NUD17_MOUSE
ID NUD17_MOUSE Reviewed; 296 AA.
AC Q9CWD3; Q14BX3; Q3URR9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Nucleoside diphosphate-linked moiety X motif 17;
DE Short=Nudix motif 17;
DE EC=3.6.1.-;
GN Name=Nudt17;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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] (ISOFORM 2).
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).
CC -!- FUNCTION: Probably mediates the hydrolysis of some nucleoside
CC diphosphate derivatives. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CWD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CWD3-2; Sequence=VSP_037799;
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AK019109; BAB31551.1; -; mRNA.
DR EMBL; AK134929; BAE22341.1; -; mRNA.
DR EMBL; AK141256; BAE24619.1; -; mRNA.
DR EMBL; BC115559; AAI15560.1; -; mRNA.
DR CCDS; CCDS51008.1; -. [Q9CWD3-1]
DR CCDS; CCDS51009.1; -. [Q9CWD3-2]
DR RefSeq; NP_001156397.1; NM_001162925.1. [Q9CWD3-2]
DR RefSeq; NP_084370.1; NM_030094.1. [Q9CWD3-1]
DR AlphaFoldDB; Q9CWD3; -.
DR SMR; Q9CWD3; -.
DR STRING; 10090.ENSMUSP00000029742; -.
DR PhosphoSitePlus; Q9CWD3; -.
DR EPD; Q9CWD3; -.
DR MaxQB; Q9CWD3; -.
DR PRIDE; Q9CWD3; -.
DR ProteomicsDB; 295460; -. [Q9CWD3-1]
DR ProteomicsDB; 295461; -. [Q9CWD3-2]
DR Antibodypedia; 33964; 43 antibodies from 15 providers.
DR Ensembl; ENSMUST00000029742; ENSMUSP00000029742; ENSMUSG00000028100. [Q9CWD3-2]
DR Ensembl; ENSMUST00000171249; ENSMUSP00000129851; ENSMUSG00000028100. [Q9CWD3-1]
DR GeneID; 78373; -.
DR KEGG; mmu:78373; -.
DR UCSC; uc008qny.2; mouse. [Q9CWD3-2]
DR UCSC; uc008qnz.2; mouse. [Q9CWD3-1]
DR CTD; 200035; -.
DR MGI; MGI:1925623; Nudt17.
DR VEuPathDB; HostDB:ENSMUSG00000028100; -.
DR eggNOG; ENOG502QWT5; Eukaryota.
DR GeneTree; ENSGT00390000013847; -.
DR HOGENOM; CLU_061877_1_0_1; -.
DR InParanoid; Q9CWD3; -.
DR OMA; VSALMWL; -.
DR OrthoDB; 1602447at2759; -.
DR PhylomeDB; Q9CWD3; -.
DR TreeFam; TF313611; -.
DR BioGRID-ORCS; 78373; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Nudt17; mouse.
DR PRO; PR:Q9CWD3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CWD3; protein.
DR Bgee; ENSMUSG00000028100; Expressed in lip and 102 other tissues.
DR ExpressionAtlas; Q9CWD3; baseline and differential.
DR Genevisible; Q9CWD3; MM.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IBA:GO_Central.
DR GO; GO:0019677; P:NAD catabolic process; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR GO; GO:0006742; P:NADP catabolic process; IBA:GO_Central.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..296
FT /note="Nucleoside diphosphate-linked moiety X motif 17"
FT /id="PRO_0000019954"
FT DOMAIN 90..236
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 127..148
FT /note="Nudix box"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 125..134
FT /note="PGGHMEPDEE -> PDFLCPLENGVPGGRQQPFTLGPLLLQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037799"
SQ SEQUENCE 296 AA; 32681 MW; 09439EAD2F1CFBB3 CRC64;
MAAARLLLRL AGRLESVSFT QSVCGLLGAG QRPGPWHTHC SLERGQLVLS SNPFPGASER
LPIQRPLFCP FAALDQQPEV SKTEPLTNRG VDLGVAVILQ SSDQTVLLTR RTCTLRISPN
LWVPPGGHME PDEEILECGF RELWEECGLQ LPKNQFSCVL LGLWESAYPP RLSWGFPKYH
HLILYVLVIS QESQEQLQAR IQVNPNEVNA FMWLGPDVAA AVVATEDGTR TPGLFSQDLP
LSVCATELKD DGGTQPLVLP MPTLMRTTPT TAEEDKERIG AGTKFALQLW LQHLGR
