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Q29RV1 (PDIA4_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein disulfide-isomerase A4
EC=5.3.4.1
Gene names
Name:PDIA4
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length643 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Subcellular location

Endoplasmic reticulum lumen By similarity. Melanosome By similarity.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 3 thioredoxin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 643623Protein disulfide-isomerase A4
PRO_0000240338

Regions

Domain21 – 168148Thioredoxin 1
Domain170 – 300131Thioredoxin 2
Domain503 – 634132Thioredoxin 3
Motif640 – 6434Prevents secretion from ER By similarity
Compositional bias39 – 5416Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue3651N6-acetyllysine By similarity
Disulfide bond90 ↔ 93Redox-active By similarity
Disulfide bond205 ↔ 208Redox-active By similarity
Disulfide bond553 ↔ 556Redox-active By similarity

Experimental info

Sequence conflict161V → A in ABG81434. Ref.2
Sequence conflict321T → S in ABG81434. Ref.2
Sequence conflict321T → S in ABQ12930. Ref.2
Sequence conflict4151V → I in ABG81434. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q29RV1 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: EFBBB755DE97A35E

FASTA64372,526
        10         20         30         40         50         60 
MRPRKAWMLV LLLALVQLLA VASAGAPDED STDKEDAIEE DEEEDEDDDD DDDDLEVKEE 

        70         80         90        100        110        120 
NGVLILNDAN FDNFVADKDT VLLEFYAPWC GHCKQFAPEY EKIAATLKEN DPPIPVAKID 

       130        140        150        160        170        180 
ATSESALASR FDVSGYPTIK ILKKGQEVDY EGSRTQEEIV AKVKEVSQPN WTPPPEVTLV 

       190        200        210        220        230        240 
LTKDNFDEVV NDADIILVEF YAPWCGHCKK LAPEYEKAAK ELSKSSPPIP LAKVDAIAET 

       250        260        270        280        290        300 
DLAKRFDVSS YPTLKIFRKG KAFSYNGPRE KYGIVDYMME QSGPPSKQIL ALKQVQEFLK 

       310        320        330        340        350        360 
DGDDVIIIGV FKSESDPAYQ LYQDAANSLR EDYKFHHTFS TEIAKFLKVS LGKLVVMQPE 

       370        380        390        400        410        420 
KFQSKYEPKS YVMDIKDSTE AAAITEHVVK HTLPLVGHRK AADAKRYTRR PLVVVYYSVD 

       430        440        450        460        470        480 
FSFDYRAATQ FWRNKVLEVA KDFPEYTFAV ADEEDFATEL KDLGLSESGE EVNAAILDEG 

       490        500        510        520        530        540 
GRRFAMEPDD FDADALRDFV TAFKKGKLKP VIKSQPVPKN NKGPVKVVVG KTFDSIVMDP 

       550        560        570        580        590        600 
KKDVLIEFYA PWCGHCKQLE PVYTSLGKKY KGHKNLVIAK MDATANDVTS DRYKVEGFPT 

       610        620        630        640 
IYFAPSGDKK KPIKFEDGNR DLEHLSKFIE EHATKLSRTK EEL

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Testis.
[2]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-478.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC114004 mRNA. Translation: AAI14005.1.
BT026278 mRNA. Translation: ABG81434.1.
BT030490 mRNA. Translation: ABQ12930.1.
IPIIPI00706136.
RefSeqNP_001039344.1. NM_001045879.2.
UniGeneBt.23128.

3D structure databases

ProteinModelPortalQ29RV1.
SMRQ29RV1. Positions 55-283, 521-643.
ModBaseSearch...

Protein-protein interaction databases

IntActQ29RV1. 1 interaction.
STRING9913.ENSBTAP00000022782.

Proteomic databases

PaxDbQ29RV1.
PRIDEQ29RV1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID415110.
KEGGbta:415110.

Organism-specific databases

CTD9601.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
HOVERGENHBG005920.
InParanoidQ29RV1.
KOK09582.
OrthoDBEOG405S0R.

Family and domain databases

Gene3D3.40.30.10. 4 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFPIRSF036862. Disulphide_isom_A4. 1 hit.
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF52833. Thiordxn-like_fd. 5 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20818794.

Entry information

Entry namePDIA4_BOVIN
AccessionPrimary (citable) accession number: Q29RV1
Secondary accession number(s): A5D971, Q0V8E1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: April 4, 2006
Last modified: April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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