PDI_HUMIN
ID PDI_HUMIN Reviewed; 505 AA.
AC P55059;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Protein disulfide-isomerase;
DE Short=PDI;
DE EC=5.3.4.1;
DE Flags: Precursor;
OS Humicola insolens (Soft-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Humicola.
OX NCBI_TaxID=34413;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=KASI;
RX PubMed=7765273; DOI=10.1271/bbb.58.1424;
RA Kajino T., Sarai K., Imaeda T., Idekoba C., Asami O., Yamada Y., Hirai M.,
RA Udaka S.;
RT "Molecular cloning of a fungal cDNA encoding protein disulfide isomerase.";
RL Biosci. Biotechnol. Biochem. 58:1424-1429(1994).
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; S74296; AAC60578.1; -; mRNA.
DR PIR; JC2291; JC2291.
DR PDB; 2DJJ; NMR; -; A=354-469.
DR PDB; 2DJK; NMR; -; A=228-355.
DR PDB; 2KP1; NMR; -; A=354-469.
DR PDB; 2KP2; NMR; -; A=228-355.
DR PDB; 2RUE; NMR; -; A=354-469.
DR PDB; 2RUF; NMR; -; A=354-469.
DR PDB; 3WT1; X-ray; 1.85 A; A/B/C/D=228-469.
DR PDB; 3WT2; X-ray; 3.30 A; A/B/C=228-469.
DR PDB; 5CRW; X-ray; 1.60 A; A=228-469.
DR PDBsum; 2DJJ; -.
DR PDBsum; 2DJK; -.
DR PDBsum; 2KP1; -.
DR PDBsum; 2KP2; -.
DR PDBsum; 2RUE; -.
DR PDBsum; 2RUF; -.
DR PDBsum; 3WT1; -.
DR PDBsum; 3WT2; -.
DR PDBsum; 5CRW; -.
DR AlphaFoldDB; P55059; -.
DR BMRB; P55059; -.
DR SMR; P55059; -.
DR BRENDA; 5.3.4.1; 2710.
DR EvolutionaryTrace; P55059; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR IDEAL; IID50214; -.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Endoplasmic reticulum; Isomerase;
KW Redox-active center; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..505
FT /note="Protein disulfide-isomerase"
FT /id="PRO_0000034215"
FT DOMAIN 21..128
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 335..465
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 470..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 502..505
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 474..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 50
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 53
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 385
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 388
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 51
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 52
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 113
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 386
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 387
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 451
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT DISULFID 50..53
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 385..388
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:5CRW"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:5CRW"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:5CRW"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:5CRW"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:5CRW"
FT HELIX 256..272
FT /evidence="ECO:0007829|PDB:5CRW"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:5CRW"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:5CRW"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:5CRW"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:5CRW"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:5CRW"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:5CRW"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:5CRW"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:3WT2"
FT HELIX 325..337
FT /evidence="ECO:0007829|PDB:5CRW"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:5CRW"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:5CRW"
FT STRAND 374..381
FT /evidence="ECO:0007829|PDB:5CRW"
FT HELIX 386..403
FT /evidence="ECO:0007829|PDB:5CRW"
FT TURN 406..410
FT /evidence="ECO:0007829|PDB:5CRW"
FT STRAND 411..417
FT /evidence="ECO:0007829|PDB:5CRW"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:5CRW"
FT STRAND 429..436
FT /evidence="ECO:0007829|PDB:5CRW"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:2RUE"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:2KP1"
FT HELIX 453..463
FT /evidence="ECO:0007829|PDB:5CRW"
SQ SEQUENCE 505 AA; 55114 MW; 27E7C0D1A61B5F95 CRC64;
MHKAQKFALG LLAAAAVATA SDVVQLKKDT FDDFIKTNDL VLAEFFAPWC GHCKALAPEY
EEAATTLKEK NIKLAKVDCT EETDLCQQHG VEGYPTLKVF RGLDNVSPYK GQRKAAAITS
YMIKQSLPAV SEVTKDNLEE FKKADKAVLV AYVDASDKAS SEVFTQVAEK LRDNYPFGSS
SDAALAEAEG VKAPAIVLYK DFDEGKAVFS EKFEVEAIEK FAKTGATPLI GEIGPETYSD
YMSAGIPLAY IFAETAEERK ELSDKLKPIA EAQRGVINFG TIDAKAFGAH AGNLNLKTDK
FPAFAIQEVA KNQKFPFDQE KEITFEAIKA FVDDFVAGKI EPSIKSEPIP EKQEGPVTVV
VAKNYNEIVL DDTKDVLIEF YAPWCGHCKA LAPKYEELGA LYAKSEFKDR VVIAKVDATA
NDVPDEIQGF PTIKLYPAGA KGQPVTYSGS RTVEDLIKFI AENGKYKAAI SEDAEETSSA
TETTTETATK SEEAAKETAT EHDEL
