PDIA4_CAEEL
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 03-AUG-2022, entry version 173.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 11.
DR STRING; 6239.C14B9.2; -.
DR EPD; P34329; -.
DR PaxDb; P34329; -.
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 CTD; 176147; -.
DR WormBase; C14B9.2; CE30601; WBGene00015752; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_6_2_1; -.
DR InParanoid; P34329; -.
DR OMA; ISQPNWT; -.
DR OrthoDB; 462118at2759; -.
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 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 InterPro; IPR005788; Disulphide_isomerase.
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 Pfam; PF00085; Thioredoxin; 3.
DR PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR SUPFAM; SSF52833; SSF52833; 5.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 3.
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
