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Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMN/NaMN adenylyltransferase 2) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide mononucleotide adenylyltransferase 2) (NMN adenylyltransferase 2) (Nicotinate-nucleotide adenylyltransferase 2) (NaMN adenylyltransferase 2)

 NMNA2_MOUSE             Reviewed;         307 AA.
Q8BNJ3;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
28-FEB-2018, entry version 122.
RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 {ECO:0000305};
Short=NMN/NaMN adenylyltransferase 2;
EC=2.7.7.1;
EC=2.7.7.18;
AltName: Full=Nicotinamide mononucleotide adenylyltransferase 2;
Short=NMN adenylyltransferase 2;
AltName: Full=Nicotinate-nucleotide adenylyltransferase 2;
Short=NaMN adenylyltransferase 2;
Name=Nmnat2; Synonyms=Kiaa0479;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
-!- FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide
mononucleotide (NMN) and ATP. Can also use the deamidated form;
nicotinic acid mononucleotide (NaMN) as substrate but with a lower
efficiency. Cannot use triazofurin monophosphate (TrMP) as
substrate. Also catalyzes the reverse reaction, i.e. the
pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic
activity prefers NAD(+), NADH and NaAD as substrates and degrades
nicotinic acid adenine dinucleotide phosphate (NHD) less
effectively. Fails to cleave phosphorylated dinucleotides NADP(+),
NADPH and NaADP(+) (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+).
-!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide =
diphosphate + deamido-NAD(+).
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Divalent metal cations. Mg(2+) confers the highest activity.
{ECO:0000250};
-!- ENZYME REGULATION: Inhibited by P1-(adenosine-5')-P3-
(nicotinamide-riboside-5')-triphosphate (Np3AD) and P1-(adenosine-
5')-P4-(nicotinamide-riboside-5')-tetraphosphate (Np4AD).
{ECO:0000250}.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
nicotinamide D-ribonucleotide: step 1/1.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-
NAD(+) from nicotinate D-ribonucleotide: step 1/1.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
{ECO:0000250}.
-!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC97965.1; Type=Frameshift; Positions=252; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AK129155; BAC97965.1; ALT_FRAME; mRNA.
EMBL; AK083532; BAC38943.1; -; mRNA.
CCDS; CCDS15368.1; -.
RefSeq; NP_780669.1; NM_175460.3.
UniGene; Mm.40548; -.
ProteinModelPortal; Q8BNJ3; -.
STRING; 10090.ENSMUSP00000041110; -.
iPTMnet; Q8BNJ3; -.
PhosphoSitePlus; Q8BNJ3; -.
SwissPalm; Q8BNJ3; -.
PaxDb; Q8BNJ3; -.
PRIDE; Q8BNJ3; -.
Ensembl; ENSMUST00000043313; ENSMUSP00000041110; ENSMUSG00000042751.
GeneID; 226518; -.
KEGG; mmu:226518; -.
UCSC; uc007czq.1; mouse.
CTD; 23057; -.
MGI; MGI:2444155; Nmnat2.
eggNOG; KOG3199; Eukaryota.
eggNOG; COG1057; LUCA.
GeneTree; ENSGT00530000063189; -.
HOGENOM; HOG000216047; -.
HOVERGEN; HBG052640; -.
InParanoid; Q8BNJ3; -.
KO; K06210; -.
OMA; YILQSQL; -.
OrthoDB; EOG091G0JTI; -.
PhylomeDB; Q8BNJ3; -.
TreeFam; TF315035; -.
Reactome; R-MMU-196807; Nicotinate metabolism.
UniPathway; UPA00253; UER00332.
UniPathway; UPA00253; UER00600.
ChiTaRS; Nmnat2; mouse.
PRO; PR:Q8BNJ3; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000042751; -.
CleanEx; MM_NMNAT2; -.
ExpressionAtlas; Q8BNJ3; baseline and differential.
Genevisible; Q8BNJ3; MM.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0005770; C:late endosome; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IBA:GO_Central.
GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; ISO:MGI.
GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
InterPro; IPR004821; Cyt_trans-like.
Pfam; PF01467; CTP_transf_like; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Cytoplasm; Golgi apparatus; NAD;
Nucleotide-binding; Nucleotidyltransferase;
Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
CHAIN 1 307 Nicotinamide/nicotinic acid
mononucleotide adenylyltransferase 2.
/FTId=PRO_0000135015.
NP_BIND 15 17 ATP. {ECO:0000250|UniProtKB:Q96T66}.
NP_BIND 200 202 ATP. {ECO:0000250|UniProtKB:Q96T66}.
NP_BIND 271 274 ATP. {ECO:0000250|UniProtKB:Q96T66}.
REGION 55 57 Substrate binding.
{ECO:0000250|UniProtKB:Q96T66}.
REGION 92 95 Substrate binding.
{ECO:0000250|UniProtKB:Q96T66}.
REGION 212 213 Substrate binding.
{ECO:0000250|UniProtKB:Q96T66}.
BINDING 24 24 ATP. {ECO:0000250|UniProtKB:Q96T66}.
SEQUENCE 307 AA; 34505 MW; B9B4902D3EE03DC6 CRC64;
MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP VHDSYGKQGL
VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP
SMTPVIGQPQ HENTQPIYQN SNVPTKPTAA KILGKVGESL SRICCVRPPV ERFTFVDENA
NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADTDRI
MNHSSILRKY KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ
LYINASG


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