ID   PDIA6_MEDSA             Reviewed;         364 AA.
AC   P38661;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Probable protein disulfide-isomerase A6;
DE            EC=5.3.4.1;
DE   AltName: Full=P5;
DE   Flags: Precursor;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1303795; DOI=10.1111/j.1365-313x.1992.00051.x;
RA   Shorrosh B.S., Dixon R.A.;
RT   "Molecular characterization and expression of an alfalfa protein with
RT   sequence similarity to mammalian ERp72, a glucose-regulated endoplasmic
RT   reticulum protein containing active site sequences of protein disulphide
RT   isomerase.";
RL   Plant J. 2:51-58(1992).
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:0000250}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; M80235; AAB46930.1; -; mRNA.
DR   PIR; T09614; T09614.
DR   AlphaFoldDB; P38661; -.
DR   SMR; P38661; -.
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; cd00238; ERp29c; 1.
DR   Gene3D; 1.20.1150.12; -; 1.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR011679; ERp29_C.
DR   InterPro; IPR036356; ERp29_C_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF07749; ERp29; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   SUPFAM; SSF47933; SSF47933; 1.
DR   SUPFAM; SSF52833; SSF52833; 2.
DR   TIGRFAMs; TIGR01126; pdi_dom; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center;
KW   Repeat; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..364
FT                   /note="Probable protein disulfide-isomerase A6"
FT                   /id="PRO_0000034243"
FT   DOMAIN          29..137
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          139..256
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        58
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        61
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        177
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        180
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            59
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            60
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            123
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            178
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            179
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            242
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..61
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        177..180
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   364 AA;  40492 MW;  7496F4093C3A01E6 CRC64;
     MKMEMHQIWS RIALASFAFA ILFVSVSADD VVVLTEENFE KEVGHDKGAL VEFYAPWCGH
     CKKLAPEYEK LPNSFKKAKS VLIAKVDCDE HKSVCSKYGV SGYPTIQWFP KGSLEPKKFE
     GPRTAESLAE FVNTEGGTNV KIATAPSHVV VLTPETFNEV VLDGTKDVLV EFYAPWCGHC
     KSLAPIYEKV AAVFKSEDDV VIANLDADKY RDLAEKYDVS GFPTLKFFPK GNKAGEDYGG
     GRDLDDFVAF INEKSGTSRD AKGQLTSEAG IVEDLDELVK EFVAANDEEK KAVFARIEEE
     VKKLEGSASR YGKIYLKVSK KYLEKGSDYA KNEIQRLERL LEKSISPAKA DELTLKKNIL
     STYA