位置:首页 > 蛋白库 > DTWD2_MOUSE
DTWD2_MOUSE
ID   DTWD2_MOUSE             Reviewed;         298 AA.
AC   Q9D0U1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=tRNA-uridine aminocarboxypropyltransferase 2 {ECO:0000305};
DE            EC=2.5.1.25 {ECO:0000250|UniProtKB:Q8NBA8};
DE   AltName: Full=DTW domain-containing protein 2;
GN   Name=Dtwd2 {ECO:0000312|MGI:MGI:1916107};
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; TISSUE=Embryo, and Lung;
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).
CC   -!- FUNCTION: Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine
CC       (acp3U) at position 20a in the D-loop of several cytoplasmic tRNAs
CC       (acp3U(20a)). Also has a weak activity to form acp3U at position 20 in
CC       the D-loop of tRNAs (acp3U(20)). {ECO:0000250|UniProtKB:Q8NBA8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a uridine in tRNA + S-adenosyl-L-methionine = a 3-[(3S)-3-
CC         amino-3-carboxypropyl]uridine in tRNA + H(+) + S-methyl-5'-
CC         thioadenosine; Xref=Rhea:RHEA:62432, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC         COMP:16092, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:82930; EC=2.5.1.25;
CC         Evidence={ECO:0000250|UniProtKB:Q8NBA8};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NBA8}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8NBA8}.
CC   -!- DOMAIN: Contains 1 DXTW motif.
CC   -!- SIMILARITY: Belongs to the TDD superfamily. DTWD2 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK004450; BAB23309.1; -; mRNA.
DR   EMBL; AK144689; BAE26015.1; -; mRNA.
DR   CCDS; CCDS37815.1; -.
DR   RefSeq; NP_001164431.1; NM_001170960.1.
DR   RefSeq; NP_081130.1; NM_026854.3.
DR   AlphaFoldDB; Q9D0U1; -.
DR   STRING; 10090.ENSMUSP00000025383; -.
DR   PhosphoSitePlus; Q9D0U1; -.
DR   PaxDb; Q9D0U1; -.
DR   PRIDE; Q9D0U1; -.
DR   Antibodypedia; 52885; 66 antibodies from 14 providers.
DR   Ensembl; ENSMUST00000163590; ENSMUSP00000128219; ENSMUSG00000024505.
DR   GeneID; 68857; -.
DR   KEGG; mmu:68857; -.
DR   UCSC; uc008ewl.2; mouse.
DR   CTD; 285605; -.
DR   MGI; MGI:1916107; Dtwd2.
DR   VEuPathDB; HostDB:ENSMUSG00000024505; -.
DR   eggNOG; KOG4382; Eukaryota.
DR   GeneTree; ENSGT00390000006867; -.
DR   HOGENOM; CLU_066458_3_0_1; -.
DR   InParanoid; Q9D0U1; -.
DR   OMA; HTLCKYQ; -.
DR   OrthoDB; 910985at2759; -.
DR   PhylomeDB; Q9D0U1; -.
DR   TreeFam; TF324734; -.
DR   BioGRID-ORCS; 68857; 2 hits in 72 CRISPR screens.
DR   PRO; PR:Q9D0U1; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q9D0U1; protein.
DR   Bgee; ENSMUSG00000024505; Expressed in ectoplacental cone and 181 other tissues.
DR   ExpressionAtlas; Q9D0U1; baseline and differential.
DR   Genevisible; Q9D0U1; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0016432; F:tRNA-uridine aminocarboxypropyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR   InterPro; IPR005636; DTW.
DR   InterPro; IPR039262; DTWD2/YfiP.
DR   PANTHER; PTHR21392; PTHR21392; 1.
DR   Pfam; PF03942; DTW; 1.
DR   SMART; SM01144; DTW; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..298
FT                   /note="tRNA-uridine aminocarboxypropyltransferase 2"
FT                   /id="PRO_0000271130"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           178..181
FT                   /note="DXTW"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBA8"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBA8"
SQ   SEQUENCE   298 AA;  33102 MW;  191BED0F20041329 CRC64;
     MEPQAEERTL GEPAPPPSGA LASPTPDEEE RTEGGAPPTA TPAGASGDST SADGLWGLPV
     EHAERRPECG RCSRPQKVCL CPYLPVRPLQ ISTHLYIIQH PAEESRVLRT VPLLAACLPP
     DRCTVKIGRR FSEERDVELA TVCRDSGTLI LYPGAEATNL EEFILDSPVY PSTIILIDGT
     WSQAKDIFYK NSLFRLPKQV QLKTSVCSQY VIRMQPTNRC LSTLECAAVA LSILEKNNCI
     QETLLRPLQA LCSFQLQHGA QIRLSKEYLL RNGLYPKPMP KNKRKLRKME LLMNSVKI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024