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Q8BNJ3 (NMNA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nicotinamide mononucleotide adenylyltransferase 2
Short name=NMN adenylyltransferase 2
EC=2.7.7.1
Alternative name(s):
Nicotinate-nucleotide adenylyltransferase 1
Short name=NaMN adenylyltransferase 1
EC=2.7.7.18
Gene names
Name:Nmnat2
Synonyms:Kiaa0479
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Catalytic activity

ATP + nicotinamide ribonucleotide = diphosphate + NAD+.

ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD+.

Cofactor

Divalent metal cations. Magnesium confers the highest activity By similarity.

Enzyme regulation

Inhibited by P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate (Np3AD) and P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate (Np4AD) By similarity.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity. Golgi apparatus By similarity.

Sequence similarities

Belongs to the eukaryotic NMN adenylyltransferase family.

Sequence caution

The sequence BAC97965.1 differs from that shown. Reason: Frameshift at position 252.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 307307Nicotinamide mononucleotide adenylyltransferase 2
PRO_0000135015

Regions

Nucleotide binding15 – 2410ATP Potential
Nucleotide binding269 – 2746ATP Potential

Sites

Binding site161Substrate By similarity
Binding site551Substrate By similarity
Binding site2021Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BNJ3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: B9B4902D3EE03DC6

FASTA30734,505
        10         20         30         40         50         60 
MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP VHDSYGKQGL 

        70         80         90        100        110        120 
VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP 

       130        140        150        160        170        180 
SMTPVIGQPQ HENTQPIYQN SNVPTKPTAA KILGKVGESL SRICCVRPPV ERFTFVDENA 

       190        200        210        220        230        240 
NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADTDRI 

       250        260        270        280        290        300 
MNHSSILRKY KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ 


LYINASG

« Hide

References

[1]"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."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK129155 mRNA. Translation: BAC97965.1. Frameshift.
AK083532 mRNA. Translation: BAC38943.1.
IPIIPI00309131.
RefSeqNP_780669.1. NM_175460.3.
UniGeneMm.40548.

3D structure databases

ProteinModelPortalQ8BNJ3.
SMRQ8BNJ3. Positions 9-109, 197-302.
ModBaseSearch...

PTM databases

PhosphoSiteQ8BNJ3.

Proteomic databases

PRIDEQ8BNJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043313; ENSMUSP00000041110; ENSMUSG00000042751.
GeneID226518.
KEGGmmu:226518.

Organism-specific databases

CTD23057.
MGIMGI:2444155. Nmnat2.
RougeSearch...

Phylogenomic databases

eggNOGCOG1057.
GeneTreeENSGT00530000063189.
HOGENOMHOG000216047.
HOVERGENHBG052640.
InParanoidQ8BNJ3.
KOK06210.
OMAPMERFTF.
OrthoDBEOG4N30PB.

Enzyme and pathway databases

UniPathwayUPA00253; UER00600.

Gene expression databases

ArrayExpressQ8BNJ3.
BgeeQ8BNJ3.
CleanExMM_NMNAT2.
GenevestigatorQ8BNJ3.
GermOnlineENSMUSG00000042751. Mus musculus.

Family and domain databases

Gene3D3.40.50.620. 2 hits.
InterProIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR12039. PTHR12039. 1 hit.
PfamPF01467. CTP_transf_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio378196.
SOURCESearch...

Entry information

Entry nameNMNA2_MOUSE
AccessionPrimary (citable) accession number: Q8BNJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 1, 2003
Last modified: May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents