ID A8XPB1_CAEBR Unreviewed; 616 AA.
AC A8XPB1;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Protein disulfide-isomerase A4 {ECO:0000256|PIRNR:PIRNR036862};
DE EC=5.3.4.1 {ECO:0000256|PIRNR:PIRNR036862};
DE AltName: Full=ERp-72 homolog {ECO:0000256|PIRNR:PIRNR036862};
GN ORFNames=CBG16681 {ECO:0000313|EMBL:CAP34591.1,
GN ECO:0000313|WormBase:CBG16681}, CBG_16681
GN {ECO:0000313|EMBL:CAP34591.1};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP34591.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP34591.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP34591.1,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182,
CC ECO:0000256|PIRNR:PIRNR036862, ECO:0000256|RuleBase:RU361130};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319, ECO:0000256|PIRNR:PIRNR036862}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|PIRNR:PIRNR036862,
CC ECO:0000256|RuleBase:RU004208}.
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DR EMBL; HE600949; CAP34591.1; -; Genomic_DNA.
DR RefSeq; XP_002641974.1; XM_002641928.1.
DR AlphaFoldDB; A8XPB1; -.
DR STRING; 6238.A8XPB1; -.
DR EnsemblMetazoa; CBG16681.1; CBG16681.1; WBGene00036560.
DR GeneID; 8583968; -.
DR KEGG; cbr:CBG_16681; -.
DR CTD; 8583968; -.
DR WormBase; CBG16681; CBP03985; WBGene00036560; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_6_2_1; -.
DR InParanoid; A8XPB1; -.
DR OMA; FRSKHEP; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
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: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; PS00194; THIOREDOXIN_1; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR036862};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR036862};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR605792-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 22..616
FT /note="Protein disulfide-isomerase A4"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005122090"
FT DOMAIN 10..134
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 136..252
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 478..607
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 174..177
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 527..530
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 616 AA; 69659 MW; E4B6B65A22B9EF4A CRC64;
MLFDRRIFAL VVVVCLSAIH AEETDEELNY EMDEGVVVLT DKNFDAFLKK NPSTLVKFYA
PWCGHCKHLA PEYEKATSRV SIPLAKVDAT VETELGKRFE IQGYPTLKFW KDGKGPTDYD
GGRDEAGIVE WVESRVDPNY KPPPEEVVTL TTENFDDFIS NNELVLVEFY APWCGHCKKL
APEYEKAAQK LKAQGSKVRL GKVDATIEKD LGTKYGVSGY PTMKVIRNGR RFDYNGPREA
AGIVKYMTEQ SKPAATKLAK LKDIERFMSK DDVTIIGFFA TEDSSAFEAF SDSAEMLREE
FKTMGHTSDP AAFKKWDAKP NDIIIFYPSL FHSKFEPKSR TYNKASATSE DLLAFFREHS
APLVGKMTKK NAATRYTKKP LVVVYYNADF SVQYREGSEY WRQKVLNIAQ KYQKDKYRFA
VADEEEFTTE LSELGLGDSG LEHNVVVFGY DGKKYPMNPD DFDGELDENL EAFMKQISSG
KAKAHVKSAP APKDDKGPVK TVVGSNFDKI VNDESKDVLI EFYAPWCGHC KSFEPKYKEL
AQALKKSQPN VVLAKMDATI NDAPSQFAVE GFPTIYFAPS GKKTEPIKYS GNRDLEDLKK
FMTKHGVKSF QKKDEL
//
