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Protein

Protein disulfide-isomerase A4

Gene

PDIA4

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

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

Isomerase

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A4 (EC:5.3.4.1)
Gene namesi
Name:PDIA4
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation. Melanosome By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 643623Protein disulfide-isomerase A4PRO_0000240338Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi90 ↔ 93Redox-activePROSITE-ProRule annotation
Disulfide bondi205 ↔ 208Redox-activePROSITE-ProRule annotation
Modified residuei365 – 3651N6-acetyllysineBy similarity
Disulfide bondi553 ↔ 556Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiQ29RV1.
PRIDEiQ29RV1.

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.

Protein-protein interaction databases

IntActiQ29RV1. 1 interaction.
STRINGi9913.ENSBTAP00000022782.

Structurei

3D structure databases

ProteinModelPortaliQ29RV1.
SMRiQ29RV1. Positions 55-283, 521-643.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 168148Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini170 – 300131Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST
Domaini503 – 634132Thioredoxin 3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi640 – 6434Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 5416Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 3 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiQ29RV1.
KOiK09582.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFiPIRSF036862. Disulphide_isom_A4. 1 hit.
SUPFAMiSSF52833. SSF52833. 5 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q29RV1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRPRKAWMLV LLLALVQLLA VASAGAPDED STDKEDAIEE DEEEDEDDDD
60 70 80 90 100
DDDDLEVKEE NGVLILNDAN FDNFVADKDT VLLEFYAPWC GHCKQFAPEY
110 120 130 140 150
EKIAATLKEN DPPIPVAKID ATSESALASR FDVSGYPTIK ILKKGQEVDY
160 170 180 190 200
EGSRTQEEIV AKVKEVSQPN WTPPPEVTLV LTKDNFDEVV NDADIILVEF
210 220 230 240 250
YAPWCGHCKK LAPEYEKAAK ELSKSSPPIP LAKVDAIAET DLAKRFDVSS
260 270 280 290 300
YPTLKIFRKG KAFSYNGPRE KYGIVDYMME QSGPPSKQIL ALKQVQEFLK
310 320 330 340 350
DGDDVIIIGV FKSESDPAYQ LYQDAANSLR EDYKFHHTFS TEIAKFLKVS
360 370 380 390 400
LGKLVVMQPE KFQSKYEPKS YVMDIKDSTE AAAITEHVVK HTLPLVGHRK
410 420 430 440 450
AADAKRYTRR PLVVVYYSVD FSFDYRAATQ FWRNKVLEVA KDFPEYTFAV
460 470 480 490 500
ADEEDFATEL KDLGLSESGE EVNAAILDEG GRRFAMEPDD FDADALRDFV
510 520 530 540 550
TAFKKGKLKP VIKSQPVPKN NKGPVKVVVG KTFDSIVMDP KKDVLIEFYA
560 570 580 590 600
PWCGHCKQLE PVYTSLGKKY KGHKNLVIAK MDATANDVTS DRYKVEGFPT
610 620 630 640
IYFAPSGDKK KPIKFEDGNR DLEHLSKFIE EHATKLSRTK EEL
Length:643
Mass (Da):72,526
Last modified:April 4, 2006 - v1
Checksum:iEFBBB755DE97A35E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161V → A in ABG81434. (PubMed:16305752)Curated
Sequence conflicti32 – 321T → S in ABG81434. (PubMed:16305752)Curated
Sequence conflicti32 – 321T → S in ABQ12930. (PubMed:16305752)Curated
Sequence conflicti415 – 4151V → I in ABG81434. (PubMed:16305752)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC114004 mRNA. Translation: AAI14005.1.
BT026278 mRNA. Translation: ABG81434.1.
BT030490 mRNA. Translation: ABQ12930.1.
RefSeqiNP_001039344.1. NM_001045879.2.
UniGeneiBt.23128.

Genome annotation databases

GeneIDi415110.
KEGGibta:415110.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC114004 mRNA. Translation: AAI14005.1.
BT026278 mRNA. Translation: ABG81434.1.
BT030490 mRNA. Translation: ABQ12930.1.
RefSeqiNP_001039344.1. NM_001045879.2.
UniGeneiBt.23128.

3D structure databases

ProteinModelPortaliQ29RV1.
SMRiQ29RV1. Positions 55-283, 521-643.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ29RV1. 1 interaction.
STRINGi9913.ENSBTAP00000022782.

Proteomic databases

PaxDbiQ29RV1.
PRIDEiQ29RV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi415110.
KEGGibta:415110.

Organism-specific databases

CTDi9601.

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiQ29RV1.
KOiK09582.

Miscellaneous databases

NextBioi20818794.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFiPIRSF036862. Disulphide_isom_A4. 1 hit.
SUPFAMiSSF52833. SSF52833. 5 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-478.

Entry informationi

Entry nameiPDIA4_BOVIN
AccessioniPrimary (citable) accession number: Q29RV1
Secondary accession number(s): A5D971, Q0V8E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: April 4, 2006
Last modified: January 7, 2015
This is version 77 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

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.