Protein disulfide-isomerase 2 precursor

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Q17770 (PDI2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase 2
EC=5.3.4.1

Alternative name(s):
PDI 1
Prolyl 4-hydroxylase subunit beta-2

Gene names

Name:	pdi-2
ORF Names:	C07A12.4

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	Heterotetramer of two alpha chains and two beta chains. Exist either as a phy-1₂/pdi-2₂ tetramer, a phy-2₂/pdi-2₂ tetramer or as a phy-1/phy-2/pdi-2₂ tetramer. Ref.4
Subcellular location	Endoplasmic reticulum lumen.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	body morphogenesis Inferred from mutant phenotype. Source: WormBase cell redox homeostasis Inferred from electronic annotation. Source: InterPro embryo development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase endoplasmic reticulum unfolded protein response Inferred from expression pattern. Source: WormBase gastrulation with mouth forming first Inferred from mutant phenotype. Source: WormBase glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro growth Inferred from mutant phenotype. Source: WormBase locomotion Inferred from mutant phenotype. Source: WormBase nematode larval development Inferred from mutant phenotype. Source: WormBase positive regulation of locomotion Inferred from mutant phenotype. Source: WormBase
Cellular component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from direct assay Ref.1. Source: WormBase protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro protein-glutamine gamma-glutamyltransferase activity Inferred from direct assay. Source: WormBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

Potential

Chain

17 – 493

477

Protein disulfide-isomerase 2

PRO_0000034204

Regions

Domain

17 – 130

114

Thioredoxin 1

Domain

342 – 470

129

Thioredoxin 2

Motif

490 – 493

Prevents secretion from ER Potential

Sites

Active site

Nucleophile By similarity

Active site

Nucleophile By similarity

Active site

393

Nucleophile By similarity

Active site

396

Nucleophile By similarity

Site

Contributes to redox potential value By similarity

Site

Contributes to redox potential value By similarity

Site

116

Lowers pKa of C-terminal Cys of first active site By similarity

Site

394

Contributes to redox potential value By similarity

Site

395

Contributes to redox potential value By similarity

Site

456

Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation

334

N-linked (GlcNAc...) Ref.5

Disulfide bond

52 ↔ 55

Redox-active By similarity

Disulfide bond

393 ↔ 396

Redox-active By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q17770 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 41BC0C1185EBFB5E
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FASTA

493

55,152

        10         20         30         40         50         60 
MFRLVGLFFL VLGASAAVIE EEENVIVLTK DNFDEVINGN EFILVEFYAP WCGHCKSLAP 

        70         80         90        100        110        120 
EYAKAATQLK EEGSDIKLGK LDATVHGEVS SKFEVRGYPT LKLFRNGKPQ EYNGGRDHDS 

       130        140        150        160        170        180 
IIAWLKKKTG PVAKPLADAD AVKELQESAD VVVIGYFKDT TSDDAKTFLE VAAGIDDVPF 

       190        200        210        220        230        240 
GISTEDAVKS EIELKGEGIV LFKKFDDGRV AFDEKLTQDG LKTWIQANRL ALVSEFTQET 

       250        260        270        280        290        300 
ASVIFGGEIK SHNLLFVSKE SSEFAKLEQE FKNAAKQFKG KVLFVYINTD VEENARIMEF 

       310        320        330        340        350        360 
FGLKKDELPA IRLISLEEDM TKFKPDFEEI TTENISKFTQ NYLDGSVKPH LMSEDIPEDW 

       370        380        390        400        410        420 
DKNPVKILVG KNFEQVARDN TKNVLVEFYA PWCGHCKQLA PTWDKLGEKF ADDESIVIAK 

       430        440        450        460        470        480 
MDSTLNEVED VKIQSFPTIK FFPAGSNKVV DYTGDRTIEG FTKFLETNGK EGAGASEEEK 

       490 
AEEEADEEGH TEL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit." Veijola J., Annunen P., Koivunen P., Page A.P., Pihlajaniemi T., Kivirikko K.I. Biochem. J. 317:721-729(1996) [PubMed: 8760355] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans." Winter A.D., Page A.P. Mol. Cell. Biol. 20:4084-4093(2000) [PubMed: 10805750] [Abstract] Cited for: FUNCTION.
[4]	"The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl 4-hydroxylases with unique combinations of subunits." Myllyharju J., Kukkola L., Winter A.D., Page A.P. J. Biol. Chem. 277:29187-29196(2002) [PubMed: 12036960] [Abstract] Cited for: SUBUNIT.
[5]	"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-334, MASS SPECTROMETRY. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FO080373 Genomic DNA. Translation: CCD63277.1.
PIR	S71862. T34092.
RefSeq	NP_508778.1. NM_076377.2.
UniGene	Cel.18353.
3D structure databases
ProteinModelPortal	Q17770.
SMR	Q17770. Positions 20-353, 364-466.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q17770. 5 interactions.
MINT	MINT-230414.
STRING	Q17770.
Proteomic databases
PRIDE	Q17770.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	C07A12.4a.1; C07A12.4a.1; C07A12.4. C07A12.4a.2; C07A12.4a.2; C07A12.4.
GeneID	180724.
KEGG	cel:C07A12.4.
UCSC	C07A12.4a.1. c. elegans.
Organism-specific databases
CTD	180724.
WormBase	C07A12.4a; CE03972; WBGene00003963; pdi-2.
Phylogenomic databases
eggNOG	meNOG04114.
GeneTree	EMGT00050000002774.
HOGENOM	HBG627841.
InParanoid	Q17770.
OMA	DMTKFKP.
PhylomeDB	Q17770.
Gene expression databases
ArrayExpress	Q17770.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 4 hits.
KO	K09580.
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 4 hits.
TIGRFAMs	TIGR01130. ER_PDI_fam. 1 hit. TIGR01126. Pdi_dom. 2 hits.
PROSITE	PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	910644.

Entry information

Entry name

PDI2_CAEEL

Accession

Primary (citable) accession number: Q17770

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2003
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents