ID RIMKA_MOUSE Reviewed; 380 AA.
AC Q6PFX8; Q8BXH0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=N-acetylaspartylglutamate synthase A;
DE Short=NAAG synthetase A;
DE Short=NAAGS;
DE EC=6.3.2.41 {ECO:0000269|PubMed:20657015, ECO:0000269|PubMed:21454531};
DE AltName: Full=N-acetylaspartylglutamylglutamate synthase A;
DE EC=6.3.2.42 {ECO:0000269|PubMed:21454531};
DE AltName: Full=Ribosomal protein S6 modification-like protein A;
GN Name=Rimkla; Synonyms=Fam80a, Rimk;
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=Cerebellum;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP 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 [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20657015; DOI=10.1074/jbc.m110.152629;
RA Collard F., Stroobant V., Lamosa P., Kapanda C.N., Lambert D.M.,
RA Muccioli G.G., Poupaert J.H., Opperdoes F., Van Schaftingen E.;
RT "Molecular identification of N-acetylaspartylglutamate synthase and beta-
RT citrylglutamate synthase.";
RL J. Biol. Chem. 285:29826-29833(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=21454531; DOI=10.1074/jbc.m111.230136;
RA Lodder-Gadaczek J., Becker I., Gieselmann V., Wang-Eckhardt L.,
RA Eckhardt M.;
RT "N-acetylaspartylglutamate synthetase II synthesizes N-
RT acetylaspartylglutamylglutamate.";
RL J. Biol. Chem. 286:16693-16706(2011).
CC -!- FUNCTION: Catalyzes the synthesis of N-acetyl-L-aspartyl-L-glutamate
CC (NAAG) and N-acetyl-L-aspartyl-L-glutamyl-L-glutamate.
CC {ECO:0000269|PubMed:20657015, ECO:0000269|PubMed:21454531}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + N-acetyl-L-aspartate = ADP + H(+) + N-
CC acetyl-L-aspartyl-L-glutamate + phosphate; Xref=Rhea:RHEA:40035,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16953, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:76931,
CC ChEBI:CHEBI:456216; EC=6.3.2.41;
CC Evidence={ECO:0000269|PubMed:20657015, ECO:0000269|PubMed:21454531};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + 2 L-glutamate + N-acetyl-L-aspartate = 2 ADP + 2 H(+)
CC + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate + 2 phosphate;
CC Xref=Rhea:RHEA:40039, ChEBI:CHEBI:15378, ChEBI:CHEBI:16953,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:76935, ChEBI:CHEBI:456216; EC=6.3.2.42;
CC Evidence={ECO:0000269|PubMed:21454531};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in spinal cord and brain.
CC {ECO:0000269|PubMed:21454531}.
CC -!- MISCELLANEOUS: N-acetyl-L-aspartyl-L-glutamate (NAAG) is the most
CC abundant dipeptide present in vertebrate central nervous system (CNS).
CC {ECO:0000303|PubMed:20657015}.
CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000305}.
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DR EMBL; AK047164; BAC32976.1; -; mRNA.
DR EMBL; AL645563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057371; AAH57371.1; -; mRNA.
DR CCDS; CCDS18583.1; -.
DR RefSeq; NP_808240.2; NM_177572.4.
DR AlphaFoldDB; Q6PFX8; -.
DR SMR; Q6PFX8; -.
DR STRING; 10090.ENSMUSP00000058996; -.
DR iPTMnet; Q6PFX8; -.
DR PhosphoSitePlus; Q6PFX8; -.
DR PaxDb; 10090-ENSMUSP00000058996; -.
DR ProteomicsDB; 255269; -.
DR Antibodypedia; 32199; 127 antibodies from 20 providers.
DR Ensembl; ENSMUST00000049994.8; ENSMUSP00000058996.8; ENSMUSG00000048899.9.
DR GeneID; 194237; -.
DR KEGG; mmu:194237; -.
DR UCSC; uc008umo.3; mouse.
DR AGR; MGI:3040686; -.
DR CTD; 284716; -.
DR MGI; MGI:3040686; Rimkla.
DR VEuPathDB; HostDB:ENSMUSG00000048899; -.
DR eggNOG; ENOG502QT4M; Eukaryota.
DR GeneTree; ENSGT00390000014577; -.
DR HOGENOM; CLU_054353_3_1_1; -.
DR InParanoid; Q6PFX8; -.
DR OMA; EKHGVMV; -.
DR OrthoDB; 4026633at2759; -.
DR PhylomeDB; Q6PFX8; -.
DR TreeFam; TF332035; -.
DR BRENDA; 6.3.2.41; 3474.
DR BRENDA; 6.3.2.42; 3474.
DR Reactome; R-MMU-8964539; Glutamate and glutamine metabolism.
DR BioGRID-ORCS; 194237; 5 hits in 76 CRISPR screens.
DR PRO; PR:Q6PFX8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6PFX8; Protein.
DR Bgee; ENSMUSG00000048899; Expressed in secondary oocyte and 137 other cell types or tissues.
DR Genevisible; Q6PFX8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0072590; F:N-acetyl-L-aspartate-L-glutamate ligase activity; IDA:UniProtKB.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621:SF1; N-ACETYLASPARTYLGLUTAMATE SYNTHASE A; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..380
FT /note="N-acetylaspartylglutamate synthase A"
FT /id="PRO_0000282569"
FT DOMAIN 115..300
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 345..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 189..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 260
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 369
FT /note="P -> R (in Ref. 1; BAC32976)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 41504 MW; 437D6477E6E9EE9B CRC64;
MCAQVWLLTD RLIREDYPQV QILRALRQRC SEQDVGFRAV FLDQIAVTVV GGHLGLQLSQ
KPLTTFPDVV VVRVSTPSVQ SDSEITILRH LEKLGCRLVN RPQSILNCIN KFWTFQELAG
HGVPMPDTFS YGGHEDFSKM IDEAEPLGYP VVVKSTRGHR GKAVFLARDK HHLSDICHLV
RHDVPYLFQK YVKESHGKDI RVVVVGGQVI GSMLRCSTDG RMQSNCFLGG VGVKCPLTEQ
GKQLAIQVSN ILGMDFCGID LLIMDDGSFT VCEANANVGF LAFDQACNLD VGAIIADYAM
SLLPNRQTGK MAILPGLASP REKNEPNGCV SAQGVAESVY AITNGSTSSE SEPELGEARD
SSVKTMGAPP AHVAQAWLQH
//
