ID A0A443NZQ4_9MAGN Unreviewed; 571 AA.
AC A0A443NZQ4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN ORFNames=CKAN_01272700 {ECO:0000313|EMBL:RWR83946.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR83946.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR83946.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR83946.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWR83946.1}.
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DR EMBL; QPKB01000004; RWR83946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443NZQ4; -.
DR STRING; 337451.A0A443NZQ4; -.
DR Proteomes; UP000283530; Unassembled WGS sequence.
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; 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 PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF246; PROTEIN DISULFIDE-ISOMERASE; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:RWR83946.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR605792-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000283530};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..571
FT /note="protein disulfide-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019304883"
FT DOMAIN 85..199
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 412..541
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 26..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 124..127
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 462..465
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 571 AA; 62847 MW; 383B879284B94B44 CRC64;
MAIRKLLFVL SISAILLSHG FSSATTSKEI EDLEEEDLSF LEEDDESAAT SSKNSFSDLD
HGSGDHEPEN VDDFEGSDSD HGGYSPPAPP AVDEKDVVVL AKGNFSEFLE KNQYVMVEFY
APWCGHCHAL APVYAAAATE LKGKAVLAKV DATVENDLAQ KYDVQGFPTV IFFVDGVHRP
YPGQRNKDAI VTWIKKKTGP SIHNVTTTEE AETILTSEDK LVLGFLGSLV CPESQELAAV
SRLEDDVSFY QTTNPDVAKL FHIDSKAKSP ALVMLKKDDE KIVHFDGEFT KSAIVDFVFA
NKLPLVTTFS RESASLIFEN PIKKQLLLFA SKSDSDKVLP IFQESAKLFK GKLLFVSVER
DNEDVGKPVS EYFGVTGDGP KVLAYEGIDD PKKYILDGEL TLDSVKAFGE GFLENKLKPF
YKSDPIPDTN DGDIKIVVGD NVDEIVLDDS KDVLLEVYAP WCGHCQALEP IYNKLAKHLR
GIESLVIAKM DGTTNEHPRI KADGFPTILF FPAGKKSSGP LPVETDRTVV AFYKFIKKHA
SIPFKLQKPE SAVKSASEKS GSKEEDVKDE L
//
