GLUCM_MOUSE
ID GLUCM_MOUSE Reviewed; 617 AA.
AC Q8BH86; Q8BNN0; Q8VC99;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=D-glutamate cyclase, mitochondrial {ECO:0000305};
DE EC=4.2.1.48 {ECO:0000269|PubMed:28266638};
DE Flags: Precursor;
GN Name=Dglucy;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Colon, Corpus striatum, and Hypothalamus;
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 MRNA] (ISOFORM 1).
RC STRAIN=CD-1; TISSUE=Kidney, and Neural stem cell;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Liver;
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28266638; DOI=10.1038/srep43911;
RA Ariyoshi M., Katane M., Hamase K., Miyoshi Y., Nakane M., Hoshino A.,
RA Okawa Y., Mita Y., Kaimoto S., Uchihashi M., Fukai K., Ono K., Tateishi S.,
RA Hato D., Yamanaka R., Honda S., Fushimura Y., Iwai-Kanai E., Ishihara N.,
RA Mita M., Homma H., Matoba S.;
RT "D-Glutamate is metabolized in the heart mitochondria.";
RL Sci. Rep. 7:43911-43911(2017).
CC -!- FUNCTION: D-glutamate cyclase that converts D-glutamate to 5-oxo-D-
CC proline. {ECO:0000269|PubMed:28266638}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glutamate = 5-oxo-D-proline + H2O; Xref=Rhea:RHEA:22360,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29986, ChEBI:CHEBI:57948; EC=4.2.1.48;
CC Evidence={ECO:0000269|PubMed:28266638};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:28266638}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BH86-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BH86-2; Sequence=VSP_010512, VSP_010513;
CC -!- DISRUPTION PHENOTYPE: Accumulation of D-glutamate in heart. Mice
CC develop normally and do not display any visible phenotype under normal
CC conditions. {ECO:0000269|PubMed:28266638}.
CC -!- SIMILARITY: Belongs to the D-glutamate cyclase family. {ECO:0000305}.
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DR EMBL; AK033551; BAC28352.1; -; mRNA.
DR EMBL; AK038436; BAC29998.1; -; mRNA.
DR EMBL; AK081256; BAC38177.1; -; mRNA.
DR EMBL; BC021385; AAH21385.1; -; mRNA.
DR EMBL; BC066161; AAH66161.1; -; mRNA.
DR CCDS; CCDS26108.1; -. [Q8BH86-1]
DR RefSeq; NP_663423.2; NM_145448.4. [Q8BH86-1]
DR RefSeq; XP_006515800.1; XM_006515737.2.
DR RefSeq; XP_006515801.1; XM_006515738.2. [Q8BH86-1]
DR AlphaFoldDB; Q8BH86; -.
DR SMR; Q8BH86; -.
DR BioGRID; 229965; 2.
DR STRING; 10090.ENSMUSP00000067830; -.
DR iPTMnet; Q8BH86; -.
DR PhosphoSitePlus; Q8BH86; -.
DR SwissPalm; Q8BH86; -.
DR REPRODUCTION-2DPAGE; IPI00308195; -.
DR EPD; Q8BH86; -.
DR jPOST; Q8BH86; -.
DR MaxQB; Q8BH86; -.
DR PaxDb; Q8BH86; -.
DR PeptideAtlas; Q8BH86; -.
DR PRIDE; Q8BH86; -.
DR ProteomicsDB; 271400; -. [Q8BH86-1]
DR ProteomicsDB; 271401; -. [Q8BH86-2]
DR Antibodypedia; 52277; 32 antibodies from 14 providers.
DR DNASU; 217830; -.
DR Ensembl; ENSMUST00000069782; ENSMUSP00000067830; ENSMUSG00000021185. [Q8BH86-1]
DR Ensembl; ENSMUST00000110069; ENSMUSP00000105696; ENSMUSG00000021185. [Q8BH86-1]
DR Ensembl; ENSMUST00000110070; ENSMUSP00000105697; ENSMUSG00000021185. [Q8BH86-2]
DR Ensembl; ENSMUST00000167322; ENSMUSP00000129876; ENSMUSG00000021185. [Q8BH86-1]
DR GeneID; 217830; -.
DR KEGG; mmu:217830; -.
DR UCSC; uc007osw.1; mouse. [Q8BH86-1]
DR CTD; 80017; -.
DR MGI; MGI:2444813; Dglucy.
DR VEuPathDB; HostDB:ENSMUSG00000021185; -.
DR eggNOG; ENOG502QV7A; Eukaryota.
DR GeneTree; ENSGT00390000002237; -.
DR HOGENOM; CLU_033607_0_0_1; -.
DR InParanoid; Q8BH86; -.
DR OMA; GIMGMEV; -.
DR PhylomeDB; Q8BH86; -.
DR TreeFam; TF300254; -.
DR BRENDA; 4.2.1.48; 3474.
DR BioGRID-ORCS; 217830; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q8BH86; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BH86; protein.
DR Bgee; ENSMUSG00000021185; Expressed in right kidney and 138 other tissues.
DR ExpressionAtlas; Q8BH86; baseline and differential.
DR Genevisible; Q8BH86; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0047820; F:D-glutamate cyclase activity; IDA:UniProtKB.
DR GO; GO:0006536; P:glutamate metabolic process; IDA:UniProtKB.
DR InterPro; IPR009906; D-Glu_cyclase.
DR InterPro; IPR017135; D-Glu_cyclase_mito.
DR InterPro; IPR025504; DUF4392.
DR InterPro; IPR038021; Putative_hydro-lyase.
DR Pfam; PF07286; DUF1445; 1.
DR Pfam; PF14336; DUF4392; 1.
DR PIRSF; PIRSF037204; UCP037204; 1.
DR SUPFAM; SSF160920; SSF160920; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Lyase; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..617
FT /note="D-glutamate cyclase, mitochondrial"
FT /id="PRO_0000036293"
FT MOD_RES 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 569..570
FT /note="EE -> PV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010512"
FT VAR_SEQ 571..617
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010513"
FT CONFLICT 80
FT /note="S -> P (in Ref. 2; AAH21385)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="L -> M (in Ref. 2; AAH21385)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="S -> F (in Ref. 2; AAH21385)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="G -> E (in Ref. 2; AAH21385)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 66366 MW; 418AA90D96F2F6DB CRC64;
MTISFLLRSC LRSAVRSLPK AALIRNTSSM TEGLQPASVV VLPRSLAPAF ESFCQGNRGP
LPLLGQSEAV KTLPQLSAVS DIRTICPQLQ KYKFGTCTGI LTSLEEHSEQ LKEMVTFIID
CSFSIEEALE QAGIPRRDLT GPSHAGAYKT TVPCATIAGF CCPLVVTMRP IPKDKLERLL
QATHAIRGQQ GQPIHIGDPG LLGIEALSKP DYGSYVECRP EDVPVFWPSP LTSLEAVISC
KAPLAFASPP GCMVMVPKDT ASSASCLTPE MVPEVHAISK DPLHYSIVSA PAAQKVRELE
STIAVDPGNR GIGHLLLKDE LLQAALSLSH ARSVLVTTGF PTHFNHEPPE ETDGPPGAIA
LAAFLQALGK ETAMVVDQRA LNLHMRIVED AIRQGVLKTP IPILTYQGRS MEDARAFLCK
DGDPKSPRFD HLVAIERAGR AADGNYYNAR KMNIKHLVDP IDDIFLAAQK IPGISSTGVG
DGGNELGMGK VKAAVKKHIR NGDVIACDVE ADFAVIAGVS NWGGYALACA LYILNSCQVH
ERYLRRATGP SRRAGEQSWI QALPSVAKEE KMLGILVENQ VRSGVSGIVG MEVDGLPFHD
VHAEMIRKLV GATTVHM
