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TXND9_BOVIN
ID   TXND9_BOVIN             Reviewed;         226 AA.
AC   O18883; Q17QD0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Thioredoxin domain-containing protein 9;
DE   AltName: Full=Protein 1-4;
GN   Name=TXNDC9; Synonyms=APACD;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal lung;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-226.
RC   TISSUE=Corpus luteum;
RA   Brule S., Lussier J.G.;
RT   "Bovine ATP binding protein.";
RL   Submitted (OCT-1997) 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=AAB84006.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC118430; AAI18431.1; -; mRNA.
DR   EMBL; AF027733; AAB84006.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; NP_001069617.1; NM_001076149.1.
DR   AlphaFoldDB; O18883; -.
DR   SMR; O18883; -.
DR   STRING; 9913.ENSBTAP00000009353; -.
DR   PaxDb; O18883; -.
DR   PRIDE; O18883; -.
DR   GeneID; 539143; -.
DR   KEGG; bta:539143; -.
DR   CTD; 10190; -.
DR   eggNOG; KOG1672; Eukaryota.
DR   InParanoid; O18883; -.
DR   OrthoDB; 1444223at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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.
DR   PROSITE; PS51352; THIOREDOXIN_2; 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_0000120165"
FT   DOMAIN          52..180
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
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"
FT   CONFLICT        86
FT                   /note="D -> V (in Ref. 2; AAI18431)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   226 AA;  26504 MW;  77B7C56B1EE8B96A CRC64;
     MEANASVDMF SKVLENQLLQ TTKLVEEHLD SEIQKLDQMD EDELERLKEK RLEALKKAQQ
     QKQEWLSKGH GEYREIPSER DFFQEDKESK KVVCHFYRDS TFRCKILDRH LVILSKKHLE
     TKFLKLNVEK APFLCERLRI KVIPTLALVK DGKTQDFVVG FSDLGNTDDF TTETLEWRLG
     CSDILNYSGN LMEPPFQSQK KFGTNFTKLE KKTIRGKKYD SDSDDD
 
 
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