ID   TXND9_RAT               Reviewed;         226 AA.
AC   Q8K581;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Thioredoxin domain-containing protein 9;
DE   AltName: Full=ES cell-related protein;
GN   Name=Txndc9;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li Y., Xu C., Zhang Y.;
RT   "Cloning and analysis of up-regulated genes in rat liver.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Significantly diminishes the chaperonin TCP1 complex ATPase
CC       activity, thus negatively impacts protein folding, including that of
CC       actin or tubulin. {ECO:0000250}.
CC   -!- SUBUNIT: Forms ternary complexes with the chaperonin TCP1 complex,
CC       spanning the cylindrical chaperonin cavity and contacting at least 2
CC       subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9CQ79}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9CQ79}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q9CQ79}. Midbody
CC       {ECO:0000250|UniProtKB:Q9CQ79}. Note=Co-localizes with beta-tubulin in
CC       the centrosome. {ECO:0000250|UniProtKB:Q9CQ79}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM34684.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF508022; AAM34684.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q8K581; -.
DR   SMR; Q8K581; -.
DR   STRING; 10116.ENSRNOP00000025098; -.
DR   jPOST; Q8K581; -.
DR   PaxDb; Q8K581; -.
DR   UCSC; RGD:708355; rat.
DR   RGD; 708355; Txndc9.
DR   eggNOG; KOG1672; Eukaryota.
DR   InParanoid; Q8K581; -.
DR   PRO; PR:Q8K581; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005813; C:centrosome; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0030496; C:midbody; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..226
FT                   /note="Thioredoxin domain-containing protein 9"
FT                   /id="PRO_0000120168"
FT   DOMAIN          75..180
FT                   /note="Thioredoxin"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14530"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14530"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14530"
SQ   SEQUENCE   226 AA;  26272 MW;  EDA5BF54C18AE68A CRC64;
     MEGNGSIDMF SEVLENQFLQ AAKLVENHLD SEIQKLDQIG EDELELLKEK RLAALRKAQQ
     QKQEWLSKGH GEYREIGSER DFFQEVKESE KVVCHFYRDT TFRCKILDRH LAILAKKHLE
     TKFLKPNVEK APFLCERLRI KVIPTLALLR DGKTQDYIVG FTDLGNTDDF TTETLEWRLG
     CSDVINYSGN LMEPPFQSQK KFGTNFTKLE KKTIRGKKYD SDSDDD