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Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMN/NaMN adenylyltransferase 1) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide-nucleotide adenylyltransferase 1) (NMN adenylyltransferase 1) (Nicotinate-nucleotide adenylyltransferase 1) (NaMN adenylyltransferase 1)

 NMNA1_HUMAN             Reviewed;         279 AA.
Q9HAN9; B1AN63; Q8TAE9; Q9H247; Q9H6B6;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
28-MAR-2018, entry version 154.
RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 {ECO:0000305};
Short=NMN/NaMN adenylyltransferase 1;
EC=2.7.7.1;
EC=2.7.7.18;
AltName: Full=Nicotinamide-nucleotide adenylyltransferase 1;
Short=NMN adenylyltransferase 1;
AltName: Full=Nicotinate-nucleotide adenylyltransferase 1;
Short=NaMN adenylyltransferase 1;
Name=NMNAT1; Synonyms=NMNAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAG33632.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 208-225 AND 262-272,
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH ADPRT.
PubMed=11248244; DOI=10.1016/S0014-5793(01)02180-9;
Schweiger M., Hennig K., Lerner F., Niere M., Hirsch-Kauffmann M.,
Specht T., Weise C., Oei S.L., Ziegler M.;
"Characterization of recombinant human nicotinamide mononucleotide
adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD
synthesis.";
FEBS Lett. 492:95-100(2001).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 238-250 AND 262-272,
COFACTOR, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=11027696; DOI=10.1074/jbc.M008700200;
Emanuelli M., Carnevali F., Saccucci F., Pierella F., Amici A.,
Raffaelli N., Magni G.;
"Molecular cloning, chromosomal localization, tissue mRNA levels,
bacterial expression, and enzymatic properties of human NMN
adenylyltransferase.";
J. Biol. Chem. 276:406-412(2001).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
PubMed=11891043; DOI=10.1016/S0378-1119(02)00394-3;
Fernando F.S., Conforti L., Tosi S., Smith A.D., Coleman M.P.;
"Human homologue of a gene mutated in the slow Wallerian degeneration
(C57BL/Wld(s)) mouse.";
Gene 284:23-29(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6] {ECO:0000312|EMBL:BAB15345.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
SUBCELLULAR LOCATION.
PubMed=12574164; DOI=10.1074/jbc.M300073200;
Zhang X., Kurnasov O.V., Karthikeyan S., Grishin N.V., Osterman A.L.,
Zhang H.;
"Structural characterization of a human cytosolic NMN/NaMN
adenylyltransferase and implication in human NAD biosynthesis.";
J. Biol. Chem. 278:13503-13511(2003).
[9]
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
PubMed=16118205; DOI=10.1074/jbc.M508660200;
Berger F., Lau C., Dahlmann M., Ziegler M.;
"Subcellular compartmentation and differential catalytic properties of
the three human nicotinamide mononucleotide adenylyltransferase
isoforms.";
J. Biol. Chem. 280:36334-36341(2005).
[10]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND
COFACTOR.
PubMed=17402747; DOI=10.1021/bi6023379;
Sorci L., Cimadamore F., Scotti S., Petrelli R., Cappellacci L.,
Franchetti P., Orsomando G., Magni G.;
"Initial-rate kinetics of human NMN-adenylyltransferases: substrate
and metal ion specificity, inhibition by products and multisubstrate
analogues, and isozyme contributions to NAD+ biosynthesis.";
Biochemistry 46:4912-4922(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
SUBCELLULAR LOCATION, VARIANTS LCA9 THR-13; PHE-67; GLY-98; PHE-151;
TRP-207; LEU-237; LYS-257 AND ASP-273, AND CHARACTERIZATION OF
VARIANTS LCA9 TRP-207; LYS-257 AND ASP-273.
PubMed=22842230; DOI=10.1038/ng.2356;
Koenekoop R.K., Wang H., Majewski J., Wang X., Lopez I., Ren H.,
Chen Y., Li Y., Fishman G.A., Genead M., Schwartzentruber J.,
Solanki N., Traboulsi E.I., Cheng J., Logan C.V., McKibbin M.,
Hayward B.E., Parry D.A., Johnson C.A., Nageeb M., Poulter J.A.,
Mohamed M.D., Jafri H., Rashid Y., Taylor G.R., Keser V., Mardon G.,
Xu H., Inglehearn C.F., Fu Q., Toomes C., Chen R.;
"Mutations in NMNAT1 cause Leber congenital amaurosis and identify a
new disease pathway for retinal degeneration.";
Nat. Genet. 44:1035-1039(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND THR-119, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
FUNCTION.
PubMed=27257257; DOI=10.1126/science.aad9335;
Wright R.H., Lioutas A., Le Dily F., Soronellas D., Pohl A., Bonet J.,
Nacht A.S., Samino S., Font-Mateu J., Vicent G.P., Wierer M.,
Trabado M.A., Schelhorn C., Carolis C., Macias M.J., Yanes O.,
Oliva B., Beato M.;
"ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for
chromatin remodeling.";
Science 352:1221-1225(2016).
[16]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 5-278 IN COMPLEX WITH
SUBSTRATE NMN.
PubMed=11959140; DOI=10.1016/S0014-5793(02)02556-5;
Werner E., Ziegler M., Lerner F., Schweiger M., Heinemann U.;
"Crystal structure of human nicotinamide mononucleotide
adenylyltransferase in complex with NMN.";
FEBS Lett. 516:239-244(2002).
[17]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=11751893; DOI=10.1074/jbc.M111589200;
Garavaglia S., D'Angelo I., Emanuelli M., Carnevali F., Pierella F.,
Magni G., Rizzi M.;
"Structure of human NMN adenylyltransferase. A key nuclear enzyme for
NAD homeostasis.";
J. Biol. Chem. 277:8524-8530(2002).
[18]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PRODUCTS NAD AND
NAAD.
PubMed=11788603; DOI=10.1074/jbc.M111469200;
Zhou T., Kurnasov O., Tomchick D.R., Binns D.D., Grishin N.V.,
Marquez V.E., Osterman A.L., Zhang H.;
"Structure of human nicotinamide/nicotinic acid mononucleotide
adenylyltransferase. Basis for the dual substrate specificity and
activation of the oncolytic agent tiazofurin.";
J. Biol. Chem. 277:13148-13154(2002).
[19]
VARIANTS LCA9 THR-35; GLY-98; PHE-151; VAL-153; LYS-257 AND ASP-273.
PubMed=22842231; DOI=10.1038/ng.2370;
Chiang P.W., Wang J., Chen Y., Fu Q., Zhong J., Chen Y., Yi X., Wu R.,
Gan H., Shi Y., Chen Y., Barnett C., Wheaton D., Day M.,
Sutherland J., Heon E., Weleber R.G., Gabriel L.A., Cong P.,
Chuang K., Ye S., Sallum J.M., Qi M.;
"Exome sequencing identifies NMNAT1 mutations as a cause of Leber
congenital amaurosis.";
Nat. Genet. 44:972-974(2012).
[20]
VARIANTS LCA9 THR-13; VAL-69; PRO-147; PRO-153; GLY-173; MET-178;
CYS-181; TRP-207; ASN-217; CYS-237; SER-239 AND PRO-251.
PubMed=22842229; DOI=10.1038/ng.2357;
Perrault I., Hanein S., Zanlonghi X., Serre V., Nicouleau M.,
Defoort-Delhemmes S., Delphin N., Fares-Taie L., Gerber S., Xerri O.,
Edelson C., Goldenberg A., Duncombe A., Le Meur G., Hamel C.,
Silva E., Nitschke P., Calvas P., Munnich A., Roche O., Dollfus H.,
Kaplan J., Rozet J.M.;
"Mutations in NMNAT1 cause Leber congenital amaurosis with early-onset
severe macular and optic atrophy.";
Nat. Genet. 44:975-977(2012).
[21]
VARIANTS LCA9 MET-9; THR-13; ASN-20; GLY-33; VAL-54; TRP-66; VAL-69;
HIS-72; GLY-98; ARG-156; MET-184; CYS-237 AND LYS-257, AND
CHARACTERIZATION OF VARIANTS LCA9 MET-9; TRP-66 AND CYS-237.
PubMed=22842227; DOI=10.1038/ng.2361;
Falk M.J., Zhang Q., Nakamaru-Ogiso E., Kannabiran C.,
Fonseca-Kelly Z., Chakarova C., Audo I., Mackay D.S., Zeitz C.,
Borman A.D., Staniszewska M., Shukla R., Palavalli L., Mohand-Said S.,
Waseem N.H., Jalali S., Perin J.C., Place E., Ostrovsky J., Xiao R.,
Bhattacharya S.S., Consugar M., Webster A.R., Sahel J.A., Moore A.T.,
Berson E.L., Liu Q., Gai X., Pierce E.A.;
"NMNAT1 mutations cause Leber congenital amaurosis.";
Nat. Genet. 44:1040-1045(2012).
-!- FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide
mononucleotide (NMN) and ATP (PubMed:17402747). Can also use the
deamidated form; nicotinic acid mononucleotide (NaMN) as substrate
with the same efficiency (PubMed:17402747). Can use triazofurin
monophosphate (TrMP) as substrate (PubMed:17402747). Also
catalyzes the reverse reaction, i.e. the pyrophosphorolytic
cleavage of NAD(+) (PubMed:17402747). For the pyrophosphorolytic
activity, prefers NAD(+) and NaAD as substrates and degrades NADH,
nicotinic acid adenine dinucleotide phosphate (NHD) and
nicotinamide guanine dinucleotide (NGD) less effectively
(PubMed:17402747). Involved in the synthesis of ATP in the
nucleus, together with PARP1, PARG and NUDT5 (PubMed:27257257).
Nuclear ATP generation is required for extensive chromatin
remodeling events that are energy-consuming (PubMed:27257257).
Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and
NaADP(+) (PubMed:17402747). Protects against axonal degeneration
following mechanical or toxic insults (By similarity).
{ECO:0000250|UniProtKB:Q9EPA7, ECO:0000269|PubMed:17402747,
ECO:0000269|PubMed:27257257}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+). {ECO:0000269|PubMed:11027696}.
-!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide =
diphosphate + deamido-NAD(+).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:11027696,
ECO:0000269|PubMed:17402747};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11027696,
ECO:0000269|PubMed:17402747};
Note=Divalent metal cations. Zn(2+) confers higher activity as
compared to Mg(2+). {ECO:0000269|PubMed:11027696,
ECO:0000269|PubMed:17402747};
-!- ENZYME REGULATION: Activity is strongly inhibited by galotannin.
Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-
tetraphosphate (Nap4AD). {ECO:0000269|PubMed:17402747}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=34 uM for NMN {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
KM=40 uM for ATP {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
KM=937 uM for PPi {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
KM=59 uM for NAD(+) {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
Vmax=25 umol/min/mg enzyme for NAD synthesis
{ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
Vmax=60.5 umol/min/ug enzyme for NAD(+) cleavage
{ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
Vmax=8.5 umol/min/ug enzyme for NADH cleavage
{ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
-!- 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: Homohexamer. Interacts with ADPRT/PARP1.
{ECO:0000269|PubMed:11248244, ECO:0000269|PubMed:11751893}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-3917542, EBI-3917542;
A0A0S2Z5G4:BANP; NbExp=3; IntAct=EBI-3917542, EBI-16429704;
B4DE54:BANP; NbExp=4; IntAct=EBI-3917542, EBI-16429313;
Q8N9N5-2:BANP; NbExp=6; IntAct=EBI-3917542, EBI-11524452;
P24863:CCNC; NbExp=3; IntAct=EBI-3917542, EBI-395261;
P52292:KPNA2; NbExp=5; IntAct=EBI-3917542, EBI-349938;
Q06178:NMA1 (xeno); NbExp=3; IntAct=EBI-3917542, EBI-11803;
P38151:PBP2 (xeno); NbExp=3; IntAct=EBI-3917542, EBI-12968;
Q96EB6:SIRT1; NbExp=3; IntAct=EBI-3917542, EBI-1802965;
Q02821:SRP1 (xeno); NbExp=3; IntAct=EBI-3917542, EBI-1797;
P38340:TAE1 (xeno); NbExp=3; IntAct=EBI-3917542, EBI-21116;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11248244,
ECO:0000269|PubMed:12574164, ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:22842230}.
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in
skeletal muscle, heart and kidney. Also expressed in the liver
pancreas and placenta. Widely expressed throughout the brain.
{ECO:0000269|PubMed:11027696, ECO:0000269|PubMed:11891043}.
-!- DISEASE: Leber congenital amaurosis 9 (LCA9) [MIM:608553]: A
severe dystrophy of the retina, typically becoming evident in the
first years of life. Visual function is usually poor and often
accompanied by nystagmus, sluggish or near-absent pupillary
responses, photophobia, high hyperopia and keratoconus.
{ECO:0000269|PubMed:22842227, ECO:0000269|PubMed:22842229,
ECO:0000269|PubMed:22842230, ECO:0000269|PubMed:22842231}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
family. {ECO:0000305}.
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EMBL; AF314163; AAG33632.1; -; mRNA.
EMBL; AF312734; AAG33629.1; -; mRNA.
EMBL; AF459819; AAL76934.1; -; mRNA.
EMBL; AF459823; AAL76935.1; -; Genomic_DNA.
EMBL; AF459820; AAL76935.1; JOINED; Genomic_DNA.
EMBL; AF459821; AAL76935.1; JOINED; Genomic_DNA.
EMBL; AF459822; AAL76935.1; JOINED; Genomic_DNA.
EMBL; AK026065; BAB15345.1; -; mRNA.
EMBL; AK315640; BAG38007.1; -; mRNA.
EMBL; AL603962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL357140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471130; EAW71635.1; -; Genomic_DNA.
EMBL; BC014943; AAH14943.1; -; mRNA.
CCDS; CCDS108.1; -.
RefSeq; NP_001284707.1; NM_001297778.1.
RefSeq; NP_073624.2; NM_022787.3.
RefSeq; XP_016857596.1; XM_017002107.1.
UniGene; Hs.633762; -.
PDB; 1GZU; X-ray; 2.90 A; A/B/C=2-279.
PDB; 1KKU; X-ray; 2.50 A; A=1-279.
PDB; 1KQN; X-ray; 2.20 A; A/B/C/D/E/F=1-279.
PDB; 1KQO; X-ray; 2.50 A; A/B/C/D/E/F=1-279.
PDB; 1KR2; X-ray; 2.30 A; A/B/C/D/E/F=1-279.
PDBsum; 1GZU; -.
PDBsum; 1KKU; -.
PDBsum; 1KQN; -.
PDBsum; 1KQO; -.
PDBsum; 1KR2; -.
ProteinModelPortal; Q9HAN9; -.
SMR; Q9HAN9; -.
BioGrid; 122308; 48.
DIP; DIP-60881N; -.
IntAct; Q9HAN9; 25.
MINT; Q9HAN9; -.
STRING; 9606.ENSP00000366410; -.
DrugBank; DB04099; Deamido-Nad+.
DrugBank; DB03227; Nicotinamide Mononucleotide.
iPTMnet; Q9HAN9; -.
PhosphoSitePlus; Q9HAN9; -.
BioMuta; NMNAT1; -.
DMDM; 30580491; -.
EPD; Q9HAN9; -.
MaxQB; Q9HAN9; -.
PaxDb; Q9HAN9; -.
PeptideAtlas; Q9HAN9; -.
PRIDE; Q9HAN9; -.
DNASU; 64802; -.
Ensembl; ENST00000377205; ENSP00000366410; ENSG00000173614.
Ensembl; ENST00000462686; ENSP00000435134; ENSG00000173614.
GeneID; 64802; -.
KEGG; hsa:64802; -.
UCSC; uc001aqp.3; human.
CTD; 64802; -.
DisGeNET; 64802; -.
EuPathDB; HostDB:ENSG00000173614.13; -.
GeneCards; NMNAT1; -.
GeneReviews; NMNAT1; -.
HGNC; HGNC:17877; NMNAT1.
HPA; HPA059447; -.
MalaCards; NMNAT1; -.
MIM; 608553; phenotype.
MIM; 608700; gene.
neXtProt; NX_Q9HAN9; -.
OpenTargets; ENSG00000173614; -.
Orphanet; 65; Leber congenital amaurosis.
PharmGKB; PA31660; -.
eggNOG; KOG3199; Eukaryota.
eggNOG; COG1057; LUCA.
GeneTree; ENSGT00530000063189; -.
HOGENOM; HOG000216047; -.
HOVERGEN; HBG052640; -.
InParanoid; Q9HAN9; -.
KO; K06210; -.
OMA; DHFDHEI; -.
OrthoDB; EOG091G0JTI; -.
PhylomeDB; Q9HAN9; -.
TreeFam; TF315035; -.
BioCyc; MetaCyc:HS10701-MONOMER; -.
BRENDA; 2.7.7.1; 2681.
BRENDA; 2.7.7.18; 2681.
Reactome; R-HSA-196807; Nicotinate metabolism.
SABIO-RK; Q9HAN9; -.
UniPathway; UPA00253; UER00332.
UniPathway; UPA00253; UER00600.
ChiTaRS; NMNAT1; human.
EvolutionaryTrace; Q9HAN9; -.
GeneWiki; NMNAT1; -.
GenomeRNAi; 64802; -.
PRO; PR:Q9HAN9; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000173614; -.
CleanEx; HS_NMNAT1; -.
ExpressionAtlas; Q9HAN9; baseline and differential.
Genevisible; Q9HAN9; HS.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IDA:UniProtKB.
GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IDA:UniProtKB.
GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; IDA:UniProtKB.
GO; GO:0009435; P:NAD biosynthetic process; IC:UniProtKB.
GO; GO:0019674; P:NAD metabolic process; TAS:Reactome.
GO; GO:0009611; P:response to wounding; IEA:Ensembl.
InterPro; IPR004821; Cyt_trans-like.
InterPro; IPR005248; NadD/NMNAT.
Pfam; PF01467; CTP_transf_like; 1.
TIGRFAMs; TIGR00482; TIGR00482; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome;
Direct protein sequencing; Disease mutation;
Leber congenital amaurosis; Magnesium; NAD; Nucleotide-binding;
Nucleotidyltransferase; Nucleus; Phosphoprotein;
Pyridine nucleotide biosynthesis; Reference proteome; Transferase;
Zinc.
CHAIN 1 279 Nicotinamide/nicotinic acid
mononucleotide adenylyltransferase 1.
/FTId=PRO_0000135012.
NP_BIND 15 17 ATP. {ECO:0000250|UniProtKB:Q96T66,
ECO:0000305|PubMed:11788603}.
NP_BIND 156 158 ATP. {ECO:0000250|UniProtKB:Q96T66}.
NP_BIND 224 227 ATP. {ECO:0000250|UniProtKB:Q96T66}.
REGION 55 57 Substrate binding.
{ECO:0000269|PubMed:11959140}.
REGION 92 95 Substrate binding.
{ECO:0000269|PubMed:11788603,
ECO:0000269|PubMed:11959140}.
REGION 168 169 Substrate binding.
{ECO:0000269|PubMed:11788603,
ECO:0000269|PubMed:11959140}.
MOTIF 123 129 Nuclear localization signal.
{ECO:0000255}.
BINDING 24 24 ATP. {ECO:0000250|UniProtKB:Q96T66}.
BINDING 58 58 ATP. {ECO:0000250|UniProtKB:Q96T66}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 119 119 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
VARIANT 9 9 V -> M (in LCA9; does not affect nuclear
localization; results in significantly
reduced enzymatic activity;
dbSNP:rs387907294).
{ECO:0000269|PubMed:22842227}.
/FTId=VAR_068856.
VARIANT 13 13 A -> T (in LCA9; dbSNP:rs138613460).
{ECO:0000269|PubMed:22842227,
ECO:0000269|PubMed:22842229,
ECO:0000269|PubMed:22842230}.
/FTId=VAR_068857.
VARIANT 20 20 I -> N (in LCA9; dbSNP:rs761948762).
{ECO:0000269|PubMed:22842227}.
/FTId=VAR_068858.
VARIANT 33 33 D -> G (in LCA9).
{ECO:0000269|PubMed:22842227}.
/FTId=VAR_068859.
VARIANT 35 35 M -> T (in LCA9).
{ECO:0000269|PubMed:22842231}.
/FTId=VAR_068860.
VARIANT 54 54 A -> V (in LCA9; dbSNP:rs760965874).
{ECO:0000269|PubMed:22842227}.
/FTId=VAR_068861.
VARIANT 66 66 R -> W (in LCA9; does not affect nuclear
localization; results in significantly
reduced enzymatic activity;
dbSNP:rs763325435).
{ECO:0000269|PubMed:22842227}.
/FTId=VAR_068862.
VARIANT 67 67 V -> F (in LCA9; dbSNP:rs756903689).
{ECO:0000269|PubMed:22842230}.
/FTId=VAR_068863.
VARIANT 69 69 M -> V (in LCA9; dbSNP:rs372066126).
{ECO:0000269|PubMed:22842227,
ECO:0000269|PubMed:22842229}.
/FTId=VAR_068864.
VARIANT 72 72 L -> H (in LCA9).
{ECO:0000269|PubMed:22842227}.
/FTId=VAR_068865.
VARIANT 98 98 V -> G (in LCA9; dbSNP:rs771336246).
{ECO:0000269|PubMed:22842227,
ECO:0000269|PubMed:22842230,
ECO:0000269|PubMed:22842231}.
/FTId=VAR_068866.
VARIANT 147 147 A -> P (in LCA9).
{ECO:0000269|PubMed:22842229}.
/FTId=VAR_068867.
VARIANT 151 151 V -> F (in LCA9; dbSNP:rs387907292).
{ECO:0000269|PubMed:22842230,
ECO:0000269|PubMed:22842231}.
/FTId=VAR_068868.
VARIANT 153 153 L -> P (in LCA9).
{ECO:0000269|PubMed:22842229}.
/FTId=VAR_068869.
VARIANT 153 153 L -> V (in LCA9; dbSNP:rs387907293).
{ECO:0000269|PubMed:22842231}.
/FTId=VAR_068870.
VARIANT 156 156 G -> R (in LCA9).
{ECO:0000269|PubMed:22842227}.
/FTId=VAR_068871.
VARIANT 173 173 D -> G (in LCA9).
{ECO:0000269|PubMed:22842229}.
/FTId=VAR_068872.
VARIANT 178 178 V -> M (in LCA9; dbSNP:rs757724544).
{ECO:0000269|PubMed:22842229}.
/FTId=VAR_068873.
VARIANT 181 181 Y -> C (in LCA9; dbSNP:rs748913297).
{ECO:0000269|PubMed:22842229}.
/FTId=VAR_068874.
VARIANT 184 184 I -> M (in LCA9).
{ECO:0000269|PubMed:22842227}.
/FTId=VAR_068875.
VARIANT 207 207 R -> W (in LCA9; results in significantly
reduced enzymatic activity;
dbSNP:rs142968179).
{ECO:0000269|PubMed:22842229,
ECO:0000269|PubMed:22842230}.
/FTId=VAR_068876.
VARIANT 217 217 I -> N (in LCA9).
{ECO:0000269|PubMed:22842229}.
/FTId=VAR_068877.
VARIANT 237 237 R -> C (in LCA9; does not affect nuclear
localization; dbSNP:rs375110174).
{ECO:0000269|PubMed:22842227,
ECO:0000269|PubMed:22842229}.
/FTId=VAR_068878.
VARIANT 237 237 R -> L (in LCA9; dbSNP:rs368062092).
{ECO:0000269|PubMed:22842230}.
/FTId=VAR_068879.
VARIANT 239 239 L -> S (in LCA9; dbSNP:rs778606847).
{ECO:0000269|PubMed:22842229}.
/FTId=VAR_068880.
VARIANT 251 251 H -> P (in LCA9).
{ECO:0000269|PubMed:22842229}.
/FTId=VAR_068881.
VARIANT 257 257 E -> K (in LCA9; results in significantly
reduced enzymatic activity; the mutant
localizes to the cytoplasm;
dbSNP:rs150726175).
{ECO:0000269|PubMed:22842227,
ECO:0000269|PubMed:22842230,
ECO:0000269|PubMed:22842231}.
/FTId=VAR_068882.
VARIANT 273 273 N -> D (in LCA9; results in significantly
reduced enzymatic activity;
dbSNP:rs387907291).
{ECO:0000269|PubMed:22842230,
ECO:0000269|PubMed:22842231}.
/FTId=VAR_068883.
CONFLICT 20 20 I -> F (in Ref. 2; AAL76934/AAL76935).
{ECO:0000305}.
CONFLICT 217 217 I -> F (in Ref. 3; AAG33629).
{ECO:0000305}.
STRAND 7 15 {ECO:0000244|PDB:1KQN}.
HELIX 22 37 {ECO:0000244|PDB:1KQN}.
STRAND 39 50 {ECO:0000244|PDB:1KQN}.
HELIX 53 55 {ECO:0000244|PDB:1KQN}.
HELIX 63 73 {ECO:0000244|PDB:1KQN}.
TURN 74 76 {ECO:0000244|PDB:1KQN}.
STRAND 78 82 {ECO:0000244|PDB:1KQN}.
HELIX 86 88 {ECO:0000244|PDB:1KQN}.
HELIX 95 106 {ECO:0000244|PDB:1KQN}.
STRAND 150 156 {ECO:0000244|PDB:1KQN}.
HELIX 157 162 {ECO:0000244|PDB:1KQN}.
TURN 166 168 {ECO:0000244|PDB:1KQN}.
HELIX 171 180 {ECO:0000244|PDB:1KQN}.
STRAND 183 188 {ECO:0000244|PDB:1KQN}.
HELIX 190 198 {ECO:0000244|PDB:1KQN}.
HELIX 201 205 {ECO:0000244|PDB:1KQN}.
HELIX 206 209 {ECO:0000244|PDB:1KQN}.
STRAND 210 214 {ECO:0000244|PDB:1KQN}.
STRAND 217 219 {ECO:0000244|PDB:1KR2}.
HELIX 223 231 {ECO:0000244|PDB:1KQN}.
HELIX 242 251 {ECO:0000244|PDB:1KQN}.
HELIX 256 259 {ECO:0000244|PDB:1KQN}.
TURN 260 264 {ECO:0000244|PDB:1KQN}.
HELIX 268 274 {ECO:0000244|PDB:1KQN}.
SEQUENCE 279 AA; 31932 MW; 740DE872CD9C22E7 CRC64;
MENSEKTEVV LLACGSFNPI TNMHLRLFEL AKDYMNGTGR YTVVKGIISP VGDAYKKKGL
IPAYHRVIMA ELATKNSKWV EVDTWESLQK EWKETLKVLR HHQEKLEASD CDHQQNSPTL
ERPGRKRKWT ETQDSSQKKS LEPKTKAVPK VKLLCGADLL ESFAVPNLWK SEDITQIVAN
YGLICVTRAG NDAQKFIYES DVLWKHRSNI HVVNEWIAND ISSTKIRRAL RRGQSIRYLV
PDLVQEYIEK HNLYSSESED RNAGVILAPL QRNTAEAKT


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