Q8N9F0 (NAT8L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetylaspartate synthetase
Short name=NAA synthetase
EC=2.3.1.17

Alternative name(s):
Camello-like protein 3
N-acetyltransferase 8-like protein

Gene names

Name:	NAT8L
Synonyms:	CML3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.6
Catalytic activity	Acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartate.
Enzyme regulation	Aminooxyacetic acid (AOAA) blocks its activity in both cytoplasm and mitochondria. Ref.8
Subcellular location	Cytoplasm. Membrane; Single-pass membrane protein Potential. Microsome membrane; Single-pass membrane protein By similarity. Mitochondrion membrane; Single-pass membrane protein. Rough endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Note: Its enzymatic activity contribution is quantitatively larger in mitochondrial compartment than in extramitochondrial compartment. Ref.6 Ref.8
Tissue specificity	Expressed in brain. Ref.7
Induction	By methamphetamine in brain, via dopamine receptor activation (at protein level). Ref.8
Involvement in disease	Defects in NAT8L are the cause of N-acetylaspartate deficiency (NACED) [MIM:614063]. A metabolic disorder resulting in truncal ataxia, marked developmental delay, seizures, and secondary microcephaly. Ref.7
Sequence similarities	Belongs to the camello family. Contains 1 N-acetyltransferase domain.
Sequence caution	The sequence AAH93906.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH93908.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAI03749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC04426.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAM15218.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum Membrane Microsome Mitochondrion
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial membrane Inferred from direct assay Ref.6Ref.8. Source: UniProtKB rough endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartate N-acetyltransferase activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	N-acetylaspartate synthetase		PRO_0000305229
Regions
	Transmembrane	121 – 141	21	Helical; Potential
	Domain	143 – 283	141	N-acetyltransferase
	Compositional bias	40 – 73	34	Pro-rich

Sequences

	Sequence		Length	Mass (Da)
	Q8N9F0 [UniParc]. Last modified September 22, 2009. Version 3. Checksum: 2080E54930F3292B	FASTA	302	32,837
	10 20 30 40 50 60 MHCGPPDMVC ETKIVAAEDH EALPGAKKDA LLAAAGAMWP PLPAAPGPAA APPAPPPAPV 70 80 90 100 110 120 AQPHGGAGGA GPPGGRGVCI REFRAAEQEA ARRIFYDGIM ERIPNTAFRG LRQHPRAQLL 130 140 150 160 170 180 YALLAALCFA VSRSLLLTCL VPAALLGLRY YYSRKVIRAY LECALHTDMA DIEQYYMKPP 190 200 210 220 230 240 GSCFWVAVLD GNVVGIVAAR AHEEDNTVEL LRMSVDSRFR GKGIAKALGR KVLEFAVVHN 250 260 270 280 290 300 YSAVVLGTTA VKVAAHKLYE SLGFRHMGAS DHYVLPGMTL SLAERLFFQV RYHRYRLQLR EE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." 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. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation." 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. Nat. Biotechnol. 22:707-716(2004) [PubMed: 15146197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-291.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-302. Tissue: Brain and PNS.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-302. Tissue: Brain.
[5]	"Overexpression of camello, a member of a novel protein family, reduces blastomere adhesion and inhibits gastrulation in Xenopus laevis." 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. Dev. Biol. 234:483-496(2001) [PubMed: 11397015] [Abstract] Cited for: IDENTIFICATION.
[6]	"Evidence for mitochondrial and cytoplasmic N-acetylaspartate synthesis in SH-SY5Y neuroblastoma cells." Arun P., Moffett J.R., Namboodiri A.M. Neurochem. Int. 55:219-225(2009) [PubMed: 19524112] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Molecular identification of aspartate N-acetyltransferase and its mutation in hypoacetylaspartia." 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. Biochem. J. 425:127-136(2010) [PubMed: 19807691] [Abstract] Cited for: TISSUE SPECIFICITY, INVOLVEMENT IN NACED.
[8]	"Methamphetamine-induced neuronal protein NAT8L is the NAA biosynthetic enzyme: implications for specialized acetyl coenzyme A metabolism in the CNS." Ariyannur P.S., Moffett J.R., Manickam P., Pattabiraman N., Arun P., Nitta A., Nabeshima T., Madhavarao C.N., Namboodiri A.M. Brain Res. 1335:1-13(2010) [PubMed: 20385109] [Abstract] Cited for: ENZYME REGULATION, INDUCTION BY METHAMPHETAMINE, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL132868 Genomic DNA. Translation: CAM15218.1. Sequence problems. CN256164 mRNA. No translation available. BC093906 mRNA. Translation: AAH93906.1. Different initiation. BC093908 mRNA. Translation: AAH93908.1. Different initiation. BC103748 mRNA. Translation: AAI03749.1. Different initiation. AK094797 mRNA. Translation: BAC04426.1. Different initiation.
IPI	IPI00167703.
RefSeq	NP_848652.2. NM_178557.3. XP_003403822.1. XM_003403774.1.
UniGene	Hs.318529.
3D structure databases
ProteinModelPortal	Q8N9F0.
SMR	Q8N9F0. Positions 182-271.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8N9F0.
Polymorphism databases
DMDM	259016335.
Proteomic databases
PRIDE	Q8N9F0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000423729; ENSP00000413064; ENSG00000185818.
GeneID	339983.
KEGG	hsa:339983.
Organism-specific databases
CTD	339983.
GeneCards	GC04P002031.
HGNC	HGNC:26742. NAT8L.
HPA	HPA040677.
MIM	610647. gene. 614063. phenotype.
neXtProt	NX_Q8N9F0.
PharmGKB	PA162396985.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000009559.
HOVERGEN	HBG108173.
InParanoid	Q8N9F0.
Gene expression databases
ArrayExpress	Q8N9F0.
Bgee	Q8N9F0.
CleanEx	HS_NAT8L.
Genevestigator	Q8N9F0.
Family and domain databases
InterPro	IPR000182. AcTrfase_GCN5-related_dom. IPR016181. Acyl_CoA_acyltransferase. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 2 hits.
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	97660.
SOURCE	Search...

Entry information

Entry name

NAT8L_HUMAN

Accession

Primary (citable) accession number: Q8N9F0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	September 22, 2009
Last modified:	December 14, 2011
This is version 68 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.