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