ID A0A2C9W3F7_MANES Unreviewed; 533 AA.
AC A0A2C9W3F7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=MANES_04G128900 {ECO:0000313|EMBL:OAY53008.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY53008.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY53008.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY53008.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347}.
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; CM004390; OAY53008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9W3F7; -.
DR STRING; 3983.A0A2C9W3F7; -.
DR EnsemblPlants; OAY53008; OAY53008; MANES_04G128900.
DR Gramene; OAY53008; OAY53008; MANES_04G128900.
DR OMA; FTPWCIN; -.
DR OrthoDB; 314307at2759; -.
DR Proteomes; UP000091857; Chromosome lg4.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF189; PROTEIN DISULFIDE ISOMERASE-LIKE 1-5-RELATED; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..533
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012813140"
FT DOMAIN 59..183
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 395..533
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 533 AA; 60376 MW; E774A0AB46844643 CRC64;
MFPRKPISRF VLFTFTLLLL LTSKISVTAA EDSEIDTEND EELEELIAID EQGEDEDHRQ
QGDQQKEAEV LSKAQRIVLE LNSDNAKRVI NENEFVMILG YAPWCPRSAE LMPQFAEAAN
RLKEFGSPLL MSKLDAERYP KAASTLDIKG FPTLLLFVNG SSQVYTGGFS AEDILIWARK
KTGAPVIRIR SVIEAEEFLK NYYMFIFGFF QKFEGHDYEE FVKAATSDNE IQFVEVSDPG
VAKVLYPDRK STNFIGIVKS EPEKYTAYEG TFEMDKILQF LDHNKFPLVT KLTELNSGRV
YSSPIKLQVM VFAEADDFKN LIQPLQEVAR KFKTQIMFIY IDIADENLAK PFLTLYGLED
SENIAVTAFD NKIHSKYLLE ADPTPSNIEE FCSAFLRGSL SPYFKSQPIP DNKEADVQVI
VGKTFDGLVL NSPKNVLLEV YTPWCINCET TSKKIEKLAK HFKGLENLVF GKIDASANEH
AKLQVDDYPT LLFYPVGDKA NPIMLSSKSS SKELAAVINK YVRAKEQSTK DEL
//