NAT8L_RAT
ID NAT8L_RAT Reviewed; 299 AA.
AC D3ZVU9;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=N-acetylaspartate synthetase;
DE Short=NAA synthetase;
DE AltName: Full=N-acetyltransferase 8-like protein;
DE EC=2.3.1.17 {ECO:0000269|PubMed:18621030};
GN Name=Nat8l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18621030; DOI=10.1016/j.brainres.2008.06.040;
RA Ariyannur P.S., Madhavarao C.N., Namboodiri A.M.;
RT "N-acetylaspartate synthesis in the brain: mitochondria vs. microsomes.";
RL Brain Res. 1227:34-41(2008).
RN [3]
RP TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Catalyzes the synthesis of N-acetylaspartate acid (NAA) from
CC L-aspartate and acetyl-CoA (PubMed:18621030). Promotes dopamine uptake
CC by regulating TNF-alpha expression (By similarity). Attenuates
CC methamphetamine-induced inhibition of dopamine uptake (By similarity).
CC {ECO:0000250|UniProtKB:Q3UGX3, ECO:0000250|UniProtKB:Q8N9F0,
CC ECO:0000269|PubMed:18621030}.
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:18621030};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14166;
CC Evidence={ECO:0000305|PubMed:18621030};
CC -!- ACTIVITY REGULATION: Aminooxyacetic acid (AOAA) blocks its activity in
CC both cytoplasm and mitochondria. {ECO:0000250|UniProtKB:Q8N9F0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N9F0}.
CC Microsome membrane {ECO:0000269|PubMed:18621030}; Single-pass type I
CC membrane protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000269|PubMed:18621030}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q3UGX3}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, including in mesencephalic
CC dopaminergic neurons of the substantia nigra and ventral tegmental area
CC and oligodendrocytes. Expressed in cortical pyramidal neurons and
CC granule cells of the hippocampus (at protein level).
CC {ECO:0000269|PubMed:20385109}.
CC -!- SIMILARITY: Belongs to the camello family. {ECO:0000305}.
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DR EMBL; CH473963; EDM00108.1; -; Genomic_DNA.
DR RefSeq; NP_001178610.1; NM_001191681.1.
DR AlphaFoldDB; D3ZVU9; -.
DR SMR; D3ZVU9; -.
DR STRING; 10116.ENSRNOP00000066413; -.
DR PaxDb; D3ZVU9; -.
DR Ensembl; ENSRNOT00000074734; ENSRNOP00000066413; ENSRNOG00000049351.
DR GeneID; 289727; -.
DR KEGG; rno:289727; -.
DR CTD; 339983; -.
DR RGD; 1305719; Nat8l.
DR eggNOG; KOG3139; Eukaryota.
DR GeneTree; ENSGT00950000182932; -.
DR HOGENOM; CLU_013985_10_0_1; -.
DR InParanoid; D3ZVU9; -.
DR OMA; HCGPPDM; -.
DR OrthoDB; 1341682at2759; -.
DR PhylomeDB; D3ZVU9; -.
DR TreeFam; TF324687; -.
DR Reactome; R-RNO-8963693; Aspartate and asparagine metabolism.
DR PRO; PR:D3ZVU9; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Proteomes; UP000234681; Chromosome 14.
DR Bgee; ENSRNOG00000049351; Expressed in frontal cortex and 15 other tissues.
DR Genevisible; D3ZVU9; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA: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; ISO:RGD.
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_0000406989"
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"
SQ SEQUENCE 299 AA; 32719 MW; 4F971F8FFBE65780 CRC64;
MHCGPPDMVC ETKIVATEDH EALPGAKKDA LLAAAGAMWP PLPAAPGPAA APPPAAGPQP
HGGTGGAGPP EGRGVCIREF RAAEQEAARR IFYDGILERI PNTAFRGLRQ HPRTQLLYAL
LAALCFAVTR SLLLTCLVPA GLLALRYYYS RKVILAYLEC ALHTDMADIE QYYMKPPGSC
FWVAVLDGNV VGIVAARAHE EDNTVELLRM SVDSRFRGKG IAKALGRRVL EFAMLHNYSA
VVLGTTAVKV AAHKLYESLG FRHMGASDHY VLPGMTLSLA ERLFFQVRYH RYRLQLREE
