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Q921X9

- PDIA5_MOUSE

UniProt

Q921X9 - PDIA5_MOUSE

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Protein

Protein disulfide-isomerase A5

Gene

Pdia5

Organism
Mus musculus (Mouse)
Status
Reviewed - 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: RefGenome

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

ReactomeiREACT_106572. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A5 (EC:5.3.4.1)
Alternative name(s):
Protein disulfide isomerase-related protein
Gene namesi
Name:Pdia5
Synonyms:Pdir
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1919849. Pdia5.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: RefGenome
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_0000034234Add
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

MaxQBiQ921X9.
PaxDbiQ921X9.
PRIDEiQ921X9.

PTM databases

PhosphoSiteiQ921X9.

Expressioni

Gene expression databases

BgeeiQ921X9.
CleanExiMM_PDIA5.
ExpressionAtlasiQ921X9. baseline and differential.
GenevestigatoriQ921X9.

Interactioni

Protein-protein interaction databases

IntActiQ921X9. 2 interactions.
MINTiMINT-4122674.
STRINGi10090.ENSMUSP00000023550.

Structurei

3D structure databases

ProteinModelPortaliQ921X9.
SMRiQ921X9. Positions 27-500.
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 ERPROSITE-ProRule annotation

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.
InParanoidiQ921X9.
KOiK09583.
OMAiYYHYGKF.
OrthoDBiEOG74TWZ6.
PhylomeDBiQ921X9.
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.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. 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.

Q921X9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARAWGLLLA IGVVLPTWLS STKVSSLIER ISDPKDLKKL LRTRNNVLVL
60 70 80 90 100
YSESEVAAES HLKLLSTVAQ AVKGQGTVCW VDCGDAESRK LCKKMKVDLS
110 120 130 140 150
PKDKKIELFH YQDGAFHMQY DRAVTLKSIV AFLKDPKGPP LWEEDPGAKD
160 170 180 190 200
VVHIDSEKDF RRLLKREEKP LLMMFYAPWC SMCKRIMPHF QKAATQVRGH
210 220 230 240 250
IVLAGMNVYP SEFENIKEEY NVRGYPTICY FEKGRFLFPY ENYGSTAEDI
260 270 280 290 300
VEWLKNPLPP QPQVPETPWA DEGGSVYHLT DEDFDQFVKE HSSVLVMFHA
310 320 330 340 350
PWCGHCKKMK PEFESAAEVL HGDAESSGVL AAVDATVNEA LAGRFHISAF
360 370 380 390 400
PTLKYFKNGE QQAVPALRTK KKFIEWMQNP EAPPPPEPTW EEQQTSVLHL
410 420 430 440 450
VGDNFRDTLK KKKHTLVMFY APWCPHCKKV IPHFTATADA FKEDRKIACA
460 470 480 490 500
AVDCVKDKNQ DLCQQEAVKA YPTFHYYHYG KLVEKYESDR TELGFTSFIR
510
TLREGDLKRL EKRREEL
Length:517
Mass (Da):59,267
Last modified:December 1, 2001 - v1
Checksum:i6702B9C5EF9F1C84
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC009151 mRNA. Translation: AAH09151.1.
CCDSiCCDS37323.1.
RefSeqiNP_082571.1. NM_028295.1.
UniGeneiMm.71015.

Genome annotation databases

EnsembliENSMUST00000023550; ENSMUSP00000023550; ENSMUSG00000022844.
GeneIDi72599.
KEGGimmu:72599.
UCSCiuc007zbl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC009151 mRNA. Translation: AAH09151.1 .
CCDSi CCDS37323.1.
RefSeqi NP_082571.1. NM_028295.1.
UniGenei Mm.71015.

3D structure databases

ProteinModelPortali Q921X9.
SMRi Q921X9. Positions 27-500.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q921X9. 2 interactions.
MINTi MINT-4122674.
STRINGi 10090.ENSMUSP00000023550.

PTM databases

PhosphoSitei Q921X9.

Proteomic databases

MaxQBi Q921X9.
PaxDbi Q921X9.
PRIDEi Q921X9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023550 ; ENSMUSP00000023550 ; ENSMUSG00000022844 .
GeneIDi 72599.
KEGGi mmu:72599.
UCSCi uc007zbl.1. mouse.

Organism-specific databases

CTDi 10954.
MGIi MGI:1919849. Pdia5.

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00730000110455.
HOGENOMi HOG000039967.
HOVERGENi HBG053547.
InParanoidi Q921X9.
KOi K09583.
OMAi YYHYGKF.
OrthoDBi EOG74TWZ6.
PhylomeDBi Q921X9.
TreeFami TF106379.

Enzyme and pathway databases

Reactomei REACT_106572. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSi PDIA5. mouse.
NextBioi 336573.
PROi Q921X9.
SOURCEi Search...

Gene expression databases

Bgeei Q921X9.
CleanExi MM_PDIA5.
ExpressionAtlasi Q921X9. baseline and differential.
Genevestigatori Q921X9.

Family and domain databases

Gene3Di 3.40.30.10. 4 hits.
InterProi IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 3 hits.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 4 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiPDIA5_MOUSE
AccessioniPrimary (citable) accession number: Q921X9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 101 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3