PDI2_CAEEL
ID PDI2_CAEEL Reviewed; 493 AA.
AC Q17770;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Protein disulfide-isomerase 2;
DE EC=5.3.4.1;
DE AltName: Full=PDI 1;
DE AltName: Full=Prolyl 4-hydroxylase subunit beta-2;
DE Flags: Precursor;
GN Name=pdi-2; ORFNames=C07A12.4;
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 [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).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=10805750; DOI=10.1128/mcb.20.11.4084-4093.2000;
RA Winter A.D., Page A.P.;
RT "Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required
RT for exoskeleton formation and the maintenance of body shape in the nematode
RT Caenorhabditis elegans.";
RL Mol. Cell. Biol. 20:4084-4093(2000).
RN [4]
RP SUBUNIT.
RX PubMed=12036960; DOI=10.1074/jbc.m203824200;
RA Myllyharju J., Kukkola L., Winter A.D., Page A.P.;
RT "The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl
RT 4-hydroxylases with unique combinations of subunits.";
RL J. Biol. Chem. 277:29187-29196(2002).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-334, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21199936; DOI=10.1073/pnas.1006328108;
RA Stenvall J., Fierro-Gonzalez J.C., Swoboda P., Saamarthy K., Cheng Q.,
RA Cacho-Valadez B., Arner E.S., Persson O.P., Miranda-Vizuete A., Tuck S.;
RT "Selenoprotein TRXR-1 and GSR-1 are essential for removal of old cuticle
RT during molting in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1064-1069(2011).
CC -!- FUNCTION: Involved in cuticle formation (PubMed:10805750). May play a
CC role in the unfolded protein response (PubMed:21199936).
CC {ECO:0000269|PubMed:10805750, ECO:0000269|PubMed:21199936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains. Exist
CC either as a phy-1(2)/pdi-2(2) tetramer, a phy-2(2)/pdi-2(2) tetramer or
CC as a phy-1/phy-2/pdi-2(2) tetramer. {ECO:0000269|PubMed:12036960}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- DEVELOPMENTAL STAGE: Expressed in oscillating waves in hypodermal cells
CC during the 4 larval stages and in adults.
CC {ECO:0000269|PubMed:10805750}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes embryonic
CC lethality characterized by a retraction of the fully elongated embryo,
CC a progressive disorganization of the embryo and a failure to hatch
CC (PubMed:10805750). Also causes increased expression of the unfolded
CC protein response (UPR) marker hsp-4 (PubMed:21199936).
CC {ECO:0000269|PubMed:10805750, ECO:0000269|PubMed:21199936}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; FO080373; CCD63277.1; -; Genomic_DNA.
DR PIR; S71862; S71862.
DR PIR; T34092; T34092.
DR RefSeq; NP_508778.1; NM_076377.3.
DR AlphaFoldDB; Q17770; -.
DR SMR; Q17770; -.
DR BioGRID; 45659; 19.
DR IntAct; Q17770; 5.
DR MINT; Q17770; -.
DR STRING; 6239.C07A12.4a.1; -.
DR iPTMnet; Q17770; -.
DR EPD; Q17770; -.
DR PaxDb; Q17770; -.
DR PeptideAtlas; Q17770; -.
DR EnsemblMetazoa; C07A12.4.1; C07A12.4.1; WBGene00003963.
DR EnsemblMetazoa; C07A12.4.2; C07A12.4.2; WBGene00003963.
DR GeneID; 180724; -.
DR KEGG; cel:CELE_C07A12.4; -.
DR UCSC; C07A12.4a.1; c. elegans.
DR CTD; 180724; -.
DR WormBase; C07A12.4; CE03972; WBGene00003963; pdi-2.
DR eggNOG; KOG0190; Eukaryota.
DR GeneTree; ENSGT00940000168917; -.
DR InParanoid; Q17770; -.
DR OMA; FCDRFLE; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; Q17770; -.
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 Reactome; R-CEL-8964041; LDL remodeling.
DR PRO; PR:Q17770; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003963; Expressed in embryo and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016222; C:procollagen-proline 4-dioxygenase complex; IDA:WormBase.
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:0030968; P:endoplasmic reticulum unfolded protein response; HEP:WormBase.
DR GO; GO:0043412; P:macromolecule modification; IDA:WormBase.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; 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; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..493
FT /note="Protein disulfide-isomerase 2"
FT /id="PRO_0000034204"
FT DOMAIN 17..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 REGION 467..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 490..493
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT COMPBIAS 478..493
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 52
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 396
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 53
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 54
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 116
FT /note="Lowers pKa of C-terminal Cys of first active site"
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 CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
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 493 AA; 55152 MW; 41BC0C1185EBFB5E CRC64;
MFRLVGLFFL VLGASAAVIE EEENVIVLTK DNFDEVINGN EFILVEFYAP WCGHCKSLAP
EYAKAATQLK EEGSDIKLGK LDATVHGEVS SKFEVRGYPT LKLFRNGKPQ EYNGGRDHDS
IIAWLKKKTG PVAKPLADAD AVKELQESAD VVVIGYFKDT TSDDAKTFLE VAAGIDDVPF
GISTEDAVKS EIELKGEGIV LFKKFDDGRV AFDEKLTQDG LKTWIQANRL ALVSEFTQET
ASVIFGGEIK SHNLLFVSKE SSEFAKLEQE FKNAAKQFKG KVLFVYINTD VEENARIMEF
FGLKKDELPA IRLISLEEDM TKFKPDFEEI TTENISKFTQ NYLDGSVKPH LMSEDIPEDW
DKNPVKILVG KNFEQVARDN TKNVLVEFYA PWCGHCKQLA PTWDKLGEKF ADDESIVIAK
MDSTLNEVED VKIQSFPTIK FFPAGSNKVV DYTGDRTIEG FTKFLETNGK EGAGASEEEK
AEEEADEEGH TEL
