ID   PDIA4_CAEEL             Reviewed;         618 AA.
AC   P34329;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Probable protein disulfide-isomerase A4;
DE            EC=5.3.4.1;
DE   AltName: Full=ERp-72 homolog;
DE   Flags: Precursor;
GN   ORFNames=C14B9.2;
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=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
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; FO080531; CCD64436.1; -; Genomic_DNA.
DR   PIR; S44756; S44756.
DR   RefSeq; NP_498775.2; NM_066374.7.
DR   AlphaFoldDB; P34329; -.
DR   SMR; P34329; -.
DR   BioGRID; 41353; 12.
DR   STRING; 6239.C14B9.2.1; -.
DR   EPD; P34329; -.
DR   PaxDb; 6239-C14B9-2; -.
DR   PeptideAtlas; P34329; -.
DR   EnsemblMetazoa; C14B9.2.1; C14B9.2.1; WBGene00015752.
DR   GeneID; 176147; -.
DR   KEGG; cel:CELE_C14B9.2; -.
DR   UCSC; C14B9.2.1; c. elegans.
DR   AGR; WB:WBGene00015752; -.
DR   WormBase; C14B9.2; CE30601; WBGene00015752; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   HOGENOM; CLU_025879_6_2_1; -.
DR   InParanoid; P34329; -.
DR   OMA; FRSKHEP; -.
DR   OrthoDB; 5399045at2759; -.
DR   PhylomeDB; P34329; -.
DR   PRO; PR:P34329; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00015752; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; HEP: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   CDD; cd02961; PDI_a_family; 2.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd03073; PDI_b'_ERp72_ERp57; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 5.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR017068; Protein_diS-isomerase_A4.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR   NCBIfam; TIGR01126; pdi_dom; 3.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF210; PROTEIN DISULFIDE-ISOMERASE A4; 1.
DR   Pfam; PF00085; Thioredoxin; 3.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 5.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 3.
DR   PROSITE; PS51352; THIOREDOXIN_2; 3.
PE   3: Inferred from homology;
KW   Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..618
FT                   /note="Probable protein disulfide-isomerase A4"
FT                   /id="PRO_0000034232"
FT   DOMAIN          22..139
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          138..254
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          480..609
FT                   /note="Thioredoxin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           615..618
FT                   /note="Prevents secretion from ER"
FT   DISULFID        65..68
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        176..179
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        529..532
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   618 AA;  69797 MW;  1DC0207A71444220 CRC64;
     MMFDRRFFAL VVLLCVSAVR STEDASDDEL NYEMDEGVVV LTDKNFDAFL KKNPSVLVKF
     YAPWCGHCKH LAPEYEKASS KVSIPLAKVD ATVETELGKR FEIQGYPTLK FWKDGKGPND
     YDGGRDEAGI VEWVESRVDP NYKPPPEEVV TLTTENFDDF ISNNELVLVE FYAPWCGHCK
     KLAPEYEKAA QKLKAQGSKV KLGKVDATIE KDLGTKYGVS GYPTMKIIRN GRRFDYNGPR
     EAAGIIKYMT DQSKPAAKKL PKLKDVERFM SKDDVTIIGF FATEDSTAFE AFSDSAEMLR
     EEFKTMGHTS DPAAFKKWDA KPNDIIIFYP SLFHSKFEPK SRTYNKAAAT SEDLLAFFRE
     HSAPLVGKMT KKNAATRYTK KPLVVVYYNA DFSVQYREGS EYWRSKVLNI AQKYQKDKYK
     FAVADEEEFA KELEELGLGD SGLEHNVVVF GYDGKKYPMN PDEFDGELDE NLEAFMKQIS
     SGKAKAHVKS APAPKDDKGP VKTVVGSNFD KIVNDESKDV LIEFYAPWCG HCKSFESKYV
     ELAQALKKTQ PNVVLAKMDA TINDAPSQFA VEGFPTIYFA PAGKKSEPIK YSGNRDLEDL
     KKFMTKHGVK SFQKKDEL
//