RIMKB_MOUSE
ID RIMKB_MOUSE Reviewed; 387 AA.
AC Q80WS1; Q69ZN3; Q8CA77; Q9D3Z1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Beta-citrylglutamate synthase B;
DE EC=6.3.1.17 {ECO:0000269|PubMed:20643647, ECO:0000269|PubMed:20657015};
DE AltName: Full=N-acetyl-aspartylglutamate synthetase B;
DE Short=NAAG synthetase B;
DE Short=NAAGS;
DE EC=6.3.2.41 {ECO:0000269|PubMed:20643647};
DE AltName: Full=Ribosomal protein S6 modification-like protein B;
GN Name=Rimklb; Synonyms=Fam80b, Kiaa1238;
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] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
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).
CC -!- FUNCTION: Catalyzes the synthesis of beta-citryl-L-glutamate and N-
CC acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized
CC more efficiently than N-acetyl-L-aspartyl-L-glutamate.
CC {ECO:0000269|PubMed:20643647, ECO:0000269|PubMed:20657015}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + citrate + L-glutamate = ADP + beta-citrylglutamate +
CC H(+) + phosphate; Xref=Rhea:RHEA:40043, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16947, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:76942, ChEBI:CHEBI:456216;
CC EC=6.3.1.17; Evidence={ECO:0000269|PubMed:20643647,
CC ECO:0000269|PubMed:20657015};
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:20643647, ECO:0000269|PubMed:20657015};
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:0000269|PubMed:20643647}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80WS1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80WS1-2; Sequence=VSP_024200, VSP_024201;
CC Name=3;
CC IsoId=Q80WS1-3; Sequence=VSP_024200, VSP_024201, VSP_024202,
CC VSP_024203;
CC -!- TISSUE SPECIFICITY: Strongly expressed in brain and testis. Expressed
CC in eyes, thymus, lung, kidney, skeletal muscle, spleen, skin and heart.
CC Expressed in neurons of the neocortex, the gray matter and Purkinje
CC cells. {ECO:0000269|PubMed:20643647}.
CC -!- MISCELLANEOUS: N-acetyl-L-aspartyl-L-glutamate (NAAG) is the most
CC abundant dipeptide present in vertebrate central nervous system (CNS).
CC Beta-citryl-L-glutamate, a structural analog of NAAG, is present in
CC testis and immature brain. {ECO:0000303|PubMed:20657015}.
CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32413.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173135; BAD32413.1; ALT_INIT; mRNA.
DR EMBL; AK016936; BAB30506.1; -; mRNA.
DR EMBL; AK039398; BAC30339.1; -; mRNA.
DR EMBL; BC052078; AAH52078.1; -; mRNA.
DR CCDS; CCDS39622.1; -. [Q80WS1-1]
DR RefSeq; NP_081940.1; NM_027664.1. [Q80WS1-1]
DR RefSeq; XP_011239417.1; XM_011241115.1.
DR RefSeq; XP_011239418.1; XM_011241116.2.
DR RefSeq; XP_011239419.1; XM_011241117.1.
DR RefSeq; XP_011239420.1; XM_011241118.2.
DR RefSeq; XP_011239421.1; XM_011241119.1.
DR RefSeq; XP_011239422.1; XM_011241120.1.
DR AlphaFoldDB; Q80WS1; -.
DR SMR; Q80WS1; -.
DR STRING; 10090.ENSMUSP00000064467; -.
DR PhosphoSitePlus; Q80WS1; -.
DR MaxQB; Q80WS1; -.
DR PaxDb; Q80WS1; -.
DR PeptideAtlas; Q80WS1; -.
DR PRIDE; Q80WS1; -.
DR ProteomicsDB; 255270; -. [Q80WS1-1]
DR ProteomicsDB; 255271; -. [Q80WS1-2]
DR ProteomicsDB; 255272; -. [Q80WS1-3]
DR Antibodypedia; 23082; 73 antibodies from 21 providers.
DR Ensembl; ENSMUST00000068242; ENSMUSP00000064467; ENSMUSG00000040649. [Q80WS1-1]
DR Ensembl; ENSMUST00000146274; ENSMUSP00000138104; ENSMUSG00000040649. [Q80WS1-3]
DR Ensembl; ENSMUST00000204731; ENSMUSP00000144770; ENSMUSG00000040649. [Q80WS1-2]
DR GeneID; 108653; -.
DR KEGG; mmu:108653; -.
DR UCSC; uc009dpf.1; mouse. [Q80WS1-2]
DR UCSC; uc009dpg.1; mouse. [Q80WS1-1]
DR CTD; 57494; -.
DR MGI; MGI:1918325; Rimklb.
DR VEuPathDB; HostDB:ENSMUSG00000040649; -.
DR eggNOG; ENOG502QT4M; Eukaryota.
DR GeneTree; ENSGT00390000014577; -.
DR HOGENOM; CLU_054353_3_0_1; -.
DR InParanoid; Q80WS1; -.
DR OMA; YEHKVFY; -.
DR OrthoDB; 753616at2759; -.
DR PhylomeDB; Q80WS1; -.
DR TreeFam; TF332035; -.
DR BRENDA; 6.3.1.17; 3474.
DR BRENDA; 6.3.2.41; 3474.
DR BRENDA; 6.3.2.B11; 3474.
DR Reactome; R-MMU-8964539; Glutamate and glutamine metabolism.
DR BioGRID-ORCS; 108653; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Rimklb; mouse.
DR PRO; PR:Q80WS1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80WS1; protein.
DR Bgee; ENSMUSG00000040649; Expressed in decidua and 214 other tissues.
DR ExpressionAtlas; Q80WS1; baseline and differential.
DR Genevisible; Q80WS1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0072591; F:citrate-L-glutamate ligase activity; IDA:UniProtKB.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IBA:GO_Central.
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 Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR Pfam; PF08443; RimK; 1.
DR TIGRFAMs; TIGR00768; rimK_fam; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..387
FT /note="Beta-citrylglutamate synthase B"
FT /id="PRO_0000282572"
FT DOMAIN 119..304
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 325..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 193..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024200"
FT VAR_SEQ 58
FT /note="L -> M (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024201"
FT VAR_SEQ 282..308
FT /note="VGFIAFDKACNLDVAGIIADYAASLLP -> PFQEPKYTNTNKQKILRENTF
FT LLPPSC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024202"
FT VAR_SEQ 309..387
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024203"
SQ SEQUENCE 387 AA; 42528 MW; 97B90EABDD414CC6 CRC64;
MCSSVTGKLW FLTDRRIRED YPQKEILRAL KAKCCEEELD FRAVVMDEMV LTVEQGNLGL
RISGELISAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC RLMNRPQAIL NCVNKFWTFQ
ELAGHGVPLP DTFSYGGHEN FAKMIDEAEV LEFPMVVKNT RGHRGKAVFL ARDKHHLADL
SHLIRHEAPY LFQKYIKESH GRDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS
LSEQGKQLAI QVSNILGTDV CGIDLLMKDD GSFCVCEANA NVGFIAFDKA CNLDVAGIIA
DYAASLLPAG RLTRRMSLLS VVSTASETSE PELGPPASAA VDNMSASSSS VDSDPESTTE
REMLTKLPGG LFNMNQLLAN EIKLLVE
