GenomeNet

Database: UniProt
Entry: Q80WS1
LinkDB: Q80WS1
Original site: Q80WS1 
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   16-JAN-2019, entry version 125.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP   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
RT   beta-citrylglutamate synthase.";
RL   J. Biol. Chem. 285:29826-29833(2010).
CC   -!- FUNCTION: Catalyzes the synthesis of beta-citryl-L-glutamate and
CC       N-acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is
CC       synthesized 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(+) +
CC         N-acetyl-L-aspartyl-L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:40035, ChEBI:CHEBI:15378, ChEBI:CHEBI:16953,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:76931, ChEBI:CHEBI:456216; EC=6.3.2.41;
CC         Evidence={ECO:0000269|PubMed:20643647,
CC         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.
CC       {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         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q80WS1-3; Sequence=VSP_024200, VSP_024201, VSP_024202,
CC                                  VSP_024203;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in brain and testis.
CC       Expressed in eyes, thymus, lung, kidney, skeletal muscle, spleen,
CC       skin and heart. Expressed in neurons of the neocortex, the gray
CC       matter and Purkinje 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
CC       (CNS). Beta-citryl-L-glutamate, a structural analog of NAAG, is
CC       present in testis and immature brain.
CC       {ECO:0000303|PubMed:20657015}.
CC   -!- SIMILARITY: Belongs to the RimK family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32413.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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. [Q80WS1-1]
DR   RefSeq; XP_011239418.1; XM_011241116.2. [Q80WS1-1]
DR   RefSeq; XP_011239419.1; XM_011241117.1. [Q80WS1-1]
DR   RefSeq; XP_011239420.1; XM_011241118.2. [Q80WS1-1]
DR   RefSeq; XP_011239421.1; XM_011241119.1. [Q80WS1-1]
DR   RefSeq; XP_011239422.1; XM_011241120.1. [Q80WS1-2]
DR   UniGene; Mm.277939; -.
DR   ProteinModelPortal; Q80WS1; -.
DR   STRING; 10090.ENSMUSP00000064467; -.
DR   PhosphoSitePlus; Q80WS1; -.
DR   PaxDb; Q80WS1; -.
DR   PeptideAtlas; Q80WS1; -.
DR   PRIDE; Q80WS1; -.
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   eggNOG; ENOG410IGDC; Eukaryota.
DR   eggNOG; COG0189; LUCA.
DR   GeneTree; ENSGT00390000014577; -.
DR   HOGENOM; HOG000043112; -.
DR   HOVERGEN; HBG108408; -.
DR   InParanoid; Q80WS1; -.
DR   KO; K18310; -.
DR   OMA; PEAVCNM; -.
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-70614; Amino acid synthesis and interconversion (transamination).
DR   PRO; PR:Q80WS1; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000040649; Expressed in 238 organ(s), highest expression level in decidua.
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: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:0006464; P:cellular protein modification process; IEA:InterPro.
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; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    387       Beta-citrylglutamate synthase B.
FT                                /FTId=PRO_0000282572.
FT   DOMAIN      119    304       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     193    203       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   METAL       264    264       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       277    277       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       277    277       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       279    279       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   BINDING     158    158       ATP. {ECO:0000250}.
FT   BINDING     219    219       ATP. {ECO:0000250}.
FT   VAR_SEQ       1     57       Missing (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024200.
FT   VAR_SEQ      58     58       L -> M (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024201.
FT   VAR_SEQ     282    308       VGFIAFDKACNLDVAGIIADYAASLLP -> PFQEPKYTNT
FT                                NKQKILRENTFLLPPSC (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024202.
FT   VAR_SEQ     309    387       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=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
//
DBGET integrated database retrieval system