TXND9_MOUSE
ID TXND9_MOUSE Reviewed; 226 AA.
AC Q9CQ79; Q3TKD2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Thioredoxin domain-containing protein 9;
DE AltName: Full=ATP-binding protein associated with cell differentiation;
GN Name=Txndc9; Synonyms=Apacd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Embryonic stem cell, Kidney, Skin, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15009089; DOI=10.1111/j.1356-9597.2004.00708.x;
RA Ogawa S., Matsubayashi Y., Nishida E.;
RT "An evolutionarily conserved gene required for proper microtubule
RT architecture in Caenorhabditis elegans.";
RL Genes Cells 9:83-93(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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|UniProtKB:O14530}.
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:0000269|PubMed:15009089}. Nucleus
CC {ECO:0000269|PubMed:15009089}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:15009089}. Midbody
CC {ECO:0000269|PubMed:15009089}. Note=Co-localizes with beta-tubulin in
CC the centrosome. {ECO:0000269|PubMed:15009089}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, liver, heart, kidney, brain,
CC spleen and lung. {ECO:0000269|PubMed:15009089}.
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DR EMBL; AK002893; BAB22438.1; -; mRNA.
DR EMBL; AK006170; BAB24440.1; -; mRNA.
DR EMBL; AK010709; BAB27134.1; -; mRNA.
DR EMBL; AK011424; BAB27611.1; -; mRNA.
DR EMBL; AK016756; BAB30412.1; -; mRNA.
DR EMBL; AK028525; BAC25991.1; -; mRNA.
DR EMBL; AK153857; BAE32213.1; -; mRNA.
DR EMBL; AK167045; BAE39213.1; -; mRNA.
DR EMBL; BC022947; AAH22947.1; -; mRNA.
DR EMBL; BC083077; AAH83077.1; -; mRNA.
DR CCDS; CCDS14898.1; -.
DR RefSeq; NP_742051.1; NM_172054.4.
DR RefSeq; XP_006496420.1; XM_006496357.3.
DR RefSeq; XP_006496421.1; XM_006496358.3.
DR AlphaFoldDB; Q9CQ79; -.
DR SMR; Q9CQ79; -.
DR BioGRID; 221025; 3.
DR STRING; 10090.ENSMUSP00000125491; -.
DR iPTMnet; Q9CQ79; -.
DR PhosphoSitePlus; Q9CQ79; -.
DR EPD; Q9CQ79; -.
DR MaxQB; Q9CQ79; -.
DR PaxDb; Q9CQ79; -.
DR PeptideAtlas; Q9CQ79; -.
DR PRIDE; Q9CQ79; -.
DR ProteomicsDB; 298343; -.
DR Antibodypedia; 32814; 144 antibodies from 27 providers.
DR DNASU; 98258; -.
DR Ensembl; ENSMUST00000162031; ENSMUSP00000125491; ENSMUSG00000058407.
DR Ensembl; ENSMUST00000195032; ENSMUSP00000141595; ENSMUSG00000058407.
DR Ensembl; ENSMUST00000195247; ENSMUSP00000141609; ENSMUSG00000058407.
DR GeneID; 98258; -.
DR KEGG; mmu:98258; -.
DR UCSC; uc007asm.1; mouse.
DR CTD; 10190; -.
DR MGI; MGI:2138153; Txndc9.
DR VEuPathDB; HostDB:ENSMUSG00000058407; -.
DR eggNOG; KOG1672; Eukaryota.
DR GeneTree; ENSGT00390000015645; -.
DR InParanoid; Q9CQ79; -.
DR OMA; QVLPCVI; -.
DR OrthoDB; 1444223at2759; -.
DR PhylomeDB; Q9CQ79; -.
DR TreeFam; TF313442; -.
DR BioGRID-ORCS; 98258; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Txndc9; mouse.
DR PRO; PR:Q9CQ79; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CQ79; protein.
DR Bgee; ENSMUSG00000058407; Expressed in morula and 149 other tissues.
DR ExpressionAtlas; Q9CQ79; baseline and differential.
DR Genevisible; Q9CQ79; MM.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030496; C:midbody; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..226
FT /note="Thioredoxin domain-containing protein 9"
FT /id="PRO_0000120167"
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; 26260 MW; B90255DDAEE402BC CRC64;
MEGNGSVDMF SEVLENQFLQ AAKLVENHLD SEIQKLDQIG EDELELLKEK RLAALRKAQQ
QKQEWLSKGH GEYREIGSER DFFQEVKESE KVVCHFYRDT TFRCKILDRH LAILAKKHLE
TKFLKLNVEK APFLCERLRI KVIPTLALLR DGKTQDYVVG FTDLGNTDDF TTETLEWRLG
CSDVINYSGN LMEPPFQSQK KFGTNFTKLE KKTIRGKKYD SDSDDD
