PDI1_CAEEL
ID PDI1_CAEEL Reviewed; 485 AA.
AC Q17967;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protein disulfide-isomerase 1;
DE Short=PDI 1;
DE EC=5.3.4.1;
DE AltName: Full=Prolyl 4-hydroxylase subunit beta-1;
DE Flags: Precursor;
GN Name=pdi-1; ORFNames=C14B1.1;
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 [GENOMIC DNA].
RX PubMed=8760355; DOI=10.1042/bj3170721;
RA Veijola J., Annunen P., Koivunen P., Page A.P., Pihlajaniemi T.,
RA Kivirikko K.I.;
RT "Baculovirus expression of two protein disulphide isomerase isoforms from
RT Caenorhabditis elegans and characterization of prolyl 4-hydroxylases
RT containing one of these polypeptides as their beta subunit.";
RL Biochem. J. 317:721-729(1996).
RN [2]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; U95074; AAB94647.1; -; Genomic_DNA.
DR EMBL; Z37139; CAA85491.1; -; Genomic_DNA.
DR PIR; S71863; S71863.
DR RefSeq; NP_497746.1; NM_065345.5.
DR AlphaFoldDB; Q17967; -.
DR SMR; Q17967; -.
DR BioGRID; 40712; 14.
DR DIP; DIP-24653N; -.
DR IntAct; Q17967; 1.
DR MINT; Q17967; -.
DR STRING; 6239.C14B1.1.1; -.
DR EPD; Q17967; -.
DR PaxDb; Q17967; -.
DR PeptideAtlas; Q17967; -.
DR EnsemblMetazoa; C14B1.1.1; C14B1.1.1; WBGene00003962.
DR GeneID; 175472; -.
DR KEGG; cel:CELE_C14B1.1; -.
DR UCSC; C14B1.1.1; c. elegans.
DR CTD; 175472; -.
DR WormBase; C14B1.1; CE00897; WBGene00003962; pdi-1.
DR eggNOG; KOG0190; Eukaryota.
DR GeneTree; ENSGT00970000196645; -.
DR HOGENOM; CLU_025879_1_0_1; -.
DR InParanoid; Q17967; -.
DR OMA; PTLKLWP; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; Q17967; -.
DR PRO; PR:Q17967; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003962; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:WormBase.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IDA:WormBase.
DR GO; GO:0080058; P:protein deglutathionylation; IDA:WormBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..485
FT /note="Protein disulfide-isomerase 1"
FT /id="PRO_0000034203"
FT DOMAIN 21..130
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 342..470
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 482..485
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 396
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 394
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 395
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 456
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT DISULFID 52..55
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 393..396
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 485 AA; 53436 MW; 74070D655E6A415C CRC64;
MSLSVSFIFL LVASIGAVVA DSENVLVLTE SNFEETINGN EFVLVKFYAP WCVHCKSLAP
KYDEAADLLK EEGSDIKLAK VDATENQALA SKFEVRGYPT ILYFKSGKPT KYTGGRATAQ
IVDWVKKKSG PTVTTVESVE QLEELKGKTR VVVLGYFKDA KSDAATIYNE VADSVDDAFF
AVAGSAEVAA AASLNEDGVA LIRTDGDDSE TSTIAEAEIT NTIALKQWLH AYKLSAVTEF
THESAQEIVG GDLKKFHFLI IRKSDSSFDE TIAKFTEVAK KFRAKIVFVL LDVDVEENAR
ILEFLGVDAK NTPANRIVSL ADQVEKFKPQ EGEDFEAFTN SYLEGKSAQD LKAQDLPEDW
NALPVKVLVA SNFNEIALDE TKTVFVKFYA PWCGHCKQLV PVWDELAEKY ESNPNVVIAK
LDATLNELAD VKVNSFPTLK LWPAGSSTPV DYDGDRNLEK FEEFVNKYAG SASESETASQ
DHEEL
