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P09102

- PDIA1_CHICK

UniProt

P09102 - PDIA1_CHICK

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Protein

Protein disulfide-isomerase

Gene

P4HB

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581NucleophileBy similarity
Sitei59 – 591Contributes to redox potential valueBy similarity
Sitei60 – 601Contributes to redox potential valueBy similarity
Active sitei61 – 611NucleophileBy similarity
Sitei125 – 1251Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei402 – 4021NucleophileBy similarity
Sitei403 – 4031Contributes to redox potential valueBy similarity
Sitei404 – 4041Contributes to redox potential valueBy similarity
Active sitei405 – 4051NucleophileBy similarity
Sitei466 – 4661Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Chaperone, Isomerase

Enzyme and pathway databases

SABIO-RKP09102.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase (EC:5.3.4.1)
Short name:
PDI
Alternative name(s):
Cellular thyroid hormone-binding protein
Prolyl 4-hydroxylase subunit beta
Retina cognin
Short name:
R-cognin
Gene namesi
Name:P4HB
Synonyms:PDI, PDIA1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation. Cell membrane Curated; Peripheral membrane protein Curated
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).By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 515493Protein disulfide-isomerase1 PublicationPRO_0000034200Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 61Redox-activePROSITE-ProRule annotation
Disulfide bondi402 ↔ 405Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP09102.
PRIDEiP09102.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi9031.ENSGALP00000011689.

Structurei

3D structure databases

ProteinModelPortaliP09102.
SMRiP09102. Positions 26-362, 373-476.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 139117Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini351 – 480130Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi512 – 5154Prevents secretion from ER

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

eggNOGiCOG0526.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP09102.
KOiK09580.
PhylomeDBiP09102.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. 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.
TIGR01126. pdi_dom. 2 hits.
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.

P09102-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVVRVRAIV ALLCLVAALG LAEPLEEEDG VLVLRAANFE QALAAHRHLL
60 70 80 90 100
VEFYAPWCGH CKALAPEYAK AAAQLKAEGS EIRLAKVDAT EEAELAQQFG
110 120 130 140 150
VRGYPTIKFF RNGDKAAPRE YTAGREADDI VSWLKKRTGP AATTLTDAAA
160 170 180 190 200
AETLVDSSEV VVIGFFKDVT SDAAKEFLLA AESVDDIPFG ISSSADVFSK
210 220 230 240 250
YQLSQDGVVL FKKFDEGRNN FEGDLTKDNL LNFIKSNQLP LVIEFTEQTA
260 270 280 290 300
PKIFGGEIKT HILLFLPKSV SDYEGKLDNF KTAAGNFKGK ILFIFIDSDH
310 320 330 340 350
SDNQRILEFF GLKKEECPAV RLITLEEEMT KYKPESDDLT ADKIKEFCNK
360 370 380 390 400
FLEGKIKPHL MSQDLPEDWD KQPVKVLVGK NFEEVAFDEN KNVFVEFYAP
410 420 430 440 450
WCGHCKQLAP IWDKLGETYR DHENIVIAKM DSTANEVEAV KIHSFPTLKF
460 470 480 490 500
FPAGSGRNVI DYNGERTLEG FKKFLESGGQ DGAAADDDLE DLETDEETDL
510
EEGDDDEQKI QKDEL
Length:515
Mass (Da):57,410
Last modified:May 16, 2003 - v3
Checksum:iE7CC978A5109C2CE
GO

Sequence cautioni

The sequence AAA49054.2 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231E → Q1 PublicationCurated
Sequence conflicti23 – 231E → Q(PubMed:2852147)Curated
Sequence conflicti94 – 952EL → DV(PubMed:2852147)Curated
Sequence conflicti359 – 3591H → Q(PubMed:2852147)Curated
Sequence conflicti447 – 4471T → M in CAB57801. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11147 mRNA. Translation: AAA49054.2. Different initiation.
X13110 mRNA. Translation: CAA31502.1.
X06768 Genomic DNA. Translation: CAB57801.1.
PIRiS02084. ISCHSS.
RefSeqiNP_001185639.1. NM_001198710.1.
UniGeneiGga.4976.

Genome annotation databases

GeneIDi374091.
KEGGigga:374091.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11147 mRNA. Translation: AAA49054.2 . Different initiation.
X13110 mRNA. Translation: CAA31502.1 .
X06768 Genomic DNA. Translation: CAB57801.1 .
PIRi S02084. ISCHSS.
RefSeqi NP_001185639.1. NM_001198710.1.
UniGenei Gga.4976.

3D structure databases

ProteinModelPortali P09102.
SMRi P09102. Positions 26-362, 373-476.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000011689.

Proteomic databases

PaxDbi P09102.
PRIDEi P09102.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 374091.
KEGGi gga:374091.

Organism-specific databases

CTDi 5034.

Phylogenomic databases

eggNOGi COG0526.
HOGENOMi HOG000162459.
HOVERGENi HBG005920.
InParanoidi P09102.
KOi K09580.
PhylomeDBi P09102.

Enzyme and pathway databases

SABIO-RK P09102.

Miscellaneous databases

NextBioi 20813610.
PROi P09102.

Family and domain databases

Gene3Di 3.40.30.10. 4 hits.
InterProi IPR005788. Disulphide_isomerase.
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.
TIGR01126. pdi_dom. 2 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPDIA1_CHICK
AccessioniPrimary (citable) accession number: P09102
Secondary accession number(s): Q90969
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 16, 2003
Last modified: October 29, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3