GLSL_RAT
ID GLSL_RAT Reviewed; 602 AA.
AC P28492; Q3MHS6; Q5FVU0; Q64606;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Glutaminase liver isoform, mitochondrial;
DE Short=GLS;
DE EC=3.5.1.2 {ECO:0000250|UniProtKB:Q571F8};
DE AltName: Full=L-glutaminase;
DE AltName: Full=L-glutamine amidohydrolase;
DE Flags: Precursor;
GN Name=Gls2; Synonyms=Ga;
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 [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 68-94.
RC TISSUE=Liver;
RX PubMed=9164856; DOI=10.1042/bj3240193;
RA Chung-Bok M.I., Vincent N., Jhala U., Watford M.;
RT "Rat hepatic glutaminase: identification of the full coding sequence and
RT characterization of a functional promoter.";
RL Biochem. J. 324:193-200(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 147-602.
RC TISSUE=Liver;
RX PubMed=2191954; DOI=10.1016/s0021-9258(18)86993-9;
RA Smith E.M., Watford M.;
RT "Molecular cloning of a cDNA for rat hepatic glutaminase. Sequence
RT similarity to kidney-type glutaminase.";
RL J. Biol. Chem. 265:10631-10636(1990).
CC -!- FUNCTION: Plays an important role in the regulation of glutamine
CC catabolism. Promotes mitochondrial respiration and increases ATP
CC generation in cells by catalyzing the synthesis of glutamate and alpha-
CC ketoglutarate. Increases cellular anti-oxidant function via NADH and
CC glutathione production. May play a role in preventing tumor
CC proliferation. {ECO:0000250|UniProtKB:Q9UI32}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q571F8};
CC -!- SUBUNIT: Homotetramer, dimer of dimers (By similarity). Does not
CC assemble into higher oligomers (By similarity). Interacts with the PDZ
CC domain of the syntrophin SNTA1. Interacts with the PDZ domain of
CC TAX1BP3 (By similarity). {ECO:0000250|UniProtKB:Q571F8,
CC ECO:0000250|UniProtKB:Q9UI32}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9UI32}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28492-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28492-2; Sequence=VSP_015534;
CC -!- TISSUE SPECIFICITY: Liver specific.
CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH89776.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J05499; AAC37707.1; -; mRNA.
DR EMBL; L76175; AAC37708.1; -; Genomic_DNA.
DR EMBL; BC089776; AAH89776.1; ALT_INIT; mRNA.
DR EMBL; BC104712; AAI04713.1; -; mRNA.
DR PIR; A35444; A35444.
DR RefSeq; NP_001257715.1; NM_001270786.1. [P28492-1]
DR RefSeq; NP_001257716.1; NM_001270787.1.
DR RefSeq; NP_620259.2; NM_138904.2. [P28492-2]
DR RefSeq; XP_006240792.1; XM_006240730.2. [P28492-2]
DR AlphaFoldDB; P28492; -.
DR SMR; P28492; -.
DR BioGRID; 251392; 2.
DR IntAct; P28492; 1.
DR MINT; P28492; -.
DR STRING; 10116.ENSRNOP00000018737; -.
DR PhosphoSitePlus; P28492; -.
DR PaxDb; P28492; -.
DR PRIDE; P28492; -.
DR GeneID; 192268; -.
DR KEGG; rno:192268; -.
DR UCSC; RGD:620359; rat. [P28492-1]
DR CTD; 27165; -.
DR RGD; 620359; Gls2.
DR eggNOG; KOG0506; Eukaryota.
DR HOGENOM; CLU_016439_1_0_1; -.
DR InParanoid; P28492; -.
DR OrthoDB; 349094at2759; -.
DR PhylomeDB; P28492; -.
DR TreeFam; TF313359; -.
DR BioCyc; MetaCyc:MON-13074; -.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-8964539; Glutamate and glutamine metabolism.
DR SABIO-RK; P28492; -.
DR PRO; PR:P28492; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P28492; RN.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0004359; F:glutaminase activity; IBA:GO_Central.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006543; P:glutamine catabolic process; IBA:GO_Central.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.710.10; -; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR InterPro; IPR041541; Glutaminase_EF-hand.
DR PANTHER; PTHR12544; PTHR12544; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF17959; EF-hand_14; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR03814; Gln_ase; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; ANK repeat; Hydrolase; Mitochondrion;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 15..602
FT /note="Glutaminase liver isoform, mitochondrial"
FT /id="PRO_0000011627"
FT REPEAT 518..551
FT /note="ANK 1"
FT REPEAT 552..585
FT /note="ANK 2"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT MOD_RES 253
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q571F8"
FT MOD_RES 279
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q571F8"
FT MOD_RES 284
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q571F8"
FT MOD_RES 329
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q571F8"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9164856"
FT /id="VSP_015534"
FT CONFLICT 76
FT /note="L -> V (in Ref. 1; AAC37708)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..337
FT /note="KG -> NP (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 66248 MW; F4AE3BD30626A00F CRC64;
MRSMRALQNA LSRAGSHGQR GGWGHPSRGP LLGGGVRYYF GEAAAQGRGT PHSHQPQHSD
HDASNSGMLP RLGDLLFYTI AEGQERIPIH KFTTALKATG LQTSDPRLQD CMSKMQRMVQ
ESSSGGLLDR ELFQKCVSSN IVLLTQAFRK KFVIPDFEEF TGHVDRIFED AKELTGGKVA
AYIPHLAKSN PDLWGVSLCT VDGQRHSVGH TKIPFCLQSC VKPLTYAISV STLGTDYVHK
FVGKEPSGLR YNKLSLNEEG IPHNPMVNAG AIVVSSLIKM DCNKAEKFDF VLQYLNKMAG
NEFMGFSNAT FQSEKETGDR NYAIGYYLKE KKCFPKGVDM MAALDLYFQL CSVEVTCESG
SVMAATLANG GICPITGESV LSAEAVRNTL SLMHSCGMYD FSGQFAFHVG LPAKSAVSGA
ILLVVPNVMG MMCLSPPLDK LGNSHRGISF CQKLVSLFNF HNYDNLRHCA RKLDPRREGG
EVRNKTVVNL LFAAYSGDVS ALRRFALSAV DMEQKDYDSR TALHVAAAEG HIDVVKFLIE
ACKVNPFVKD RWGNIPLDDA VQFNHLEVVK LLQDYHDSYM LSETQAEVAA ETLSKENLES
MV
