ID Q587N4_BOMMO Unreviewed; 491 AA.
AC Q587N4;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 116.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
GN Name=erp57 {ECO:0000313|EMBL:BAD93613.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000313|EMBL:BAD93613.1};
RN [1] {ECO:0000313|EMBL:BAD93613.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nd-sD {ECO:0000313|EMBL:BAD93613.1};
RA Ozawa R., Yamashita T.;
RT "ERp57 expressed in posterior silkgland of Bombyx mori.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361130};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR EMBL; AB210111; BAD93613.1; -; mRNA.
DR AlphaFoldDB; Q587N4; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd02997; PDI_a_PDIR; 1.
DR CDD; cd03073; PDI_b'_ERp72_ERp57; 1.
DR CDD; cd03069; PDI_b_ERp57; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR046374; PDI_a_PDIR.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR041868; PDIA3_PDI_b.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
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; 1.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF132; PROTEIN DISULFIDE-ISOMERASE A3; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR605792-51}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 20..491
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005143544"
FT DOMAIN 5..131
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 344..472
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 51..54
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 393..396
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 491 AA; 55103 MW; E66C57E638044AFD CRC64;
MFGSLKFVLL LGIIYLCKAA EEDVLDLTDS DFSAVLSQHD TALVMFYAPW CGHCKRLKPE
YAVAAGLLKT DDPPVALAKV DCTEGGKSTC EQFSVSGYPT LKIFRKGELS SEYNGPRESN
GIVKYMRAQV GPSSKELLTV ADFEAFTSKD EVVVVGFFEK ESDLKGEFLK TADKLREEVT
FAHSSANEVL EKTGYKNNVV LYRPKRLQNK FEDSSVAFDG DTEKVSLKAF IKENYHGLVG
VRQKDNIHDF SNPLIVAYYD VDYTKNPKGT NYWRNRVLKV AKEQTEATFA VSDKDDFTHE
LNEFGIDFAK GDKPVVAGRD ADGNKFVMSA EFSIENLLTF TKDLLDGKLE PFVKSEAIPE
NDGPVKVAVG KNFKELVTDS NRDALIEFYA PWCGHCQKLA PVWEELGEKL KDEEVDIIKI
DATANDWPKS QFDVSGFPTI FWKPKDSSKK PQRYNGGRAL EDFIKYVSEQ ATSELKGWDR
KGNAKQGKEE L
//
