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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.
07-NOV-2018, entry version 126.
RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 {ECO:0000305};
Short=NMN/NaMN adenylyltransferase 2;
EC=2.7.7.1 {ECO:0000250|UniProtKB:Q9BZQ4};
EC=2.7.7.18 {ECO:0000250|UniProtKB:Q9BZQ4};
AltName: Full=Nicotinamide mononucleotide adenylyltransferase 2;
Short=NMN adenylyltransferase 2;
AltName: Full=Nicotinate-nucleotide adenylyltransferase 2;
Short=NaMN adenylyltransferase 2;
AltName: Full=Protein bloated bladder {ECO:0000303|PubMed:23082226};
Short=Blad {ECO:0000303|PubMed:23082226};
Name=Nmnat2 {ECO:0000312|MGI:MGI:2444155};
Synonyms=Kiaa0479 {ECO:0000303|PubMed:14621295};
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).
[3]
FUNCTION, AND PROTEIN DEGRADATION.
PubMed=20126265; DOI=10.1371/journal.pbio.1000300;
Gilley J., Coleman M.P.;
"Endogenous Nmnat2 is an essential survival factor for maintenance of
healthy axons.";
PLoS Biol. 8:E1000300-E1000300(2010).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23082226; DOI=10.1371/journal.pone.0047869;
Hicks A.N., Lorenzetti D., Gilley J., Lu B., Andersson K.E.,
Miligan C., Overbeek P.A., Oppenheim R., Bishop C.E.;
"Nicotinamide mononucleotide adenylyltransferase 2 (Nmnat2) regulates
axon integrity in the mouse embryo.";
PLoS ONE 7:E47869-E47869(2012).
[5]
PROTEIN DEGRADATION.
PubMed=23665224; DOI=10.1016/j.celrep.2013.04.013;
Babetto E., Beirowski B., Russler E.V., Milbrandt J., DiAntonio A.;
"The Phr1 ubiquitin ligase promotes injury-induced axon self-
destruction.";
Cell Rep. 3:1422-1429(2013).
[6]
PROTEIN DEGRADATION, UBIQUITINATION, SUBCELLULAR LOCATION,
PALMITOYLATION AT CYS-164 AND CYS-165, AND MUTAGENESIS OF LYS-151;
LYS-155; ARG-162; 164-CYS-CYS-165; ARG-167 AND ARG-172.
PubMed=23610559; DOI=10.1371/journal.pbio.1001539;
Milde S., Gilley J., Coleman M.P.;
"Subcellular localization determines the stability and axon protective
capacity of axon survival factor Nmnat2.";
PLoS Biol. 11:E1001539-E1001539(2013).
-!- FUNCTION: Nicotinamide/nicotinate-nucleotide adenylyltransferase
that acts as an axon maintenance factor (PubMed:20126265,
PubMed:23082226). Catalyzes the formation of NAD(+) from
nicotinamide mononucleotide (NMN) and ATP (By similarity). Can
also use the deamidated form; nicotinic acid mononucleotide (NaMN)
as substrate but with a lower efficiency (By similarity). Cannot
use triazofurin monophosphate (TrMP) as substrate (By similarity).
Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic
cleavage of NAD(+) (By similarity). For the pyrophosphorolytic
activity prefers NAD(+), NADH and NaAD as substrates and degrades
nicotinic acid adenine dinucleotide phosphate (NHD) less
effectively (By similarity). Fails to cleave phosphorylated
dinucleotides NADP(+), NADPH and NaADP(+) (By similarity). Axon
survival factor required for the maintenance of healthy axons:
acts by delaying Wallerian axon degeneration, an evolutionarily
conserved process that drives the loss of damaged axons
(PubMed:20126265, PubMed:23082226). {ECO:0000250|UniProtKB:Q9BZQ4,
ECO:0000269|PubMed:20126265, ECO:0000269|PubMed:23082226}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+). {ECO:0000250|UniProtKB:Q9BZQ4}.
-!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide =
diphosphate + deamido-NAD(+). {ECO:0000250|UniProtKB:Q9BZQ4}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9BZQ4};
Note=Divalent metal cations. Mg(2+) confers the highest activity.
{ECO:0000250|UniProtKB:Q9BZQ4};
-!- ACTIVITY REGULATION: Inhibited by P1-(adenosine-5')-P3-
(nicotinamide-riboside-5')-triphosphate (Np3AD) and P1-(adenosine-
5')-P4-(nicotinamide-riboside-5')-tetraphosphate (Np4AD).
{ECO:0000250|UniProtKB:Q9BZQ4}.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
nicotinamide D-ribonucleotide: step 1/1.
{ECO:0000250|UniProtKB:Q9BZQ4}.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-
NAD(+) from nicotinate D-ribonucleotide: step 1/1.
{ECO:0000250|UniProtKB:Q9BZQ4}.
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9BZQ4}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:23610559}; Lipid-anchor
{ECO:0000269|PubMed:23610559}. Cytoplasmic vesicle membrane;
Lipid-anchor {ECO:0000269|PubMed:23610559}. Cytoplasm
{ECO:0000250|UniProtKB:Q9BZQ4}. Cell projection, axon
{ECO:0000269|PubMed:23610559}. Note=Delivered to axons with Golgi-
derived cytoplasmic vesicles. {ECO:0000269|PubMed:23610559}.
-!- TISSUE SPECIFICITY: Expressed predominantly in the brain and
nervous system. {ECO:0000269|PubMed:23082226}.
-!- PTM: Degraded in response to injured neurite (PubMed:20126265,
PubMed:23665224, PubMed:23610559). Degradation is probably caused
by ubiquitination by MYCBP2 (PubMed:23665224, PubMed:23610559).
Ubiquitinated on threonine and/or serine residues by MYCBP2;
consequences of threonine and/or serine ubiquitination are however
unclear (By similarity). {ECO:0000250|UniProtKB:Q9BZQ4,
ECO:0000269|PubMed:20126265, ECO:0000269|PubMed:23610559,
ECO:0000269|PubMed:23665224}.
-!- PTM: Palmitoylated; palmitoylation is required for membrane
association. {ECO:0000269|PubMed:23610559}.
-!- DISRUPTION PHENOTYPE: Perinatal lethality. Mice show a greatly
distended bladder, underdeveloped diaphragm and a reduction in
total skeletal muscle mass. Defects are caused by defects in
innervation of major organs and tissues.
{ECO:0000269|PubMed:23082226}.
-!- 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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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
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; Expressed in 199 organ(s), highest expression level in cerebellum.
CleanEx; MM_NMNAT2; -.
ExpressionAtlas; Q8BNJ3; baseline and differential.
Genevisible; Q8BNJ3; MM.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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.
GO; GO:0009435; P:NAD biosynthetic process; ISO:MGI.
InterPro; IPR004821; Cyt_trans-like.
Pfam; PF01467; CTP_transf_like; 1.
1: Evidence at protein level;
ATP-binding; Cell projection; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Golgi apparatus; Lipoprotein; Membrane; NAD;
Nucleotide-binding; Nucleotidyltransferase; Palmitate;
Pyridine nucleotide biosynthesis; Reference proteome; Transferase;
Ubl conjugation.
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}.
LIPID 164 164 S-palmitoyl cysteine.
{ECO:0000269|PubMed:23610559}.
LIPID 165 165 S-palmitoyl cysteine.
{ECO:0000269|PubMed:23610559}.
MUTAGEN 151 151 K->A: Impaired membrane association in
neurons; when associated with A-155; A-
162; A-167 and A-172.
MUTAGEN 155 155 K->A: Impaired membrane association in
neurons; when associated with A-151; A-
162; A-167 and A-172.
MUTAGEN 162 162 R->A: Impaired membrane association in
neurons; when associated with A-151; A-
155; A-167 and A-172.
MUTAGEN 164 165 CC->SS: Abolished palmitoylation and
membrane association in neurons.
{ECO:0000269|PubMed:23610559}.
MUTAGEN 167 167 R->A: Impaired membrane association in
neurons; when associated with A-151; A-
155; A-162 and A-172.
MUTAGEN 172 172 R->A: Impaired membrane association in
neurons; when associated with A-151; A-
155; A-162 and A-167.
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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