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Database: UniProt
Entry: A0A2C9W3F7_MANES
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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}.
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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
//
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