ID GLSK_HUMAN Reviewed; 669 AA. AC O94925; Q9UL05; Q9UL06; Q9UL07; Q9UN40; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 220. DE RecName: Full=Glutaminase kidney isoform, mitochondrial; DE Short=GLS; DE EC=3.5.1.2 {ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000269|PubMed:24451979, ECO:0000269|PubMed:26988803, ECO:0000269|PubMed:28526749, ECO:0000269|PubMed:29317493}; DE AltName: Full=K-glutaminase; DE AltName: Full=L-glutamine amidohydrolase; DE Contains: DE RecName: Full=Glutaminase kidney isoform, mitochondrial 68 kDa chain {ECO:0000250|UniProtKB:P13264}; DE Contains: DE RecName: Full=Glutaminase kidney isoform, mitochondrial 65 kDa chain {ECO:0000250|UniProtKB:P13264}; DE Flags: Precursor; GN Name=GLS; Synonyms=GLS1, KIAA0838; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, ALTERNATIVE RP SPLICING, AND FUNCTION. RC TISSUE=Placenta; RX PubMed=11015561; DOI=10.1152/physiolgenomics.1999.1.2.51; RA Elgadi K.M., Meguid R.A., Qian M., Souba W.W., Abcouwer S.F.; RT "Cloning and analysis of unique human glutaminase isoforms generated by RT tissue-specific alternative splicing."; RL Physiol. Genomics 1:51-62(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Chavez R.A., Wang C., Cong R., Hawkinson J.E., Forsayeth J.R.; RT "Identification and expression of human renal and hepatic glutaminase RT isoforms."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10719215; DOI=10.1016/s0169-328x(99)00331-9; RA Holcomb T., Taylor L., Trohkimoinen J., Curthoys N.P.; RT "Isolation, characterization and expression of a human brain mitochondrial RT glutaminase cDNA."; RL Brain Res. Mol. Brain Res. 76:56-63(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 225-466. RC TISSUE=Colon carcinoma; RA Turner A., McGivan J.D.; RT "Adenoma and carcinoma cell lines derived from colorectal tumours express RT different isoforms of glutaminase."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [8] RP INTERACTION WITH ATCAY, AND SUBCELLULAR LOCATION. RX PubMed=16899818; DOI=10.1242/jcs.03061; RA Buschdorf J.P., Li Chew L., Zhang B., Cao Q., Liang F.Y., Liou Y.C., RA Zhou Y.T., Low B.C.; RT "Brain-specific BNIP-2-homology protein Caytaxin relocalises glutaminase to RT neurite terminals and reduces glutamate levels."; RL J. Cell Sci. 119:3337-3350(2006). RN [9] RP TISSUE SPECIFICITY (ISOFORM 1 AND ISOFORM 3). RX PubMed=17940881; DOI=10.1007/s11064-007-9507-6; RA Szeliga M., Matyja E., Obara M., Grajkowska W., Czernicki T., Albrecht J.; RT "Relative expression of mRNAs coding for glutaminase isoforms in CNS RT tissues and CNS tumors."; RL Neurochem. Res. 33:808-813(2008). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-311, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=22228304; DOI=10.1073/pnas.1112495109; RA Cassago A., Ferreira A.P., Ferreira I.M., Fornezari C., Gomes E.R., RA Greene K.S., Pereira H.M., Garratt R.C., Dias S.M., Ambrosio A.L.; RT "Mitochondrial localization and structure-based phosphate activation RT mechanism of glutaminase C with implications for cancer metabolism."; RL Proc. Natl. Acad. Sci. U.S.A. 109:1092-1097(2012). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [15] RP FUNCTION, INVOLVEMENT IN DEE71, AND VARIANTS DEE71 81-GLN--LEU-669 DEL AND RP LYS-272. RX PubMed=30575854; DOI=10.1001/jamaneurol.2018.2941; RA Rumping L., Buettner B., Maier O., Rehmann H., Lequin M., Schlump J.U., RA Schmitt B., Schiebergen-Bronkhorst B., Prinsen H.C.M.T., Losa M., RA Fingerhut R., Lemke J.R., Zwartkruis F.J.T., Houwen R.H.J., Jans J.J.M., RA Verhoeven-Duif N.M., van Hasselt P.M., Jamra R.; RT "Identification of a loss-of-function mutation in the context of RT glutaminase deficiency and neonatal epileptic encephalopathy."; RL JAMA Neurol. 76:342-350(2019). RN [16] RP FUNCTION, INVOLVEMENT IN CASGID, VARIANT CASGID CYS-482, AND RP CHARACTERIZATION OF VARIANT CASGID CYS-482. RX PubMed=30239721; DOI=10.1093/hmg/ddy330; RA Rumping L., Tessadori F., Pouwels P.J.W., Vringer E., Wijnen J.P., RA Bhogal A.A., Savelberg S.M.C., Duran K.J., Bakkers M.J.G., Ramos R.J.J., RA Schellekens P.A.W., Kroes H.Y., Klomp D.W.J., Black G.C.M., Taylor R.L., RA Bakkers J.P.W., Prinsen H.C.M.T., van der Knaap M.S., Dansen T.B., RA Rehmann H., Zwartkruis F.J.T., Houwen R.H.J., van Haaften G., RA Verhoeven-Duif N.M., Jans J.J.M., van Hasselt P.M.; RT "GLS hyperactivity causes glutamate excess, infantile cataract and profound RT developmental delay."; RL Hum. Mol. Genet. 28:96-104(2019). RN [17] RP FUNCTION, INVOLVEMENT IN GDPAG, VARIANT GDPAG LEU-313, AND CHARACTERIZATION RP OF VARIANT GDPAG LEU-313. RX PubMed=30970188; DOI=10.1056/nejmoa1806627; RA van Kuilenburg A.B.P., Tarailo-Graovac M., Richmond P.A., RA Droegemoeller B.I., Pouladi M.A., Leen R., Brand-Arzamendi K., RA Dobritzsch D., Dolzhenko E., Eberle M.A., Hayward B., Jones M.J., RA Karbassi F., Kobor M.S., Koster J., Kumari D., Li M., MacIsaac J., RA McDonald C., Meijer J., Nguyen C., Rajan-Babu I.S., Scherer S.W., Sim B., RA Trost B., Tseng L.A., Turkenburg M., van Vugt J.J.F.A., Veldink J.H., RA Walia J.S., Wang Y., van Weeghel M., Wright G.E.B., Xu X., Yuen R.K.C., RA Zhang J., Ross C.J., Wasserman W.W., Geraghty M.T., Santra S., RA Wanders R.J.A., Wen X.Y., Waterham H.R., Usdin K., van Karnebeek C.D.M.; RT "Glutaminase deficiency caused by short tandem repeat expansion in GLS."; RL N. Engl. J. Med. 380:1433-1441(2019). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 71-550 (ISOFORM 3) IN COMPLEXES RP WITH GLUTAMATE AND SYNTHETIC INHIBITOR BPTES, PROTEIN SEQUENCE OF RP N-TERMINUS, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-318; PHE-322 AND RP TYR-394, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, IDENTIFICATION RP BY MASS SPECTROMETRY, AND SUBUNIT. RX PubMed=22049910; DOI=10.1021/bi201613d; RA DeLaBarre B., Gross S., Fang C., Gao Y., Jha A., Jiang F., Song J.J., RA Wei W., Hurov J.B.; RT "Full-length human glutaminase in complex with an allosteric inhibitor."; RL Biochemistry 50:10764-10770(2011). RN [19] {ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3VOY, ECO:0007744|PDB:3VOZ, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1, ECO:0007744|PDB:3VP2, ECO:0007744|PDB:3VP3, ECO:0007744|PDB:3VP4} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 221-533 IN COMPLEXES WITH RP GLUTAMATE AND GLUTAMINE, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH RAF1 RP AND MAP2K2, AND MUTAGENESIS OF LEU-321; LEU-323 AND TYR-394. RX PubMed=22538822; DOI=10.1073/pnas.1116573109; RA Thangavelu K., Pan C.Q., Karlberg T., Balaji G., Uttamchandani M., RA Suresh V., Schuler H., Low B.C., Sivaraman J.; RT "Structural basis for the allosteric inhibitory mechanism of human kidney- RT type glutaminase (KGA) and its regulation by Raf-Mek-Erk signaling in RT cancer cell metabolism."; RL Proc. Natl. Acad. Sci. U.S.A. 109:7705-7710(2012). RN [20] {ECO:0007744|PDB:4O7D} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 221-531 IN COMPLEX WITH SUBSTRATE RP ANALOG, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF RP TYR-249; SER-286; LYS-289 AND TYR-466. RX PubMed=24451979; DOI=10.1038/srep03827; RA Thangavelu K., Chong Q.Y., Low B.C., Sivaraman J.; RT "Structural basis for the active site inhibition mechanism of human kidney- RT type glutaminase (KGA)."; RL Sci. Rep. 4:3827-3827(2014). RN [21] {ECO:0007744|PDB:5FI2, ECO:0007744|PDB:5FI6, ECO:0007744|PDB:5FI7, ECO:0007744|PDB:5I94} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 72-550, CATALYTIC ACTIVITY, AND RP SUBUNIT. RX PubMed=26988803; DOI=10.1016/j.bmc.2016.03.009; RA McDermott L.A., Iyer P., Vernetti L., Rimer S., Sun J., Boby M., Yang T., RA Fioravanti M., O'Neill J., Wang L., Drakes D., Katt W., Huang Q., RA Cerione R.; RT "Design and evaluation of novel glutaminase inhibitors."; RL Bioorg. Med. Chem. 24:1819-1839(2016). RN [22] {ECO:0007744|PDB:5U0I, ECO:0007744|PDB:5U0J, ECO:0007744|PDB:5UQE} RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 551-669, CATALYTIC ACTIVITY, RP DOMAIN, AND SUBUNIT. RX PubMed=28526749; DOI=10.1074/jbc.m117.787291; RA Pasquali C.C., Islam Z., Adamoski D., Ferreira I.M., Righeto R.D., RA Bettini J., Portugal R.V., Yue W.W., Gonzalez A., Dias S.M.G., RA Ambrosio A.L.B.; RT "The origin and evolution of human glutaminases and their atypical C- RT terminal ankyrin repeats."; RL J. Biol. Chem. 292:11572-11585(2017). RN [23] {ECO:0007744|PDB:5WJ6} RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 72-550, CATALYTIC ACTIVITY, AND RP SUBUNIT. RX PubMed=29317493; DOI=10.1074/jbc.m117.810101; RA Huang Q., Stalnecker C., Zhang C., McDermott L.A., Iyer P., O'Neill J., RA Reimer S., Cerione R.A., Katt W.P.; RT "Characterization of the interactions of potent allosteric inhibitors with RT glutaminase C, a key enzyme in cancer cell glutamine metabolism."; RL J. Biol. Chem. 293:3535-3545(2018). CC -!- FUNCTION: Catalyzes the first reaction in the primary pathway for the CC renal catabolism of glutamine. Plays a role in maintaining acid-base CC homeostasis. Regulates the levels of the neurotransmitter glutamate, CC the main excitatory neurotransmitter in the brain (PubMed:30575854, CC PubMed:30239721, PubMed:30970188). {ECO:0000269|PubMed:30239721, CC ECO:0000269|PubMed:30575854, ECO:0000269|PubMed:30970188}. CC -!- FUNCTION: [Isoform 2]: Lacks catalytic activity. CC {ECO:0000269|PubMed:11015561}. 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:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, CC ECO:0000269|PubMed:24451979, ECO:0000269|PubMed:26988803, CC ECO:0000269|PubMed:28526749, ECO:0000269|PubMed:29317493}; CC -!- ACTIVITY REGULATION: Isoform 1 and isoform 3 are activated by CC phosphate. Inhibited by BPTES. BPTES binds between subunits and favors CC dissociation of the tetramer into dimers (PubMed:22049910). Inhibited CC by 6-diazo-5-oxo-L-norleucine (DON) (PubMed:24451979). Enzyme activity CC is stimulated by phosphorylation (PubMed:22538822). CC {ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, CC ECO:0000269|PubMed:24451979}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.9 mM for glutamine (isoform 1) {ECO:0000269|PubMed:22049910}; CC KM=1.4 mM for glutamine (isoform 3) {ECO:0000269|PubMed:22049910}; CC -!- SUBUNIT: Homotetramer, dimer of dimers (PubMed:22538822, CC PubMed:26988803, PubMed:28526749, PubMed:29317493). The tetramers can CC assemble into rod-like oligomers (in vitro), but the physiological CC significance of this is not clear (By similarity). Interacts with RAF1 CC and MAP2K2 (PubMed:22538822). Interacts with ATCAY; the interaction is CC direct and may control GLS localization, negatively regulating its CC activity. {ECO:0000250|UniProtKB:D3Z7P3, ECO:0000269|PubMed:16899818, CC ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, CC ECO:0000269|PubMed:26988803, ECO:0000269|PubMed:28526749, CC ECO:0000269|PubMed:29317493}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion CC {ECO:0000250|UniProtKB:P13264}. Cytoplasm, cytosol CC {ECO:0000269|PubMed:22228304}. Note=The 74-kDa cytosolic precursor is CC translocated into the mitochondria and processed via a 72-kDa CC intermediate to yield the mature 68- and 65-kDa subunits. CC {ECO:0000250|UniProtKB:P13264}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion CC {ECO:0000269|PubMed:22228304}. CC -!- SUBCELLULAR LOCATION: [Glutaminase kidney isoform, mitochondrial 68 kDa CC chain]: Mitochondrion matrix {ECO:0000250|UniProtKB:P13264}. CC Note=Produced by the proteolytic processing of the 74-kDa cytosolic CC precursor. {ECO:0000250|UniProtKB:P13264}. CC -!- SUBCELLULAR LOCATION: [Glutaminase kidney isoform, mitochondrial 65 kDa CC chain]: Mitochondrion matrix {ECO:0000250|UniProtKB:P13264}. CC Note=Produced by the proteolytic processing of the 74-kDa cytosolic CC precursor. {ECO:0000250|UniProtKB:P13264}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=KGA {ECO:0000303|PubMed:22228304, CC ECO:0000303|PubMed:22538822, ECO:0000303|PubMed:28526749}; CC IsoId=O94925-1; Sequence=Displayed; CC Name=2; Synonyms=GAM; CC IsoId=O94925-2; Sequence=VSP_001765, VSP_001766; CC Name=3; Synonyms=Glutaminase C {ECO:0000303|PubMed:22228304}, GAC CC {ECO:0000303|PubMed:22228304, ECO:0000303|PubMed:28526749}; CC IsoId=O94925-3; Sequence=VSP_001767; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are detected in brain CC cortex. Isoform 3 is highly expressed in astrocytoma, ganglioglioma and CC ependymoma. Isoform 1 is highly expressed in brain and kidney, but not CC detected in liver. Isoform 3 is highly expressed in heart and pancreas, CC detected at lower levels in placenta, lung, pancreas and kidney, but is CC not detected in liver. Isoform 2 is expressed in cardiac and skeletal CC muscle. {ECO:0000269|PubMed:11015561}. CC -!- DOMAIN: The C-terminal ANK repeats prevent the assembly of the supra- CC tetrameric filaments. {ECO:0000269|PubMed:28526749}. CC -!- DOMAIN: A highly mobile activation loop at the dimer-dimer interface is CC important for enzyme activity. {ECO:0000250|UniProtKB:D3Z7P3}. CC -!- PTM: Synthesized as a 74-kDa cytosolic precursor which is CC proteolytically processed by the mitochondrial-processing peptidase CC (MPP) via a 72-kDa intermediate to yield the mature mitochondrial CC 68- and 65-kDa subunits. {ECO:0000250|UniProtKB:P13264}. CC -!- DISEASE: Developmental and epileptic encephalopathy 71 (DEE71) CC [MIM:618328]: A form of epileptic encephalopathy, a heterogeneous group CC of severe early-onset epilepsies characterized by refractory seizures, CC neurodevelopmental impairment, and poor prognosis. Development is CC normal prior to seizure onset, after which cognitive and motor delays CC become apparent. DEE71 is an autosomal recessive form with onset at CC birth. Death occurs in first weeks of life. CC {ECO:0000269|PubMed:30575854}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Infantile cataract, skin abnormalities, glutamate excess, and CC impaired intellectual development (CASGID) [MIM:618339]: An autosomal CC dominant disease characterized by infantile-onset cataract, erythematic CC subcutaneous nodules, profound developmental delay, self-injurious CC behavior, and intracerebral glutamate excess. Histopathologic analysis CC of skin lesions show deep perivascular and periglandular CC lymphohistiocytic infiltrates and pronounced leukocytoclasia at the CC surface of the dermis, focal vacuolar alterations, hyperkeratosis, and CC parakeratosis of the epidermis. {ECO:0000269|PubMed:30239721}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Global developmental delay, progressive ataxia, and elevated CC glutamine (GDPAG) [MIM:618412]: An autosomal recessive disease CC characterized by early-onset delay in motor skills, delayed speech, CC progressive ataxia, and neurologic deterioration. Plasma glutamine is CC persistently elevated by a factor of 2.5 despite normal plasma ammonia CC levels. {ECO:0000269|PubMed:30970188}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000305}. CC -!- CAUTION: Isoform 3 is predicted to be expressed at very low levels due CC to a premature stop codon in the mRNA, leading to nonsense-mediated CC mRNA decay. Contrary to expectations, it has been shown to be well CC expressed, and the encoded protein is detected in mitochondria CC (PubMed:11015561, PubMed:17940881, PubMed:22228304). CC {ECO:0000269|PubMed:11015561, ECO:0000269|PubMed:17940881, CC ECO:0000269|PubMed:22228304, ECO:0000305|PubMed:14759258}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA74861.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF158555; AAD47056.1; -; mRNA. DR EMBL; AF097492; AAF00088.1; -; mRNA. DR EMBL; AF097493; AAF00089.1; -; mRNA. DR EMBL; AF097495; AAF00090.1; -; mRNA. DR EMBL; AB020645; BAA74861.2; ALT_INIT; mRNA. DR EMBL; AF223943; AAF33825.1; -; mRNA. DR EMBL; AF327434; AAG47842.1; -; mRNA. DR EMBL; BC038507; AAH38507.2; -; mRNA. DR EMBL; AF279697; AAG17700.1; -; mRNA. DR CCDS; CCDS2308.1; -. [O94925-1] DR CCDS; CCDS58744.1; -. [O94925-3] DR RefSeq; NP_001243239.1; NM_001256310.1. [O94925-3] DR RefSeq; NP_055720.3; NM_014905.4. [O94925-1] DR PDB; 3CZD; X-ray; 2.40 A; A=221-533. DR PDB; 3UNW; X-ray; 2.56 A; A/B/C/D=71-597. DR PDB; 3UO9; X-ray; 2.30 A; A/B/C/D=71-597. DR PDB; 3VOY; X-ray; 2.20 A; A=221-533. DR PDB; 3VOZ; X-ray; 2.40 A; A=221-533. DR PDB; 3VP0; X-ray; 2.40 A; A=221-533. DR PDB; 3VP1; X-ray; 2.30 A; A=221-533. DR PDB; 3VP2; X-ray; 2.70 A; A=221-533. DR PDB; 3VP3; X-ray; 2.70 A; A=221-533. DR PDB; 3VP4; X-ray; 2.45 A; A=221-533. DR PDB; 4O7D; X-ray; 2.30 A; A=221-531. DR PDB; 5D3O; X-ray; 2.79 A; A/B=72-597. DR PDB; 5FI2; X-ray; 2.50 A; A/B/C/D=72-597. DR PDB; 5FI6; X-ray; 2.52 A; A/B/C/D=72-597. DR PDB; 5FI7; X-ray; 2.50 A; A/B/C/D=72-597. DR PDB; 5HL1; X-ray; 2.40 A; A/B/C/D=72-597. DR PDB; 5I94; X-ray; 2.98 A; A/B/C/D=72-597. DR PDB; 5JYO; X-ray; 2.10 A; A/B/C/D/E/F/G/H=221-533. DR PDB; 5JYP; X-ray; 2.74 A; A=221-533. DR PDB; 5U0I; X-ray; 1.42 A; A/B=551-669. DR PDB; 5U0J; X-ray; 1.72 A; A/B/C/D=551-669. DR PDB; 5UQE; X-ray; 3.60 A; A/B/C/D/F=137-656. DR PDB; 5WJ6; X-ray; 2.44 A; A/B/C/D=72-550. DR PDB; 6LOX; X-ray; 3.20 A; A/B/C/D=71-600. DR PDB; 6UJG; X-ray; 3.00 A; A/B/C/D/E/F/G/H=72-550. DR PDB; 6UJM; X-ray; 2.50 A; A/B/C/D=72-550. DR PDB; 6UK6; X-ray; 2.90 A; A/B/C/D=72-550. DR PDB; 6UKB; X-ray; 3.00 A; A/B/C/D=72-550. DR PDB; 6UL9; X-ray; 2.50 A; A/B/C/D=72-550. DR PDB; 6ULA; X-ray; 2.95 A; A/B/C/D/E/F/G/H=72-550. DR PDB; 6ULJ; X-ray; 2.69 A; A/B/C/D=72-550. DR PDB; 6UMC; X-ray; 2.75 A; A/B/C/D=72-550. DR PDB; 6UMD; X-ray; 2.70 A; A/B/C/D=72-550. DR PDB; 6UME; X-ray; 2.90 A; A/B/C/D=72-550. DR PDB; 6UMF; X-ray; 2.68 A; A/B/C/D=72-550. DR PDB; 7REN; X-ray; 2.80 A; A/B/C/D=72-550. DR PDB; 7RGG; X-ray; 3.00 A; A/B/C/D=72-550. DR PDB; 7SBM; X-ray; 2.80 A; A/B/C/D=72-550. DR PDB; 7SBN; X-ray; 2.14 A; A/B/C/D=72-550. DR PDB; 8BSK; X-ray; 2.10 A; A=221-533. DR PDB; 8BSL; X-ray; 2.38 A; A/B/C/D=123-550. DR PDB; 8BSM; X-ray; 2.78 A; A=221-533. DR PDB; 8BSN; X-ray; 2.49 A; A=221-533. DR PDB; 8GWR; X-ray; 2.80 A; A/B=1-669. DR PDB; 8JUB; X-ray; 2.01 A; A/B/C/D=71-550. DR PDB; 8JUE; X-ray; 2.39 A; A/B/C/D=71-550. DR PDBsum; 3CZD; -. DR PDBsum; 3UNW; -. DR PDBsum; 3UO9; -. DR PDBsum; 3VOY; -. DR PDBsum; 3VOZ; -. DR PDBsum; 3VP0; -. DR PDBsum; 3VP1; -. DR PDBsum; 3VP2; -. DR PDBsum; 3VP3; -. DR PDBsum; 3VP4; -. DR PDBsum; 4O7D; -. DR PDBsum; 5D3O; -. DR PDBsum; 5FI2; -. DR PDBsum; 5FI6; -. DR PDBsum; 5FI7; -. DR PDBsum; 5HL1; -. DR PDBsum; 5I94; -. DR PDBsum; 5JYO; -. DR PDBsum; 5JYP; -. DR PDBsum; 5U0I; -. DR PDBsum; 5U0J; -. DR PDBsum; 5UQE; -. DR PDBsum; 5WJ6; -. DR PDBsum; 6LOX; -. DR PDBsum; 6UJG; -. DR PDBsum; 6UJM; -. DR PDBsum; 6UK6; -. DR PDBsum; 6UKB; -. DR PDBsum; 6UL9; -. DR PDBsum; 6ULA; -. DR PDBsum; 6ULJ; -. DR PDBsum; 6UMC; -. DR PDBsum; 6UMD; -. DR PDBsum; 6UME; -. DR PDBsum; 6UMF; -. DR PDBsum; 7REN; -. DR PDBsum; 7RGG; -. DR PDBsum; 7SBM; -. DR PDBsum; 7SBN; -. DR PDBsum; 8BSK; -. DR PDBsum; 8BSL; -. DR PDBsum; 8BSM; -. DR PDBsum; 8BSN; -. DR PDBsum; 8GWR; -. DR PDBsum; 8JUB; -. DR PDBsum; 8JUE; -. DR AlphaFoldDB; O94925; -. DR SMR; O94925; -. DR BioGRID; 109006; 220. DR DIP; DIP-50591N; -. DR IntAct; O94925; 61. DR MINT; O94925; -. DR STRING; 9606.ENSP00000317379; -. DR BindingDB; O94925; -. DR ChEMBL; CHEMBL2146302; -. DR DrugBank; DB13155; Esculin. DR DrugBank; DB00142; Glutamic acid. DR DrugBank; DB00130; L-Glutamine. DR GuidetoPHARMACOLOGY; 2891; -. DR GlyConnect; 2043; 3 N-Linked glycans (1 site). DR GlyCosmos; O94925; 1 site, 6 glycans. DR GlyGen; O94925; 2 sites, 6 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; O94925; -. DR PhosphoSitePlus; O94925; -. DR SwissPalm; O94925; -. DR BioMuta; GLS; -. DR CPTAC; CPTAC-516; -. DR CPTAC; CPTAC-517; -. DR EPD; O94925; -. DR jPOST; O94925; -. DR MassIVE; O94925; -. DR MaxQB; O94925; -. DR PaxDb; 9606-ENSP00000317379; -. DR PeptideAtlas; O94925; -. DR ProteomicsDB; 50560; -. [O94925-1] DR ProteomicsDB; 50561; -. [O94925-2] DR ProteomicsDB; 50562; -. [O94925-3] DR Pumba; O94925; -. DR TopDownProteomics; O94925-2; -. [O94925-2] DR Antibodypedia; 34041; 509 antibodies from 33 providers. DR DNASU; 2744; -. DR Ensembl; ENST00000320717.8; ENSP00000317379.3; ENSG00000115419.14. [O94925-1] DR Ensembl; ENST00000338435.9; ENSP00000340689.4; ENSG00000115419.14. [O94925-3] DR GeneID; 2744; -. DR KEGG; hsa:2744; -. DR MANE-Select; ENST00000320717.8; ENSP00000317379.3; NM_014905.5; NP_055720.3. DR UCSC; uc002use.4; human. [O94925-1] DR AGR; HGNC:4331; -. DR CTD; 2744; -. DR DisGeNET; 2744; -. DR GeneCards; GLS; -. DR HGNC; HGNC:4331; GLS. DR HPA; ENSG00000115419; Tissue enhanced (kidney). DR MalaCards; GLS; -. DR MIM; 138280; gene. DR MIM; 618328; phenotype. DR MIM; 618339; phenotype. DR MIM; 618412; phenotype. DR neXtProt; NX_O94925; -. DR OpenTargets; ENSG00000115419; -. DR Orphanet; 557064; Neonatal epileptic encephalopathy due to glutaminase deficiency. DR Orphanet; 557056; Spastic ataxia-dysarthria due to glutaminase deficiency. DR PharmGKB; PA28734; -. DR VEuPathDB; HostDB:ENSG00000115419; -. DR eggNOG; KOG0506; Eukaryota. DR GeneTree; ENSGT00390000010463; -. DR HOGENOM; CLU_016439_1_0_1; -. DR InParanoid; O94925; -. DR OMA; RWGNRPI; -. DR OrthoDB; 537490at2759; -. DR PhylomeDB; O94925; -. DR TreeFam; TF313359; -. DR BRENDA; 3.5.1.2; 2681. DR PathwayCommons; O94925; -. DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle. DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-HSA-8964539; Glutamate and glutamine metabolism. DR SABIO-RK; O94925; -. DR SignaLink; O94925; -. DR SIGNOR; O94925; -. DR BioGRID-ORCS; 2744; 39 hits in 1154 CRISPR screens. DR ChiTaRS; GLS; human. DR EvolutionaryTrace; O94925; -. DR GenomeRNAi; 2744; -. DR Pharos; O94925; Tchem. DR PRO; PR:O94925; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; O94925; Protein. DR Bgee; ENSG00000115419; Expressed in middle temporal gyrus and 203 other cell types or tissues. DR ExpressionAtlas; O94925; baseline and differential. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0004359; F:glutaminase activity; IDA:UniProtKB. DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0006537; P:glutamate biosynthetic process; IDA:UniProtKB. DR GO; GO:0006543; P:glutamine catabolic process; IDA:UniProtKB. DR GO; GO:0090461; P:intracellular glutamate homeostasis; IMP:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB. DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IEA:Ensembl. DR GO; GO:0001967; P:suckling behavior; 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:SF49; GLUTAMINASE KIDNEY 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. DR Genevisible; O94925; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ANK repeat; Cataract; KW Cytoplasm; Direct protein sequencing; Disease variant; Epilepsy; Hydrolase; KW Mitochondrion; Phosphoprotein; Reference proteome; Repeat; Transit peptide. FT TRANSIT 1..54 FT /note="Mitochondrion" FT /evidence="ECO:0000305" FT CHAIN 55..669 FT /note="Glutaminase kidney isoform, mitochondrial 68 kDa FT chain" FT /id="PRO_0000011622" FT CHAIN 73..669 FT /note="Glutaminase kidney isoform, mitochondrial 65 kDa FT chain" FT /evidence="ECO:0000250|UniProtKB:P13264" FT /id="PRO_0000447412" FT REPEAT 585..614 FT /note="ANK 1" FT REPEAT 619..648 FT /note="ANK 2" FT REGION 68..118 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 315..322 FT /note="Highly mobile activation loop" FT /evidence="ECO:0000250|UniProtKB:D3Z7P3" FT REGION 647..669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 286 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22049910, FT ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, FT ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, FT ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1" FT BINDING 335 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22049910, FT ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, FT ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, FT ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1" FT BINDING 381 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22049910, FT ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, FT ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, FT ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1" FT BINDING 388 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22049910, FT ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, FT ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, FT ECO:0007744|PDB:3VP1" FT BINDING 414 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22049910, FT ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, FT ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, FT ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1" FT BINDING 466 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22049910, FT ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, FT ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, FT ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1" FT BINDING 484 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22049910, FT ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, FT ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, FT ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1" FT SITE 72..73 FT /note="Cleavage; by MPP" FT /evidence="ECO:0000250|UniProtKB:P13264" FT MOD_RES 130 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:D3Z7P3" FT MOD_RES 164 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:D3Z7P3" FT MOD_RES 311 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 652 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P13264" FT VAR_SEQ 162..169 FT /note="ALKSTGLR -> VSFYIFLS (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_001765" FT VAR_SEQ 170..669 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_001766" FT VAR_SEQ 551..669 FT /note="VKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVV FT KFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQTV FT HKNLDGLL -> HSFGPLDYESLQQELALKETVWKKVSPESNEDISTTVVYRMESLGEK FT S (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11015561" FT /id="VSP_001767" FT VARIANT 81..669 FT /note="Missing (in DEE71)" FT /evidence="ECO:0000269|PubMed:30575854" FT /id="VAR_081971" FT VARIANT 254 FT /note="A -> P (in dbSNP:rs16833035)" FT /id="VAR_049188" FT VARIANT 272 FT /note="R -> K (in DEE71; dbSNP:rs1558972120)" FT /evidence="ECO:0000269|PubMed:30575854" FT /id="VAR_081972" FT VARIANT 313 FT /note="P -> L (in GDPAG; loss of enzyme activity; FT dbSNP:rs1558973667)" FT /evidence="ECO:0000269|PubMed:30970188" FT /id="VAR_081973" FT VARIANT 482 FT /note="S -> C (in CASGID; increased enzyme activity; FT dbSNP:rs1558986214)" FT /evidence="ECO:0000269|PubMed:30239721" FT /id="VAR_081974" FT MUTAGEN 249 FT /note="Y->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:24451979" FT MUTAGEN 286 FT /note="S->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:24451979" FT MUTAGEN 289 FT /note="K->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:24451979" FT MUTAGEN 318 FT /note="F->Y: No effect on catalytic activity. Loss of FT inhibition by BPTES; when associated with S-322." FT /evidence="ECO:0000269|PubMed:22049910" FT MUTAGEN 321 FT /note="L->A: Decreased enzyme activity." FT /evidence="ECO:0000269|PubMed:22538822" FT MUTAGEN 322 FT /note="F->S: No effect on catalytic activity. Loss of FT inhibition by BPTES; when associated with Y-318." FT /evidence="ECO:0000269|PubMed:22049910" FT MUTAGEN 323 FT /note="L->A: Decreased enzyme activity." FT /evidence="ECO:0000269|PubMed:22538822" FT MUTAGEN 394 FT /note="Y->A: Decreased enzyme activity." FT /evidence="ECO:0000269|PubMed:22538822" FT MUTAGEN 394 FT /note="Y->L: No effect on catalytic activity. Loss of FT inhibition by BPTES." FT /evidence="ECO:0000269|PubMed:22049910" FT MUTAGEN 466 FT /note="Y->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:24451979" FT CONFLICT 6 FT /note="G -> S (in Ref. 1; AAF00090)" FT /evidence="ECO:0000305" FT CONFLICT 66 FT /note="E -> D (in Ref. 1; AAF00090)" FT /evidence="ECO:0000305" FT CONFLICT 219 FT /note="F -> L (in Ref. 4; AAG47842)" FT /evidence="ECO:0000305" FT CONFLICT 268 FT /note="V -> A (in Ref. 1; AAD47056)" FT /evidence="ECO:0000305" FT HELIX 140..147 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:7SBN" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:5D3O" FT HELIX 156..165 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 176..187 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 189..191 FT /evidence="ECO:0007829|PDB:7SBN" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:5WJ6" FT HELIX 197..204 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 208..215 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 219..223 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 224..239 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:5JYO" FT HELIX 251..254 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 262..267 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 272..277 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 285..288 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 289..300 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 302..308 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 315..317 FT /evidence="ECO:0007829|PDB:3VOY" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:5WJ6" FT STRAND 327..330 FT /evidence="ECO:0007829|PDB:6UMF" FT HELIX 335..342 FT /evidence="ECO:0007829|PDB:8JUB" FT TURN 343..348 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 351..365 FT /evidence="ECO:0007829|PDB:8JUB" FT TURN 366..368 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 371..373 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 375..383 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 386..397 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 407..418 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 420..422 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 424..435 FT /evidence="ECO:0007829|PDB:8JUB" FT TURN 436..438 FT /evidence="ECO:0007829|PDB:8JUB" FT TURN 441..443 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 450..463 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 466..468 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 469..475 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 486..492 FT /evidence="ECO:0007829|PDB:8JUB" FT TURN 493..495 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 496..501 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 503..505 FT /evidence="ECO:0007829|PDB:5JYO" FT STRAND 509..511 FT /evidence="ECO:0007829|PDB:8JUB" FT HELIX 512..524 FT /evidence="ECO:0007829|PDB:8JUB" FT STRAND 533..535 FT /evidence="ECO:0007829|PDB:6LOX" FT HELIX 548..553 FT /evidence="ECO:0007829|PDB:8GWR" FT HELIX 554..563 FT /evidence="ECO:0007829|PDB:5U0I" FT HELIX 566..574 FT /evidence="ECO:0007829|PDB:5U0I" FT HELIX 589..596 FT /evidence="ECO:0007829|PDB:5U0I" FT HELIX 599..607 FT /evidence="ECO:0007829|PDB:5U0I" FT HELIX 623..629 FT /evidence="ECO:0007829|PDB:5U0I" FT HELIX 633..640 FT /evidence="ECO:0007829|PDB:5U0I" SQ SEQUENCE 669 AA; 73461 MW; 4E5E63505E84E0B7 CRC64; MMRLRGSGML RDLLLRSPAG VSATLRRAQP LVTLCRRPRG GGRPAAGPAA AARLHPWWGG GGWPAEPLAR GLSSSPSEIL QELGKGSTHP QPGVSPPAAP AAPGPKDGPG ETDAFGNSEG KELVASGENK IKQGLLPSLE DLLFYTIAEG QEKIPVHKFI TALKSTGLRT SDPRLKECMD MLRLTLQTTS DGVMLDKDLF KKCVQSNIVL LTQAFRRKFV IPDFMSFTSH IDELYESAKK QSGGKVADYI PQLAKFSPDL WGVSVCTVDG QRHSTGDTKV PFCLQSCVKP LKYAIAVNDL GTEYVHRYVG KEPSGLRFNK LFLNEDDKPH NPMVNAGAIV VTSLIKQGVN NAEKFDYVMQ FLNKMAGNEY VGFSNATFQS ERESGDRNFA IGYYLKEKKC FPEGTDMVGI LDFYFQLCSI EVTCESASVM AATLANGGFC PITGERVLSP EAVRNTLSLM HSCGMYDFSG QFAFHVGLPA KSGVAGGILL VVPNVMGMMC WSPPLDKMGN SVKGIHFCHD LVSLCNFHNY DNLRHFAKKL DPRREGGDQR VKSVINLLFA AYTGDVSALR RFALSAMDME QRDYDSRTAL HVAAAEGHVE VVKFLLEACK VNPFPKDRWN NTPMDEALHF GHHDVFKILQ EYQVQYTPQG DSDNGKENQT VHKNLDGLL //