PDIA6_CAEEL
ID PDIA6_CAEEL Reviewed; 440 AA.
AC Q11067;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein disulfide-isomerase A6 homolog {ECO:0000303|PubMed:24508390};
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:Q15084};
DE Flags: Precursor;
GN Name=pdi-6 {ECO:0000303|PubMed:24508390, ECO:0000312|WormBase:B0403.4};
GN Synonyms=tag-320 {ECO:0000312|WormBase:B0403.4};
GN ORFNames=B0403.4 {ECO:0000312|WormBase:B0403.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24508390; DOI=10.1016/j.molcel.2014.01.004;
RA Eletto D., Eletto D., Dersh D., Gidalevitz T., Argon Y.;
RT "Protein disulfide isomerase A6 controls the decay of IRE1alpha signaling
RT via disulfide-dependent association.";
RL Mol. Cell 53:562-576(2014).
CC -!- FUNCTION: May function as a chaperone that inhibits aggregation of
CC misfolded proteins (By similarity). May negatively regulate the
CC unfolded protein response (UPR) through binding to UPR sensors
CC (PubMed:24508390). {ECO:0000250|UniProtKB:Q15084,
CC ECO:0000269|PubMed:24508390}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:Q15084};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q15084}.
CC -!- DISRUPTION PHENOTYPE: Lethal at the early stages of larval development.
CC Arrested larvae are small and display molting defects. RNAi-mediated
CC knockdown results in reduced fecundity, and in induction of the
CC unfolded protein response. {ECO:0000269|PubMed:24508390}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; FO080188; CCD61843.1; -; Genomic_DNA.
DR PIR; T15352; T15352.
DR RefSeq; NP_509190.1; NM_076789.3.
DR AlphaFoldDB; Q11067; -.
DR SMR; Q11067; -.
DR BioGRID; 45900; 6.
DR STRING; 6239.B0403.4; -.
DR iPTMnet; Q11067; -.
DR EPD; Q11067; -.
DR PaxDb; Q11067; -.
DR PeptideAtlas; Q11067; -.
DR EnsemblMetazoa; B0403.4.1; B0403.4.1; WBGene00015168.
DR GeneID; 180974; -.
DR KEGG; cel:CELE_B0403.4; -.
DR UCSC; B0403.4; c. elegans.
DR CTD; 180974; -.
DR WormBase; B0403.4; CE03880; WBGene00015168; pdi-6.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00940000155646; -.
DR HOGENOM; CLU_030311_0_0_1; -.
DR InParanoid; Q11067; -.
DR OMA; DDIWLVE; -.
DR OrthoDB; 840943at2759; -.
DR PhylomeDB; Q11067; -.
DR BRENDA; 5.3.4.1; 1045.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q11067; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00015168; Expressed in pharyngeal muscle cell (C elegans) and 5 other tissues.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; HEP:WormBase.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR044569; PDIA6-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45815; PTHR45815; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 3.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..440
FT /note="Protein disulfide-isomerase A6 homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000034241"
FT DOMAIN 19..131
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 127..273
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 138..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 437..440
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT COMPBIAS 139..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 54
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 57
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 194
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 197
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 55
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 56
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 117
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 195
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 196
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 259
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT DISULFID 54..57
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 194..197
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 440 AA; 47728 MW; 608785076B159578 CRC64;
MALIKLLLAS LAITSVCGMY SKKDDVVELT EANFQSKVIN SDDIWIVEFY APWCGHCKSL
VPEYKKAASA LKGVAKVGAV DMTQHQSVGG PYNVQGFPTL KIFGADKKKP TDYNGQRTAQ
AIADSVLAEA KKAVSARLGG KSSGSSSSGS GSGSGKRGGG GSGNEVVELT DANFEDLVLN
SKDIWLVEFF APWCGHCKSL EPQWKAAASE LKGKVRLGAL DATVHTVVAN KFAIRGFPTI
KYFAPGSDVS DAQDYDGGRQ SSDIVAWASA RAQENMPAPE VFEGINQQVV EDACKEKQLC
IFAFLPHILD CQSECRNNYL AMLKEQSEKF KKNLWGWIWV EGAAQPALEE SFEVGGFGYP
AMTALNFRKN KYAVLKGSFG KDGIHEFLRD LSYGKGRTSS LRGDGFPKIQ KTEKWDGKDG
ALPAEDDIDL SDIDLDKTEL
