ID   PDI_MEDSA               Reviewed;         512 AA.
AC   P29828;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Protein disulfide-isomerase;
DE            Short=PDI;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=PDI;
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].
RC   STRAIN=cv. Apollo;
RX   PubMed=1623182; DOI=10.1007/bf00027354;
RA   Shorrosh B.S., Dixon R.A.;
RT   "Sequence analysis and developmental expression of an alfalfa protein
RT   disulfide isomerase.";
RL   Plant Mol. Biol. 19:319-321(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1720555; DOI=10.1073/pnas.88.23.10941;
RA   Shorrosh B.S., Dixon R.A.;
RT   "Molecular cloning of a putative plant endomembrane protein resembling
RT   vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific
RT   phospholipase C.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:10941-10945(1991).
CC   -!- FUNCTION: Participates in the folding of proteins containing disulfide
CC       bonds, may be involved in glycosylation, prolyl hydroxylation and
CC       triglyceride transfer. {ECO:0000250}.
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}.
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DR   EMBL; Z11499; CAA77575.1; -; mRNA.
DR   EMBL; M82973; AAA32662.1; -; mRNA.
DR   PIR; A41440; A41440.
DR   PIR; S22479; ISAASS.
DR   AlphaFoldDB; P29828; -.
DR   SMR; P29828; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   SUPFAM; SSF52833; SSF52833; 4.
DR   TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR   TIGRFAMs; TIGR01126; pdi_dom; 2.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW   Redox-active center; Repeat; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..512
FT                   /note="Protein disulfide-isomerase"
FT                   /id="PRO_0000034209"
FT   DOMAIN          25..144
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          357..485
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          487..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           509..512
FT                   /note="Prevents secretion from ER"
FT   ACT_SITE        62
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        65
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        407
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        410
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            63
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            64
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            130
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            408
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            409
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            471
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        62..65
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        407..410
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        16
FT                   /note="L -> V (in Ref. 2; AAA32662)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="G -> A (in Ref. 2; AAA32662)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        491
FT                   /note="H -> Q (in Ref. 2; AAA32662)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  57087 MW;  E5EC7341A3FF7935 CRC64;
     MAKNVAIFGL LFSLLLLVPS QIFAEESSTD AKEFVLTLDN TNFHDTVKKH DFIVVEFYAP
     WCGHCKKLAP EYEKAASILS THEPPVVLAK VDANEEHNKD LASENDVKGF PTIKIFRNGG
     KNIQEYKGPR EAEGIVEYLK KQSGPASTEI KSADDATAFV GDNKVVIVGV FPKFSGEEYD
     NFIALAEKLR SDYDFAHTLN AKHLPKGDSS VSGPVVRLFK PFDELFVDSK DFNVEALEKF
     IEESSTPIVT VFNNEPSNHP FVVKFFNSPN AKAMLFINFT TEGAESFKTK YHEVAEQYKQ
     QGVSFLVGDV ESSQGAFQYF GLKEEQVPLI IIQHNDGKKF FKPNLELDQL PTWLKAYKDG
     KVEPFVKSEP IPETNNEPVK VVVGQTLEDV VFKSGKNVLI EFYAPWCGHC KQLAPILDEV
     AVSFQSDADV VIAKLDATAN DIPTDTFDVQ GYPTLYFRSA SGKLSQYDGG RTKEDIIEFI
     EKNKDKTGAA HQEVEQPKAA AQPEAEQPKD EL