Protein disulfide-isomerase precursor - Gallus gallus (Chicken)

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P09102 (PDIA1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 118. History...

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

Documents (1) |

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
Short name=PDI
EC=5.3.4.1

Alternative name(s):
Cellular thyroid hormone-binding protein
Prolyl 4-hydroxylase subunit beta
Retina cognin
Short name=R-cognin

Gene names

Name:	P4HB
Synonyms:	PDI, PDIA1

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	515 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)

Function	This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase By similarity.
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase. Stabilizes this enzyme and retains it in the ER without contributing to the catalytic activity. Binds UBQLN1 By similarity.
Subcellular location	Endoplasmic reticulum lumen By similarity. Cell membrane; Peripheral membrane protein Potential. Note: Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces By similarity.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.
Sequence caution	The sequence AAA49054.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Domain	Redox-active center Repeat Signal
Molecular function	Chaperone Isomerase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing 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 peptidyl-proline hydroxylation to 4-hydroxy-L-proline Inferred from electronic annotation. Source: Compara protein folding Inferred from electronic annotation. Source: GOC
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum-Golgi intermediate compartment Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro procollagen-proline 4-dioxygenase activity Inferred from electronic annotation. Source: Compara protein disulfide isomerase activity Inferred from electronic annotation. Source: EC protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Ref.4

Chain

23 – 515

493

Protein disulfide-isomerase Ref.4

PRO_0000034200

Regions

Domain

23 – 139

117

Thioredoxin 1

Domain

351 – 480

130

Thioredoxin 2

Motif

512 – 515

Prevents secretion from ER

Sites

Active site

Nucleophile By similarity

Active site

Nucleophile By similarity

Active site

402

Nucleophile By similarity

Active site

405

Nucleophile By similarity

Site

Contributes to redox potential value By similarity

Site

Contributes to redox potential value By similarity

Site

125

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

Site

403

Contributes to redox potential value By similarity

Site

404

Contributes to redox potential value By similarity

Site

466

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

Amino acid modifications

Disulfide bond

58 ↔ 61

Redox-active By similarity

Disulfide bond

402 ↔ 405

Redox-active By similarity

Experimental info

Sequence conflict

E → Q Ref.1

Sequence conflict

E → Q Ref.3

Sequence conflict

94 – 95

EL → DV Ref.3

Sequence conflict

359

H → Q Ref.3

Sequence conflict

447

T → M in CAB57801. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P09102 [UniParc].

Last modified May 16, 2003. Version 3.
Checksum: E7CC978A5109C2CE
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FASTA

515

57,410

        10         20         30         40         50         60 
MAVVRVRAIV ALLCLVAALG LAEPLEEEDG VLVLRAANFE QALAAHRHLL VEFYAPWCGH 

        70         80         90        100        110        120 
CKALAPEYAK AAAQLKAEGS EIRLAKVDAT EEAELAQQFG VRGYPTIKFF RNGDKAAPRE 

       130        140        150        160        170        180 
YTAGREADDI VSWLKKRTGP AATTLTDAAA AETLVDSSEV VVIGFFKDVT SDAAKEFLLA 

       190        200        210        220        230        240 
AESVDDIPFG ISSSADVFSK YQLSQDGVVL FKKFDEGRNN FEGDLTKDNL LNFIKSNQLP 

       250        260        270        280        290        300 
LVIEFTEQTA PKIFGGEIKT HILLFLPKSV SDYEGKLDNF KTAAGNFKGK ILFIFIDSDH 

       310        320        330        340        350        360 
SDNQRILEFF GLKKEECPAV RLITLEEEMT KYKPESDDLT ADKIKEFCNK FLEGKIKPHL 

       370        380        390        400        410        420 
MSQDLPEDWD KQPVKVLVGK NFEEVAFDEN KNVFVEFYAP WCGHCKQLAP IWDKLGETYR 

       430        440        450        460        470        480 
DHENIVIAKM DSTANEVEAV KIHSFPTLKF FPAGSGRNVI DYNGERTLEG FKKFLESGGQ 

       490        500        510 
DGAAADDDLE DLETDEETDL EEGDDDEQKI QKDEL

« Hide

References

[1]	Hausman R.E. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION TO 315; 356; 488; 491-493 AND 497.
[2]	"cDNA for R-cognin: homology with a multifunctional protein." Krishna Rao A.S., Hausman R.E. Proc. Natl. Acad. Sci. U.S.A. 90:2950-2954(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 139-515. Tissue: Retina.
[3]	"Structure of the gene encoding the beta-subunit of chicken prolyl 4-hydroxylase." Nakazawa M., Aida T., Everson W.V., Gonda M.A., Hughes S.H., Kao W.W. Gene 71:451-460(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-129; 163-172; 209-218; 244-253; 286-295; 353-463 AND 483-515.
[4]	"Molecular cloning of a multifunctional chicken protein acting as the prolyl 4-hydroxylase beta-subunit, protein disulphide-isomerase and a cellular thyroid-hormone-binding protein. Comparison of cDNA-deduced amino acid sequences with those in other species." Parkkonen T., Kivirikko K.Z., Pihlajaniemi T. Biochem. J. 256:1005-1011(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-515, PROTEIN SEQUENCE OF 23-31 AND 95-109.
[5]	Bassuk J.A. Submitted (FEB-1988) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-459.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L11147 mRNA. Translation: AAA49054.2. Different initiation. X13110 mRNA. Translation: CAA31502.1. X06768 Genomic DNA. Translation: CAB57801.1.
IPI	IPI00596673.
PIR	ISCHSS. S02084.
RefSeq	NP_001185639.1. NM_001198710.1.
UniGene	Gga.4976.
3D structure databases
ProteinModelPortal	P09102.
SMR	P09102. Positions 26-362, 373-476.
ModBase	Search...
Protein-protein interaction databases
STRING	9031.ENSGALP00000011689.
Proteomic databases
PaxDb	P09102.
PRIDE	P09102.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	374091.
KEGG	gga:374091.
Organism-specific databases
CTD	5034.
Phylogenomic databases
eggNOG	COG0526.
HOGENOM	HOG000162459.
HOVERGEN	HBG005920.
InParanoid	P09102.
KO	K09580.
OrthoDB	EOG4JWVDB.
Enzyme and pathway databases
SABIO-RK	P09102.
Gene expression databases
ArrayExpress	P09102.
Family and domain databases
Gene3D	3.40.30.10. 4 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	20813610.

Entry information

Entry name

PDIA1_CHICK

Accession

Primary (citable) accession number: P09102
Secondary accession number(s): Q90969

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	May 16, 2003
Last modified:	April 3, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

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

Experimental info

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents