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Protein

Protein disulfide-isomerase A5

Gene

Pdia5

Organism
Rattus norvegicus (Rat)
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_93415. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A5 (EC:5.3.4.1)
Gene namesi
Name:Pdia5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1359236. Pdia5.

Subcellular locationi

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 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 517496Protein disulfide-isomerase A5PRO_0000034235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi180 ↔ 183Redox-activePROSITE-ProRule annotation
Disulfide bondi303 ↔ 306Redox-activePROSITE-ProRule annotation
Disulfide bondi424 ↔ 427Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ5I0H9.
PRIDEiQ5I0H9.

Expressioni

Gene expression databases

ExpressionAtlasiQ5I0H9. baseline and differential.
GenevestigatoriQ5I0H9.

Interactioni

Protein-protein interaction databases

MINTiMINT-4573704.
STRINGi10116.ENSRNOP00000059945.

Structurei

3D structure databases

ProteinModelPortaliQ5I0H9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini132 – 259128Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini268 – 382115Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST
Domaini376 – 504129Thioredoxin 3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi514 – 5174Prevents secretion from ERSequence Analysis

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.
HOGENOMiHOG000039967.
HOVERGENiHBG053547.
InParanoidiQ5I0H9.
KOiK09583.
OrthoDBiEOG74TWZ6.
PhylomeDBiQ5I0H9.
TreeFamiTF106379.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5I0H9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARAWGLLLA IGVILPTWLS STKVSSLIER ISDPKDLKKL LRTRNNVLVL
60 70 80 90 100
YSESEVAAES HLKLLSTVAQ AVKGQGTICW VDCGDAESRK LCKKMKVDLS
110 120 130 140 150
PKDKKIELFH YQDGAFHMQY DRAVTLKSIV AFLKDPKGPP LWEEDPGAKD
160 170 180 190 200
VVHIDSEKDF RRLLKKEEKP LLMMFYAPWC SMCKRIMPHF QKAATQVRGH
210 220 230 240 250
TVLAGMNVYP PEFENIKEEY NVRGYPTICY FEKGRFLFQY ENYGSTAEDI
260 270 280 290 300
VEWLKNPQPP QPQVPETPWA DEGGSVYHLT DEDFDQFVKE HSSVLVMFHA
310 320 330 340 350
PWCGHCKKMK PEFESAAEVL HGDAESSGVL AAVDATINEA LAERFHISAF
360 370 380 390 400
PTLKYFKNGE QQAVPALRTK KKFIEWMQNP EAPPPPEPTW EEQQTSVLHL
410 420 430 440 450
VGDNFRETLK KKKHTLVMFY APWCPHCKKV IPHFTATADA FKDDRKIACA
460 470 480 490 500
AVDCVKDKNQ DLCQQESVKA YPTFHYYHYG KLVEKYESDR TELGFTSFIR
510
TLREGDLKRL EKRREDL
Length:517
Mass (Da):59,399
Last modified:February 15, 2005 - v1
Checksum:i038F0B07E1C15A0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088305 mRNA. Translation: AAH88305.1.
RefSeqiNP_001014147.1. NM_001014125.1.
UniGeneiRn.162053.

Genome annotation databases

GeneIDi360722.
KEGGirno:360722.
UCSCiRGD:1359236. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088305 mRNA. Translation: AAH88305.1.
RefSeqiNP_001014147.1. NM_001014125.1.
UniGeneiRn.162053.

3D structure databases

ProteinModelPortaliQ5I0H9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4573704.
STRINGi10116.ENSRNOP00000059945.

Proteomic databases

PaxDbiQ5I0H9.
PRIDEiQ5I0H9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi360722.
KEGGirno:360722.
UCSCiRGD:1359236. rat.

Organism-specific databases

CTDi10954.
RGDi1359236. Pdia5.

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000039967.
HOVERGENiHBG053547.
InParanoidiQ5I0H9.
KOiK09583.
OrthoDBiEOG74TWZ6.
PhylomeDBiQ5I0H9.
TreeFamiTF106379.

Enzyme and pathway databases

ReactomeiREACT_93415. XBP1(S) activates chaperone genes.

Miscellaneous databases

NextBioi673887.

Gene expression databases

ExpressionAtlasiQ5I0H9. baseline and differential.
GenevestigatoriQ5I0H9.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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: Liver.

Entry informationi

Entry nameiPDIA5_RAT
AccessioniPrimary (citable) accession number: Q5I0H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: February 15, 2005
Last modified: February 4, 2015
This is version 84 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.