ID W9S6C4_9ROSA Unreviewed; 339 AA.
AC W9S6C4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN ORFNames=L484_012764 {ECO:0000313|EMBL:EXC13336.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC13336.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) 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 -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR EMBL; KE345743; EXC13336.1; -; Genomic_DNA.
DR RefSeq; XP_010107024.1; XM_010108722.1.
DR AlphaFoldDB; W9S6C4; -.
DR STRING; 981085.W9S6C4; -.
DR eggNOG; KOG0191; Eukaryota.
DR Proteomes; UP000030645; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd00238; ERp29c; 1.
DR CDD; cd02998; PDI_a_ERp38; 2.
DR Gene3D; 1.20.1150.12; Endoplasmic reticulum resident protein 29, C-terminal domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR011679; ERp29_C.
DR InterPro; IPR036356; ERp29_C_sf.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01126; pdi_dom; 2.
DR PANTHER; PTHR45672:SF11; PROTEIN DISULFIDE-ISOMERASE C17H9.14C; 1.
DR PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR Pfam; PF07749; ERp29; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF47933; ERP29 C domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EXC13336.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..339
FT /note="protein disulfide-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004931846"
FT DOMAIN 16..132
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 135..242
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 339 AA; 37990 MW; 57D0F28EE1B3AE0C CRC64;
MLSSKSFYVI RTLALLFVSS VFADDVVVLT ESNFDKEVGQ DRGALVEFYA PWCGHCKKLA
PEYEKLGASF KKAKSVLIGK VDCDEHKSLC SKYGVSGYPT IQWFPKGFLE PKKYEGARGA
EALAEFVKKE GRTNVKIAAV PSNVVVLTPH DFDEIVLNNE KDVLVEFYAP WCGHCKSLAP
IYEKVASAFK LDADKHRDLA EKYGVSGYPT LKFFPKSNKA REDYDGGRDL DDFVTFINEK
CGTSRDGKGQ LTSKVVAALN DLVKEFVNAG NDEKKILAKI EEEVEKLKGA TARYSKIYVK
AAKNSLEKGA DYSKKEIQRL ERMLEKVYLI LFFFLVLSS
//
