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Protein

Protein disulfide-isomerase A2

Gene

PDIA2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: 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).By similarity

Catalytic activityi

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

Sites

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

GO - Molecular functioni

GO - Biological processi

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 Componenti: Unplaced

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 525504Protein disulfide-isomerase A2PRO_0000034223Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi18 – 18InterchainBy similarity
Disulfide bondi71 ↔ 74Redox-activePROSITE-ProRule annotation
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi284 – 2841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi418 ↔ 421Redox-activePROSITE-ProRule annotation
Glycosylationi516 – 5161N-linked (GlcNAc...)Sequence Analysis

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).By similarity

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000007818.

Structurei

3D structure databases

ProteinModelPortaliQ5RCH2.
SMRiQ5RCH2. Positions 389-492.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 152126Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini367 – 496130Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi522 – 5254Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

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

        10         20         30         40         50
MSCQLLPVLL LLLLRASCPW GHEQGPRSPS EEPPEEEIPK EDGILVLSRH
60 70 80 90 100
TLGLALREHP ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESSVVMLAKV
110 120 130 140 150
DGPAQPELAE EFGVTEYPTL KFFRDGNRTH PEEYTGPREA EGIAEWLRRR
160 170 180 190 200
VGPSAMRLED EAAAQALIDG RDLVVIGFFQ DLHDEDVATF LALAQDALDM
210 220 230 240 250
TFGLTDRPQL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL GLDLGDLSRF
260 270 280 290 300
LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLVGFGEA
310 320 330 340 350
APHFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV
360 370 380 390 400
DGGPVTTASI TAFCHAVLNG QVKPYLLSQE VPPDWDQRPV KTLVGKNFEQ
410 420 430 440 450
VAFDETKNVF VKFYAPWCTH CKEMAPAWEA LAEKYQDHED VIIAELDATA
460 470 480 490 500
NELDAFAVHG FPTLKYFPAG PGRKVIEYKS TRDLGTFSKF LDNGGVLPTE
510 520
EPLEEPAAPF PEPPANSTMG SKEEL
Length:525
Mass (Da):58,124
Last modified:December 21, 2004 - v1
Checksum:i0C402549E70D3F32
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CR858298 mRNA. Translation: CAH90535.1.
CR860523 mRNA. Translation: CAH92649.1.
RefSeqiNP_001125285.1. NM_001131813.1.
UniGeneiPab.11836.
Pab.19686.

3D structure databases

ProteinModelPortaliQ5RCH2.
SMRiQ5RCH2. Positions 389-492.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000007818.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100172183.
KEGGipon:100172183.

Organism-specific databases

CTDi64714.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 74 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.