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Q5RCH2

- PDIA2_PONAB

UniProt

Q5RCH2 - PDIA2_PONAB

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Protein
Protein disulfide-isomerase A2
Gene
PDIA2
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins By similarity.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711Nucleophile By similarity
Sitei72 – 721Contributes to redox potential value By similarity
Sitei73 – 731Contributes to redox potential value By similarity
Active sitei74 – 741Nucleophile By similarity
Sitei138 – 1381Lowers pKa of C-terminal Cys of first active site By similarity
Active sitei418 – 4181Nucleophile By similarity
Sitei419 – 4191Contributes to redox potential value By similarity
Sitei420 – 4201Contributes to redox potential value By similarity
Active sitei421 – 4211Nucleophile By similarity
Sitei482 – 4821Lowers pKa of C-terminal Cys of second active site By similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB-EC
  2. steroid binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Keywords - Ligandi

Lipid-binding, Steroid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A2 (EC:5.3.4.1)
Gene namesi
Name:PDIA2
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. 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 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 525504Protein disulfide-isomerase A2
PRO_0000034223Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi18 – 18Interchain By similarity
Disulfide bondi71 ↔ 74Redox-active By similarity
Glycosylationi127 – 1271N-linked (GlcNAc...) Reviewed prediction
Glycosylationi284 – 2841N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi418 ↔ 421Redox-active By similarity
Glycosylationi516 – 5161N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

The disulfide-linked homodimer exhibits an enhanced chaperone activity By similarity.
Glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer; predominantly as monomer under reducing conditions. Homodimer; disulfide-linked. 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 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5RCH2.
SMRiQ5RCH2. Positions 389-492.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 152126Thioredoxin 1
Add
BLAST
Domaini367 – 496130Thioredoxin 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi522 – 5254Prevents secretion from ER Reviewed prediction

Sequence similaritiesi

Contains 2 thioredoxin domains.

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG005920.
InParanoidiQ5RCH2.
KOiK09581.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5RCH2-1 [UniParc]FASTAAdd to Basket

« Hide

MSCQLLPVLL LLLLRASCPW GHEQGPRSPS EEPPEEEIPK EDGILVLSRH    50
TLGLALREHP ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESSVVMLAKV 100
DGPAQPELAE EFGVTEYPTL KFFRDGNRTH PEEYTGPREA EGIAEWLRRR 150
VGPSAMRLED EAAAQALIDG RDLVVIGFFQ DLHDEDVATF LALAQDALDM 200
TFGLTDRPQL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL GLDLGDLSRF 250
LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLVGFGEA 300
APHFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV 350
DGGPVTTASI TAFCHAVLNG QVKPYLLSQE VPPDWDQRPV KTLVGKNFEQ 400
VAFDETKNVF VKFYAPWCTH CKEMAPAWEA LAEKYQDHED VIIAELDATA 450
NELDAFAVHG FPTLKYFPAG PGRKVIEYKS TRDLGTFSKF LDNGGVLPTE 500
EPLEEPAAPF PEPPANSTMG SKEEL 525
Length:525
Mass (Da):58,124
Last modified:December 21, 2004 - v1
Checksum:i0C402549E70D3F32
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti342 – 3421E → G in CAH92649. 1 Publication
Sequence conflicti485 – 4851G → E in CAH92649. 1 Publication
Sequence conflicti505 – 5051E → G in CAH92649. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR858298 mRNA. Translation: CAH90535.1.
CR860523 mRNA. Translation: CAH92649.1.
RefSeqiNP_001125285.1. NM_001131813.1.
UniGeneiPab.11836.
Pab.19686.

Genome annotation databases

GeneIDi100172183.
KEGGipon:100172183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR858298 mRNA. Translation: CAH90535.1 .
CR860523 mRNA. Translation: CAH92649.1 .
RefSeqi NP_001125285.1. NM_001131813.1.
UniGenei Pab.11836.
Pab.19686.

3D structure databases

ProteinModelPortali Q5RCH2.
SMRi Q5RCH2. Positions 389-492.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100172183.
KEGGi pon:100172183.

Organism-specific databases

CTDi 64714.

Phylogenomic databases

HOVERGENi HBG005920.
InParanoidi Q5RCH2.
KOi K09581.

Family and domain databases

Gene3Di 3.40.30.10. 4 hits.
InterProi IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 2 hits.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 4 hits.
TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.

Entry informationi

Entry nameiPDIA2_PONAB
AccessioniPrimary (citable) accession number: Q5RCH2
Secondary accession number(s): Q5R6G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 21, 2004
Last modified: September 3, 2014
This is version 70 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