Protein disulfide-isomerase 1 precursor

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Q17967 (PDI1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. 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 1
Short name=PDI 1
EC=5.3.4.1

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

Gene names

Name:	pdi-1
ORF Names:	C14B1.1

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	485 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity

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

Subcellular location

Endoplasmic reticulum lumen By similarity.

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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro protein deglutathionylation Inferred from direct assay PubMed 17711389. 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 PubMed 12424233 PubMed 17711389 Ref.1. Source: WormBase protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro protein-glutamine gamma-glutamyltransferase activity Inferred from direct assay PubMed 12424233. Source: WormBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Potential

Chain

21 – 485

465

Protein disulfide-isomerase 1

PRO_0000034203

Regions

Domain

21 – 130

110

Thioredoxin 1

Domain

342 – 470

129

Thioredoxin 2

Motif

482 – 485

Prevents secretion from ER Potential

Sites

Active site

393

Nucleophile By similarity

Active site

396

Nucleophile 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

Disulfide bond

52 ↔ 55

Redox-active By similarity

Disulfide bond

393 ↔ 396

Redox-active By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q17967 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 74070D655E6A415C
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FASTA

485

53,436

        10         20         30         40         50         60 
MSLSVSFIFL LVASIGAVVA DSENVLVLTE SNFEETINGN EFVLVKFYAP WCVHCKSLAP 

        70         80         90        100        110        120 
KYDEAADLLK EEGSDIKLAK VDATENQALA SKFEVRGYPT ILYFKSGKPT KYTGGRATAQ 

       130        140        150        160        170        180 
IVDWVKKKSG PTVTTVESVE QLEELKGKTR VVVLGYFKDA KSDAATIYNE VADSVDDAFF 

       190        200        210        220        230        240 
AVAGSAEVAA AASLNEDGVA LIRTDGDDSE TSTIAEAEIT NTIALKQWLH AYKLSAVTEF 

       250        260        270        280        290        300 
THESAQEIVG GDLKKFHFLI IRKSDSSFDE TIAKFTEVAK KFRAKIVFVL LDVDVEENAR 

       310        320        330        340        350        360 
ILEFLGVDAK NTPANRIVSL ADQVEKFKPQ EGEDFEAFTN SYLEGKSAQD LKAQDLPEDW 

       370        380        390        400        410        420 
NALPVKVLVA SNFNEIALDE TKTVFVKFYA PWCGHCKQLV PVWDELAEKY ESNPNVVIAK 

       430        440        450        460        470        480 
LDATLNELAD VKVNSFPTLK LWPAGSSTPV DYDGDRNLEK FEEFVNKYAG SASESETASQ 


DHEEL

« 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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U95074 Genomic DNA. Translation: AAB94647.1. Z37139 Genomic DNA. Translation: CAA85491.1.
PIR	S71863.
RefSeq	NP_497746.1. NM_065345.5.
3D structure databases
ProteinModelPortal	Q17967.
SMR	Q17967. Positions 19-465.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-24653N.
IntAct	Q17967. 1 interaction.
MINT	MINT-226883.
STRING	6239.C14B1.1.2.
Proteomic databases
PaxDb	Q17967.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	C14B1.1.1; C14B1.1.1; C14B1.1. C14B1.1.2; C14B1.1.2; C14B1.1.
GeneID	175472.
KEGG	cel:CELE_C14B1.1.
UCSC	C14B1.1.1. c. elegans.
Organism-specific databases
CTD	175472.
WormBase	C14B1.1; CE00897; WBGene00003962; pdi-1.
Phylogenomic databases
eggNOG	COG0526.
GeneTree	ENSGT00700000104429.
HOGENOM	HOG000162459.
InParanoid	Q17967.
KO	K09580.
OMA	PANRIVS.
Family and domain databases
Gene3D	3.40.30.10. 3 hits.
InterPro	IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
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	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	888312.

Entry information

Entry name

PDI1_CAEEL

Accession

Primary (citable) accession number: Q17967

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2003
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
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 WormBase

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

Family and domain databases

Other

Entry information

Relevant documents