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N-acetylaspartate synthetase (NAA synthetase) (EC 2.3.1.17) (Camello-like protein 3) (N-acetyltransferase 8-like protein)

 NAT8L_HUMAN             Reviewed;         302 AA.
Q8N9F0;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 3.
12-SEP-2018, entry version 124.
RecName: Full=N-acetylaspartate synthetase;
Short=NAA synthetase;
EC=2.3.1.17;
AltName: Full=Camello-like protein 3;
AltName: Full=N-acetyltransferase 8-like protein;
Name=NAT8L; Synonyms=CML3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 101-291.
PubMed=15146197; DOI=10.1038/nbt971;
Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J.,
Li Y., Xu C., Fang R., Guegler K., Rao M.S., Mandalam R.,
Lebkowski J., Stanton L.W.;
"Transcriptome characterization elucidates signaling networks that
control human ES cell growth and differentiation.";
Nat. Biotechnol. 22:707-716(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-302.
TISSUE=Brain, and PNS;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-302.
TISSUE=Brain;
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]
IDENTIFICATION.
PubMed=11397015; DOI=10.1006/dbio.2001.0261;
Popsueva A.E., Luchinskaya N.N., Ludwig A.V., Zinovjeva O.Y.,
Poteryaev D.A., Feigelman M.M., Ponomarev M.B., Berekelya L.,
Belyavsky A.V.;
"Overexpression of camello, a member of a novel protein family,
reduces blastomere adhesion and inhibits gastrulation in Xenopus
laevis.";
Dev. Biol. 234:483-496(2001).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19524112; DOI=10.1016/j.neuint.2009.03.003;
Arun P., Moffett J.R., Namboodiri A.M.;
"Evidence for mitochondrial and cytoplasmic N-acetylaspartate
synthesis in SH-SY5Y neuroblastoma cells.";
Neurochem. Int. 55:219-225(2009).
[7]
TISSUE SPECIFICITY, AND INVOLVEMENT IN NACED.
PubMed=19807691; DOI=10.1042/BJ20091024;
Wiame E., Tyteca D., Pierrot N., Collard F., Amyere M., Noel G.,
Desmedt J., Nassogne M.C., Vikkula M., Octave J.N., Vincent M.F.,
Courtoy P.J., Boltshauser E., van Schaftingen E.;
"Molecular identification of aspartate N-acetyltransferase and its
mutation in hypoacetylaspartia.";
Biochem. J. 425:127-136(2010).
[8]
ACTIVITY REGULATION, INDUCTION BY METHAMPHETAMINE, AND SUBCELLULAR
LOCATION.
PubMed=20385109; DOI=10.1016/j.brainres.2010.04.008;
Ariyannur P.S., Moffett J.R., Manickam P., Pattabiraman N., Arun P.,
Nitta A., Nabeshima T., Madhavarao C.N., Namboodiri A.M.;
"Methamphetamine-induced neuronal protein NAT8L is the NAA
biosynthetic enzyme: implications for specialized acetyl coenzyme A
metabolism in the CNS.";
Brain Res. 1335:1-13(2010).
-!- FUNCTION: Plays a role in the regulation of lipogenesis by
producing N-acetylaspartate acid (NAA), a brain-specific
metabolite. NAA occurs in high concentration in brain and its
hydrolysis plays a significant part in the maintenance of intact
white matter. Promotes dopamine uptake by regulating TNF-alpha
expression. Attenuates methamphetamine-induced inhibition of
dopamine uptake. {ECO:0000269|PubMed:19524112}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + L-aspartate = CoA + N-acetyl-L-
aspartate.
-!- ACTIVITY REGULATION: Aminooxyacetic acid (AOAA) blocks its
activity in both cytoplasm and mitochondria.
{ECO:0000269|PubMed:20385109}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000305}; Single-
pass membrane protein {ECO:0000305}. Microsome membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Mitochondrion membrane; Single-pass membrane protein. Rough
endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane
protein {ECO:0000250}. Note=Its enzymatic activity contribution is
quantitatively larger in mitochondrial compartment than in
extramitochondrial compartment.
-!- TISSUE SPECIFICITY: Expressed in brain.
{ECO:0000269|PubMed:19807691}.
-!- INDUCTION: By methamphetamine in brain, via dopamine receptor
activation (at protein level). {ECO:0000269|PubMed:20385109}.
-!- DISEASE: N-acetylaspartate deficiency (NACED) [MIM:614063]: A
metabolic disorder resulting in truncal ataxia, marked
developmental delay, seizures, and secondary microcephaly.
{ECO:0000269|PubMed:19807691}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the camello family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH93906.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH93908.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAI03749.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC04426.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AL132868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CN256164; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC093906; AAH93906.1; ALT_INIT; mRNA.
EMBL; BC093908; AAH93908.1; ALT_INIT; mRNA.
EMBL; BC103748; AAI03749.1; ALT_INIT; mRNA.
EMBL; AK094797; BAC04426.1; ALT_INIT; mRNA.
CCDS; CCDS3359.2; -.
RefSeq; NP_848652.2; NM_178557.3.
UniGene; Hs.318529; -.
ProteinModelPortal; Q8N9F0; -.
SMR; Q8N9F0; -.
BioGrid; 130978; 5.
IntAct; Q8N9F0; 1.
STRING; 9606.ENSP00000413064; -.
BioMuta; NAT8L; -.
DMDM; 259016335; -.
EPD; Q8N9F0; -.
MaxQB; Q8N9F0; -.
PaxDb; Q8N9F0; -.
PeptideAtlas; Q8N9F0; -.
PRIDE; Q8N9F0; -.
ProteomicsDB; 72525; -.
Ensembl; ENST00000423729; ENSP00000413064; ENSG00000185818.
GeneID; 339983; -.
KEGG; hsa:339983; -.
UCSC; uc003geq.3; human.
CTD; 339983; -.
DisGeNET; 339983; -.
EuPathDB; HostDB:ENSG00000185818.7; -.
GeneCards; NAT8L; -.
H-InvDB; HIX0024613; -.
HGNC; HGNC:26742; NAT8L.
HPA; HPA040677; -.
MalaCards; NAT8L; -.
MIM; 610647; gene.
MIM; 614063; phenotype.
neXtProt; NX_Q8N9F0; -.
OpenTargets; ENSG00000185818; -.
PharmGKB; PA162396985; -.
eggNOG; ENOG410KDG3; Eukaryota.
eggNOG; ENOG410YY26; LUCA.
GeneTree; ENSGT00390000009559; -.
HOGENOM; HOG000202639; -.
HOVERGEN; HBG108173; -.
InParanoid; Q8N9F0; -.
KO; K18309; -.
OMA; YMKPTGS; -.
OrthoDB; EOG091G0JGW; -.
PhylomeDB; Q8N9F0; -.
TreeFam; TF324687; -.
BRENDA; 2.3.1.17; 2681.
Reactome; R-HSA-70614; Amino acid synthesis and interconversion (transamination).
ChiTaRS; NAT8L; human.
GenomeRNAi; 339983; -.
PRO; PR:Q8N9F0; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000185818; Expressed in 158 organ(s), highest expression level in occipital lobe.
CleanEx; HS_NAT8L; -.
ExpressionAtlas; Q8N9F0; baseline and differential.
Genevisible; Q8N9F0; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0017188; F:aspartate N-acetyltransferase activity; IDA:UniProtKB.
GO; GO:0008652; P:cellular amino acid biosynthetic process; TAS:Reactome.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR000182; GNAT_dom.
Pfam; PF00583; Acetyltransf_1; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Cytoplasm; Endoplasmic reticulum;
Membrane; Microsome; Mitochondrion; Reference proteome; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 302 N-acetylaspartate synthetase.
/FTId=PRO_0000305229.
TRANSMEM 121 141 Helical. {ECO:0000255}.
DOMAIN 143 283 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
COMPBIAS 40 73 Pro-rich.
SEQUENCE 302 AA; 32837 MW; 2080E54930F3292B CRC64;
MHCGPPDMVC ETKIVAAEDH EALPGAKKDA LLAAAGAMWP PLPAAPGPAA APPAPPPAPV
AQPHGGAGGA GPPGGRGVCI REFRAAEQEA ARRIFYDGIM ERIPNTAFRG LRQHPRAQLL
YALLAALCFA VSRSLLLTCL VPAALLGLRY YYSRKVIRAY LECALHTDMA DIEQYYMKPP
GSCFWVAVLD GNVVGIVAAR AHEEDNTVEL LRMSVDSRFR GKGIAKALGR KVLEFAVVHN
YSAVVLGTTA VKVAAHKLYE SLGFRHMGAS DHYVLPGMTL SLAERLFFQV RYHRYRLQLR
EE


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