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 27-MAR-2024, entry version 124. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P29828; 1 site, No reported glycans. 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; cd02961; PDI_a_family; 1. DR CDD; cd02995; PDI_a_PDI_a'_C; 1. DR CDD; cd02982; PDI_b'_family; 1. DR CDD; cd02981; PDI_b_family; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 4. DR InterPro; IPR005788; PDI_thioredoxin-like_dom. 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; 2. DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1. DR PANTHER; PTHR18929:SF254; PROTEIN DISULFIDE ISOMERASE-LIKE 1-1; 1. DR Pfam; PF00085; Thioredoxin; 2. DR Pfam; PF13848; Thioredoxin_6; 1. DR PRINTS; PR00421; THIOREDOXIN. DR SUPFAM; SSF52833; Thioredoxin-like; 4. 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 //