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Protein

Protein disulfide-isomerase A5

Gene

PDIA5

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: GO_Central

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. protein folding Source: GO_Central
  3. response to endoplasmic reticulum stress Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

ReactomeiREACT_211201. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A5 (EC:5.3.4.1)
Gene namesi
Name:PDIA5
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 1

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 521496Protein disulfide-isomerase A5PRO_0000244882Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi184 ↔ 187Redox-activePROSITE-ProRule annotation
Disulfide bondi307 ↔ 310Redox-activePROSITE-ProRule annotation
Disulfide bondi428 ↔ 431Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ2KIL5.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000025128.

Structurei

3D structure databases

ProteinModelPortaliQ2KIL5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini136 – 263128Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini274 – 386113Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST
Domaini387 – 508122Thioredoxin 3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi518 – 5214Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi387 – 3926Poly-Pro

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.
GeneTreeiENSGT00730000110455.
HOGENOMiHOG000039967.
HOVERGENiHBG053547.
InParanoidiQ2KIL5.
KOiK09583.
OMAiYYHYGKF.
OrthoDBiEOG74TWZ6.
TreeFamiTF106379.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q2KIL5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARVVPAWLL LPLAVWVVLP TWLSSAKFSS LIERISDPKD LKKLLRTRNN
60 70 80 90 100
VLVLYSKSEA AAESHLKLLS TVAQAVKGQG TICWVDCGDA ESRKLCKKMK
110 120 130 140 150
VDLSAKDKKV ELFHYQDGAF HTEYNRAVTF KSIVAFLKDP KGPPLWEEDP
160 170 180 190 200
GAKDVVHIDN EKDFRRLLKK EEKPILMMFY APWCSVCKRI MPHFQKAATQ
210 220 230 240 250
LRGQFVLAGM NVYPSEFENI KEEYSVRGYP TICYFEKGRF LFQYDSYGST
260 270 280 290 300
AEDIVEWLKN PQPPQPQVPE TPWADEGGSV YHLSDEDFDQ FVKEHSSVLV
310 320 330 340 350
MFHAPWCGHC KKMKPEFESA AEVLHGEGDS SGVLAAVDAT VNKALAERFH
360 370 380 390 400
IAEFPTLKYF KNGEKYAVPA LRTKKSFIEW MRNPESPPPP DPAWEEQQTS
410 420 430 440 450
VLHLSGDNFR ETLKRKKHAL VMFYAPWCPH CKKAIPHFTA AADAFKDDRK
460 470 480 490 500
IACAAIDCVK ENNKDLCQQE AVKAYPTFHY YHYGKFVEKY DTNPTELGFT
510 520
SFIRTLREGD HERLGKKKEE L
Length:521
Mass (Da):59,673
Last modified:March 7, 2006 - v1
Checksum:iA05A85EB4EEA2BEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC112593 mRNA. Translation: AAI12594.1.
RefSeqiNP_001039556.1. NM_001046091.2.
UniGeneiBt.6804.

Genome annotation databases

EnsembliENSBTAT00000025128; ENSBTAP00000025128; ENSBTAG00000018877.
GeneIDi511603.
KEGGibta:511603.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC112593 mRNA. Translation: AAI12594.1.
RefSeqiNP_001039556.1. NM_001046091.2.
UniGeneiBt.6804.

3D structure databases

ProteinModelPortaliQ2KIL5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000025128.

Proteomic databases

PRIDEiQ2KIL5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000025128; ENSBTAP00000025128; ENSBTAG00000018877.
GeneIDi511603.
KEGGibta:511603.

Organism-specific databases

CTDi10954.

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00730000110455.
HOGENOMiHOG000039967.
HOVERGENiHBG053547.
InParanoidiQ2KIL5.
KOiK09583.
OMAiYYHYGKF.
OrthoDBiEOG74TWZ6.
TreeFamiTF106379.

Enzyme and pathway databases

ReactomeiREACT_211201. XBP1(S) activates chaperone genes.

Miscellaneous databases

NextBioi20870009.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Testis.

Entry informationi

Entry nameiPDIA5_BOVIN
AccessioniPrimary (citable) accession number: Q2KIL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: March 7, 2006
Last modified: February 4, 2015
This is version 76 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.