NAT8L_MOUSE
ID NAT8L_MOUSE Reviewed; 299 AA.
AC Q3UGX3; Q3UH43; Q6DID6; Q8K065;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=N-acetylaspartate synthetase;
DE Short=NAA synthetase;
DE EC=2.3.1.17 {ECO:0000269|PubMed:19807691, ECO:0000269|PubMed:20385109, ECO:0000269|PubMed:20643647};
DE AltName: Full=N-acetyltransferase 8-like protein;
DE AltName: Full=Protein Shati;
GN Name=Nat8l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-299, IDENTIFICATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY METHAMPHETAMINE.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=17626222; DOI=10.1523/jneurosci.1575-07.2007;
RA Niwa M., Nitta A., Mizoguchi H., Ito Y., Noda Y., Nagai T., Nabeshima T.;
RT "A novel molecule 'Shati' is involved in methamphetamine-induced
RT hyperlocomotion, sensitization, and conditioned place preference.";
RL J. Neurosci. 27:7604-7615(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-299.
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=19014384; DOI=10.1111/j.1471-4159.2008.05738.x;
RA Niwa M., Nitta A., Cen X., Kitaichi K., Ozaki N., Yamada K., Nabeshima T.;
RT "A novel molecule 'shati' increases dopamine uptake via the induction of
RT tumor necrosis factor-alpha in pheochromocytoma-12 cells.";
RL J. Neurochem. 107:1697-1708(2008).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=19807691; DOI=10.1042/bj20091024;
RA Wiame E., Tyteca D., Pierrot N., Collard F., Amyere M., Noel G.,
RA Desmedt J., Nassogne M.C., Vikkula M., Octave J.N., Vincent M.F.,
RA Courtoy P.J., Boltshauser E., van Schaftingen E.;
RT "Molecular identification of aspartate N-acetyltransferase and its mutation
RT in hypoacetylaspartia.";
RL Biochem. J. 425:127-136(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20385109; DOI=10.1016/j.brainres.2010.04.008;
RA Ariyannur P.S., Moffett J.R., Manickam P., Pattabiraman N., Arun P.,
RA Nitta A., Nabeshima T., Madhavarao C.N., Namboodiri A.M.;
RT "Methamphetamine-induced neuronal protein NAT8L is the NAA biosynthetic
RT enzyme: implications for specialized acetyl coenzyme A metabolism in the
RT CNS.";
RL Brain Res. 1335:1-13(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20643647; DOI=10.1074/jbc.m110.111765;
RA Becker I., Lodder J., Gieselmann V., Eckhardt M.;
RT "Molecular characterization of N-acetylaspartylglutamate synthetase.";
RL J. Biol. Chem. 285:29156-29164(2010).
CC -!- FUNCTION: Catalyzes the synthesis of N-acetylaspartate acid (NAA) from
CC L-aspartate and acetyl-CoA (PubMed:19807691, PubMed:20385109,
CC PubMed:20643647). Promotes dopamine uptake by regulating TNF-alpha
CC expression (PubMed:19014384). Attenuates methamphetamine-induced
CC inhibition of dopamine uptake (By similarity).
CC {ECO:0000250|UniProtKB:Q8N9F0, ECO:0000269|PubMed:19014384,
CC ECO:0000269|PubMed:19807691, ECO:0000269|PubMed:20385109,
CC ECO:0000269|PubMed:20643647}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-aspartate = CoA + H(+) + N-acetyl-L-aspartate;
CC Xref=Rhea:RHEA:14165, ChEBI:CHEBI:15378, ChEBI:CHEBI:16953,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.17;
CC Evidence={ECO:0000269|PubMed:19807691, ECO:0000269|PubMed:20385109,
CC ECO:0000269|PubMed:20643647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14166;
CC Evidence={ECO:0000305|PubMed:19807691};
CC -!- ACTIVITY REGULATION: Aminooxyacetic acid (AOAA) blocks its activity in
CC both cytoplasm and mitochondria. {ECO:0000250|UniProtKB:Q8N9F0}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 uM for aspartate {ECO:0000269|PubMed:20385109};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N9F0}.
CC Microsome membrane {ECO:0000250|UniProtKB:D3ZVU9}; Single-pass membrane
CC protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q8N9F0}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19807691}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, liver and spleen. In
CC brain, present in neurons but not in astrocytes (at protein level).
CC Expressed in brain, thymus and spleen. {ECO:0000269|PubMed:17626222,
CC ECO:0000269|PubMed:19807691, ECO:0000269|PubMed:20385109}.
CC -!- INDUCTION: By methamphetamine in brain, via dopamine receptor
CC activation (at protein level). {ECO:0000269|PubMed:17626222}.
CC -!- MISCELLANEOUS: Seems to modulate behavioral effects induced by
CC methamphetamine in vivo.
CC -!- MISCELLANEOUS: 'Shati' is the name of the symbol at Nagoya castle in
CC Japan.
CC -!- SIMILARITY: Belongs to the camello family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH75616.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABA54615.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK147307; BAE27836.1; -; mRNA.
DR EMBL; AK147594; BAE28014.1; -; mRNA.
DR EMBL; AK147703; BAE28084.1; -; mRNA.
DR EMBL; DQ174094; ABA54615.1; ALT_INIT; mRNA.
DR EMBL; BC034068; AAH34068.1; -; mRNA.
DR EMBL; BC075616; AAH75616.1; ALT_INIT; mRNA.
DR CCDS; CCDS19210.1; -.
DR RefSeq; NP_001001985.3; NM_001001985.3.
DR AlphaFoldDB; Q3UGX3; -.
DR BioGRID; 234689; 1.
DR STRING; 10090.ENSMUSP00000059313; -.
DR PhosphoSitePlus; Q3UGX3; -.
DR SwissPalm; Q3UGX3; -.
DR MaxQB; Q3UGX3; -.
DR PaxDb; Q3UGX3; -.
DR PeptideAtlas; Q3UGX3; -.
DR PRIDE; Q3UGX3; -.
DR ProteomicsDB; 287608; -.
DR DNASU; 269642; -.
DR GeneID; 269642; -.
DR KEGG; mmu:269642; -.
DR UCSC; uc008xbs.1; mouse.
DR CTD; 339983; -.
DR MGI; MGI:2447776; Nat8l.
DR eggNOG; KOG3139; Eukaryota.
DR InParanoid; Q3UGX3; -.
DR OrthoDB; 1341682at2759; -.
DR PhylomeDB; Q3UGX3; -.
DR TreeFam; TF324687; -.
DR BRENDA; 2.3.1.17; 3474.
DR Reactome; R-MMU-8963693; Aspartate and asparagine metabolism.
DR BioGRID-ORCS; 269642; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Nat8l; mouse.
DR PRO; PR:Q3UGX3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UGX3; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0017188; F:aspartate N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0051586; P:positive regulation of dopamine uptake involved in synaptic transmission; IDA:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Endoplasmic reticulum; Membrane; Microsome;
KW Mitochondrion; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..299
FT /note="N-acetylaspartate synthetase"
FT /id="PRO_0000305230"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 143..280
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 44..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 220
FT /note="S -> G (in Ref. 1; BAE28014, 2; ABA54615 and 3;
FT AAH75616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 32777 MW; 488DC1B586265DAD CRC64;
MHCGPPDMVC ETKIVATEDH EALPGAKKDA LLVAAGAMWP PLPAAPGPAA APPPAAGPQP
HGGTGGAGPP EGRGVCIREF RAAEQEAARR IFYDGILERI PNTAFRGLRQ HPRTQLLYAL
LAALCFAVTR SLLLTCLVPA GLLALRYYYS RKVILAYLEC ALHTDMADIE QYYMKPPGSC
FWVAVLDGNV VGIVAARAHE EDNTVELLRM SVDSRFRGKS IAKALGRRVL EFAMLHNYSA
VVLGTTAVKV AAHKLYESLG FRHMGASDHY VLPGMTLSLA ERLFFQVRYH RYRLQLREE
