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Protein

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2

Gene

Nmnat2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Divalent metal cations. Mg2+ confers the highest activity.By similarity

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 173ATPBy similarity
Nucleotide bindingi200 – 2023ATPBy similarity
Nucleotide bindingi271 – 2744ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. nicotinamide-nucleotide adenylyltransferase activity Source: UniProtKB-EC
  3. nicotinate-nucleotide adenylyltransferase activity Source: MGI

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_340439. Nicotinate metabolism.
UniPathwayiUPA00253; UER00332.
UPA00253; UER00600.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2Curated (EC:2.7.7.1, EC:2.7.7.18)
Short name:
NMN/NaMN adenylyltransferase 2
Alternative name(s):
Nicotinamide mononucleotide adenylyltransferase 2
Short name:
NMN adenylyltransferase 2
Nicotinate-nucleotide adenylyltransferase 2
Short name:
NaMN adenylyltransferase 2
Gene namesi
Name:Nmnat2
Synonyms:Kiaa0479
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2444155. Nmnat2.

Subcellular locationi

Cytoplasm By similarity. Golgi apparatus By similarity

GO - Cellular componenti

  1. Golgi apparatus Source: MGI
  2. late endosome Source: MGI
  3. synapse Source: MGI
  4. trans-Golgi network Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2PRO_0000135015Add
BLAST

Proteomic databases

PRIDEiQ8BNJ3.

PTM databases

PhosphoSiteiQ8BNJ3.

Expressioni

Gene expression databases

BgeeiQ8BNJ3.
CleanExiMM_NMNAT2.
ExpressionAtlasiQ8BNJ3. baseline and differential.
GenevestigatoriQ8BNJ3.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8BNJ3.
SMRiQ8BNJ3. Positions 9-109, 197-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 573Substrate bindingBy similarity
Regioni92 – 954Substrate bindingBy similarity
Regioni212 – 2132Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1057.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ8BNJ3.
KOiK06210.
OMAiRPPMERF.
OrthoDBiEOG7PVWPQ.
PhylomeDBiQ8BNJ3.
TreeFamiTF315035.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
InterProiIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR12039. PTHR12039. 1 hit.
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BNJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP
60 70 80 90 100
VHDSYGKQGL VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE
110 120 130 140 150
HHRDLMKRVT GCILSNVNTP SMTPVIGQPQ HENTQPIYQN SNVPTKPTAA
160 170 180 190 200
KILGKVGESL SRICCVRPPV ERFTFVDENA NLGTVMRYEE IELRILLLCG
210 220 230 240 250
SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADTDRI MNHSSILRKY
260 270 280 290 300
KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ

LYINASG
Length:307
Mass (Da):34,505
Last modified:February 28, 2003 - v1
Checksum:iB9B4902D3EE03DC6
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129155 mRNA. Translation: BAC97965.1. Frameshift.
AK083532 mRNA. Translation: BAC38943.1.
CCDSiCCDS15368.1.
RefSeqiNP_780669.1. NM_175460.3.
UniGeneiMm.40548.

Genome annotation databases

EnsembliENSMUST00000043313; ENSMUSP00000041110; ENSMUSG00000042751.
GeneIDi226518.
KEGGimmu:226518.
UCSCiuc007czq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129155 mRNA. Translation: BAC97965.1. Frameshift.
AK083532 mRNA. Translation: BAC38943.1.
CCDSiCCDS15368.1.
RefSeqiNP_780669.1. NM_175460.3.
UniGeneiMm.40548.

3D structure databases

ProteinModelPortaliQ8BNJ3.
SMRiQ8BNJ3. Positions 9-109, 197-302.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ8BNJ3.

Proteomic databases

PRIDEiQ8BNJ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043313; ENSMUSP00000041110; ENSMUSG00000042751.
GeneIDi226518.
KEGGimmu:226518.
UCSCiuc007czq.1. mouse.

Organism-specific databases

CTDi23057.
MGIiMGI:2444155. Nmnat2.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG1057.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ8BNJ3.
KOiK06210.
OMAiRPPMERF.
OrthoDBiEOG7PVWPQ.
PhylomeDBiQ8BNJ3.
TreeFamiTF315035.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00332.
UPA00253; UER00600.
ReactomeiREACT_340439. Nicotinate metabolism.

Miscellaneous databases

ChiTaRSiNmnat2. mouse.
NextBioi378196.
PROiQ8BNJ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BNJ3.
CleanExiMM_NMNAT2.
ExpressionAtlasiQ8BNJ3. baseline and differential.
GenevestigatoriQ8BNJ3.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
InterProiIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR12039. PTHR12039. 1 hit.
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(2002) [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.
    , 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiNMNA2_MOUSE
AccessioniPrimary (citable) accession number: Q8BNJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2004
Last sequence update: February 28, 2003
Last modified: March 31, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.