ID F1SLB4_PIG Unreviewed; 602 AA.
AC F1SLB4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN Name=GLS2 {ECO:0000313|Ensembl:ENSSSCP00000000427.4,
GN ECO:0000313|VGNC:VGNC:88497};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000000427.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000000427.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000000427.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000000427.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001062};
CC -!- SIMILARITY: Belongs to the glutaminase family.
CC {ECO:0000256|ARBA:ARBA00011076}.
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DR RefSeq; XP_003481672.1; XM_003481624.3.
DR RefSeq; XP_003481677.1; XM_003481629.3.
DR AlphaFoldDB; F1SLB4; -.
DR SMR; F1SLB4; -.
DR STRING; 9823.ENSSSCP00000000427; -.
DR PaxDb; 9823-ENSSSCP00000000427; -.
DR Ensembl; ENSSSCT00000000433.4; ENSSSCP00000000427.4; ENSSSCG00000000401.4.
DR GeneID; 100738224; -.
DR KEGG; ssc:100738224; -.
DR CTD; 27165; -.
DR VGNC; VGNC:88497; GLS2.
DR GeneTree; ENSGT00390000010463; -.
DR HOGENOM; CLU_016439_1_0_1; -.
DR InParanoid; F1SLB4; -.
DR OrthoDB; 537490at2759; -.
DR TreeFam; TF313359; -.
DR Reactome; R-SSC-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-SSC-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-SSC-8964539; Glutamate and glutamine metabolism.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000000401; Expressed in oocyte and 34 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR Gene3D; 1.10.238.210; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 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 NCBIfam; TIGR03814; Gln_ase; 1.
DR PANTHER; PTHR12544; GLUTAMINASE; 1.
DR PANTHER; PTHR12544:SF33; GLUTAMINASE LIVER ISOFORM, MITOCHONDRIAL; 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; Ankyrin repeat; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 73..155
FT /note="Glutaminase EF-hand"
FT /evidence="ECO:0000259|Pfam:PF17959"
FT REPEAT 518..540
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..65
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"
SQ SEQUENCE 602 AA; 66602 MW; 6E68B103A16C03C0 CRC64;
MRSMKALQNA LSRAGSHCRQ RGWGHLSRSP LLGGGVRHHL SEAAAQGRET PHSHQPLHQD
HDPSESGMLS RLGDLLFYTV AEGQERIPIH KFTTALKATG LQTSDPRLRD CMSQMRRRVR
ESSSGGLLDR DLFRKCVSSN IVLLTQAFRK KFVIPDFEEF TSHVDRIFED AKELTGGKVA
AYIPQLAKSN PDLWGVSLCT VDGQRHSVGN TKIPFCLQSC VKPLTYAISI STLGTDYVHK
FVGKEPSGLR YNKLSLNEEG IPHNPMVNAG AIVVSSLIKM DCNKAEKFDF VLQYLNKMAG
NEYMGFSNAT FQSEKETGDR NYAIGYYLKE KKCFPKGVDM MAALDLYFQL CSVEVTCESG
SVMAATLANG GICPITGESV LSAEAVRNTL SLMHSCGMYD FSGQFAFHVG LPAKSAVSGA
ILLVVPNVMG MMCLSPPLDK LGNSYRGVSF CQKLVSLFNF HNYDNLRHCT RKLDPRREGG
EIRNKTVVNL LFAAYSGDVS ALRRFALSAM DMEQKDYDSR TALHVAAAEG HTDVVKFLIE
ACKVNPFVKD RWGNIPMDDA VQFNHLEVVK LLQDYQDSYT PSETQAEAAA EALSKENLES
MV
//
