Thioredoxin 1

Domain

151 – 287

137

Thioredoxin 2

Motif

437 – 440

Prevents secretion from ER By similarity

Compositional bias

422 – 436

Asp/Glu-rich (acidic)

Sites

Active site

Nucleophile By similarity

Active site

Nucleophile By similarity

Active site

190

Nucleophile By similarity

Active site

193

Nucleophile By similarity

Site

Contributes to redox potential value By similarity

Site

Contributes to redox potential value By similarity

Site

118

Lowers pKa of C-terminal Cys of first active site By similarity

Site

191

Contributes to redox potential value By similarity

Site

192

Contributes to redox potential value By similarity

Site

256

Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Modified residue

428

Phosphoserine By similarity

Disulfide bond

55 ↔ 58

Redox-active By similarity

Disulfide bond

190 ↔ 193

Redox-active By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q63081 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 8D388E4FFD743719
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FASTA

440

48,173

        10         20         30         40         50         60 
MARLVLGLVS CTFFLAVSAL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF YAPWCGHCQR 

        70         80         90        100        110        120 
LTPEWKKAAS ALKDVVKVGA VNADKHQSLG GQYGVQGFPT IKIFGANKNK PEDYQGGRTG 

       130        140        150        160        170        180 
EAIVDAALSA LRQLVKDRLG GRSGGYSSGK QGRGDSSSKK DVVELTDDTF DKNVLDSEDV 

       190        200        210        220        230        240 
WMVEFYAPWC GHCKNLEPEW AAAATEVKEQ TKGKVKLAAV DATVNQVLAS RYGIKGFPTI 

       250        260        270        280        290        300 
KIFQKGESPV DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKKT CEEHQLCVVA 

       310        320        330        340        350        360 
VLPHILDTGA TGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQYELENALG IGGFGYPAMA 

       370        380        390        400        410        420 
AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG GSFPNITPRE PWDGKDGELP 

       430        440 
VEDDIDLSDV ELDDLEKDEL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain and Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC082063 mRNA. Translation: AAH82063.1. Different initiation. X79328 mRNA. Translation: CAA55891.1.
IPI	IPI00365929.
PIR	S45038.
RefSeq	NP_001004442.1. NM_001004442.1.
UniGene	Rn.2685.
3D structure databases
ProteinModelPortal	Q63081.
SMR	Q63081. Positions 20-132, 154-280.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q63081. 1 interaction.
MINT	MINT-1775443.
PTM databases
PhosphoSite	Q63081.
Proteomic databases
PRIDE	Q63081.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000074829; ENSRNOP00000064632; ENSRNOG00000050197.
GeneID	286906.
KEGG	rno:286906.
Organism-specific databases
CTD	10130.
RGD	628688. Pdia6.
Phylogenomic databases
GeneTree	ENSGT00700000104354.
HOVERGEN	HBG053548.
KO	K09584.
Gene expression databases
Genevestigator	Q63081.
Family and domain databases
Gene3D	3.40.30.10. 2 hits.
InterPro	IPR005788. Disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 3 hits.
TIGRFAMs	TIGR01126. pdi_dom. 2 hits.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	625007.

Entry information

Entry name

PDIA6_RAT

Accession

Primary (citable) accession number: Q63081
Secondary accession number(s): Q641Y3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 29, 2005
Last modified:	April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents