ID GLSL_HUMAN Reviewed; 602 AA. AC Q9UI32; B7Z8Q9; Q8IX91; Q9NYY2; Q9UI31; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 2. DT 27-MAR-2024, entry version 202. 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 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 1), AND TISSUE SPECIFICITY. RC TISSUE=Brain, and Mammary cancer; RX PubMed=10620514; DOI=10.1042/bj3450365; RA Gomez-Fabre P.M., Aledo J.C., del Castillo-Olivares A., Alonso F.J., RA Nunez de Castro I., Campos J.A., Marquez J.; RT "Molecular cloning, sequencing and expression studies of the human breast RT cancer cell glutaminase."; RL Biochem. J. 345:365-375(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Brain, and Mammary cancer; RX PubMed=12444921; DOI=10.1042/bj20021445; RA Perez-Gomez C., Mates J.M., Gomez-Fabre P.M., del Castillo-Olivares A., RA Alonso F.J., Marquez J.; RT "Genomic organization and transcriptional analysis of the human l- RT glutaminase gene."; RL Biochem. J. 370:771-784(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-581. 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 [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Liver; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP INTERACTION WITH SNTA1 AND TAX1BP3. RX PubMed=11163757; DOI=10.1016/s0014-5793(00)02373-5; RA Olalla L., Aledo J.C., Bannenberg G., Marquez J.; RT "The C-terminus of human glutaminase L mediates association with PDZ RT domain-containing proteins."; RL FEBS Lett. 488:116-122(2001). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=20378837; DOI=10.1073/pnas.1001006107; RA Hu W., Zhang C., Wu R., Sun Y., Levine A., Feng Z.; RT "Glutaminase 2, a novel p53 target gene regulating energy metabolism and RT antioxidant function."; RL Proc. Natl. Acad. Sci. U.S.A. 107:7455-7460(2010). RN [9] 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 [10] {ECO:0007744|PDB:4BQM} RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 154-479. RA Ferreira I.M., Vollmar M., Krojer T., Strain-Damerell C., Froese S., RA Coutandin D., Williams E., Burgess-Brown N., von Delft F., Arrowsmith C.H., RA Bountra C., Edwards A., Dias S.M.G., Ambrosio A.L.B., Yue W.W.; RT "Crystal Structure of Human Liver-Type Glutaminase, Catalytic Domain."; RL Submitted (MAY-2013) to the PDB data bank. RN [11] {ECO:0007744|PDB:5U0K} RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 485-602, ANK REPEATS, AND RP 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). 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:0000269|PubMed:20378837}. 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 (Probable). Does not assemble CC into higher oligomers (By similarity). Interacts with the PDZ domain of CC the syntrophin SNTA1. Interacts with the PDZ domain of TAX1BP3 CC (PubMed:11163757). {ECO:0000250|UniProtKB:Q571F8, CC ECO:0000269|PubMed:11163757, ECO:0000305|PubMed:28526749}. CC -!- INTERACTION: CC Q9UI32; O00291: HIP1; NbExp=3; IntAct=EBI-3938654, EBI-473886; CC Q9UI32; Q6GPH4: XAF1; NbExp=3; IntAct=EBI-3938654, EBI-2815120; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20378837}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UI32-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UI32-2; Sequence=VSP_057009, VSP_057010; CC -!- TISSUE SPECIFICITY: Highly expressed in liver. Expressed in brain and CC pancreas. Not observed in heart, placenta, lung, skeletal muscle and CC kidney. Expression is significantly reduced in hepatocellular CC carcinomas. {ECO:0000269|PubMed:10620514, ECO:0000269|PubMed:20378837}. CC -!- INDUCTION: Up-regulated by P53 (at protein and mRNA level) under both CC stressed and non-stressed conditions. {ECO:0000269|PubMed:20378837}. CC -!- SIMILARITY: Belongs to the glutaminase family. {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; AF110330; AAF21933.1; -; mRNA. DR EMBL; AF110331; AAF21934.1; -; mRNA. DR EMBL; AF348119; AAO13298.2; -; Genomic_DNA. DR EMBL; AF223944; AAF33826.1; -; mRNA. DR EMBL; AK303772; BAH14045.1; -; mRNA. DR EMBL; AC097104; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW96943.1; -; Genomic_DNA. DR CCDS; CCDS8921.1; -. [Q9UI32-1] DR RefSeq; NP_001267727.1; NM_001280798.1. DR RefSeq; NP_037399.2; NM_013267.3. [Q9UI32-1] DR PDB; 4BQM; X-ray; 2.18 A; A/B=154-479. DR PDB; 5U0K; X-ray; 2.55 A; A/B/C/D/E/F/G/H/I/J=485-602. DR PDBsum; 4BQM; -. DR PDBsum; 5U0K; -. DR AlphaFoldDB; Q9UI32; -. DR SMR; Q9UI32; -. DR BioGRID; 118044; 20. DR IntAct; Q9UI32; 3. DR STRING; 9606.ENSP00000310447; -. DR BindingDB; Q9UI32; -. DR ChEMBL; CHEMBL4105730; -. DR DrugBank; DB11118; Ammonia. DR DrugBank; DB00142; Glutamic acid. DR DrugBank; DB00130; L-Glutamine. DR iPTMnet; Q9UI32; -. DR PhosphoSitePlus; Q9UI32; -. DR BioMuta; GLS2; -. DR DMDM; 145559477; -. DR EPD; Q9UI32; -. DR jPOST; Q9UI32; -. DR MassIVE; Q9UI32; -. DR MaxQB; Q9UI32; -. DR PaxDb; 9606-ENSP00000310447; -. DR PeptideAtlas; Q9UI32; -. DR ProteomicsDB; 6970; -. DR ProteomicsDB; 84460; -. [Q9UI32-1] DR Antibodypedia; 28236; 345 antibodies from 30 providers. DR DNASU; 27165; -. DR Ensembl; ENST00000311966.9; ENSP00000310447.4; ENSG00000135423.13. [Q9UI32-1] DR Ensembl; ENST00000486896.5; ENSP00000419661.1; ENSG00000135423.13. [Q9UI32-2] DR GeneID; 27165; -. DR KEGG; hsa:27165; -. DR MANE-Select; ENST00000311966.9; ENSP00000310447.4; NM_013267.4; NP_037399.2. DR UCSC; uc001slj.5; human. [Q9UI32-1] DR AGR; HGNC:29570; -. DR CTD; 27165; -. DR DisGeNET; 27165; -. DR GeneCards; GLS2; -. DR HGNC; HGNC:29570; GLS2. DR HPA; ENSG00000135423; Tissue enriched (liver). DR MIM; 606365; gene. DR neXtProt; NX_Q9UI32; -. DR OpenTargets; ENSG00000135423; -. DR PharmGKB; PA134933506; -. DR VEuPathDB; HostDB:ENSG00000135423; -. DR eggNOG; KOG0506; Eukaryota. DR GeneTree; ENSGT00390000010463; -. DR HOGENOM; CLU_016439_1_0_1; -. DR InParanoid; Q9UI32; -. DR OMA; CISARPC; -. DR OrthoDB; 537490at2759; -. DR PhylomeDB; Q9UI32; -. DR TreeFam; TF313359; -. DR PathwayCommons; Q9UI32; -. 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; Q9UI32; -. DR SignaLink; Q9UI32; -. DR SIGNOR; Q9UI32; -. DR BioGRID-ORCS; 27165; 21 hits in 1151 CRISPR screens. DR ChiTaRS; GLS2; human. DR GenomeRNAi; 27165; -. DR Pharos; Q9UI32; Tchem. DR PRO; PR:Q9UI32; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9UI32; Protein. DR Bgee; ENSG00000135423; Expressed in right lobe of liver and 143 other cell types or tissues. DR ExpressionAtlas; Q9UI32; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004359; F:glutaminase activity; IBA:GO_Central. DR GO; GO:0006520; P:amino acid metabolic process; TAS:ProtInc. 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; IMP:MGI. DR GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI. 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. DR Genevisible; Q9UI32; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ANK repeat; Hydrolase; KW Mitochondrion; 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_0000011625" FT REPEAT 518..547 FT /note="ANK 1" FT /evidence="ECO:0000255" FT REPEAT 552..581 FT /note="ANK 2" FT /evidence="ECO:0000255" FT REGION 1..67 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 53..67 FT /note="Basic and acidic 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 136..209 FT /note="CVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDVKELTGGKVAAYIPQLA FT KSNPDLWGVSLCTVDGQRHSVG -> HSERSLSFLILRSSRAMWIASLRMSKSSLEAKW FT QPTSLSWPSQTQTCGVSPCALWMVNGTLWATQRSPSACSPV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057009" FT VAR_SEQ 210..602 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057010" FT VARIANT 581 FT /note="L -> P (in dbSNP:rs2657879)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_031615" FT CONFLICT 87 FT /note="I -> T (in Ref. 1; AAF21933)" FT /evidence="ECO:0000305" FT CONFLICT 140 FT /note="N -> S (in Ref. 1; AAF21933)" FT /evidence="ECO:0000305" FT CONFLICT 257 FT /note="N -> D (in Ref. 1; AAF21933)" FT /evidence="ECO:0000305" FT CONFLICT 328..329 FT /note="LK -> HE (in Ref. 1; AAF21933)" FT /evidence="ECO:0000305" FT CONFLICT 560 FT /note="A -> V (in Ref. 3; AAF33826)" FT /evidence="ECO:0000305" FT HELIX 157..171 FT /evidence="ECO:0007829|PDB:4BQM" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:4BQM" FT STRAND 195..200 FT /evidence="ECO:0007829|PDB:4BQM" FT STRAND 205..210 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 218..221 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 222..233 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 235..238 FT /evidence="ECO:0007829|PDB:4BQM" FT TURN 239..241 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 268..277 FT /evidence="ECO:0007829|PDB:4BQM" FT TURN 278..281 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 284..298 FT /evidence="ECO:0007829|PDB:4BQM" FT TURN 299..301 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 308..317 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 319..330 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 340..351 FT /evidence="ECO:0007829|PDB:4BQM" FT STRAND 353..355 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 357..368 FT /evidence="ECO:0007829|PDB:4BQM" FT TURN 369..371 FT /evidence="ECO:0007829|PDB:4BQM" FT TURN 374..376 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 383..396 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 399..401 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 402..408 FT /evidence="ECO:0007829|PDB:4BQM" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:4BQM" FT STRAND 419..425 FT /evidence="ECO:0007829|PDB:4BQM" FT TURN 426..428 FT /evidence="ECO:0007829|PDB:4BQM" FT STRAND 429..434 FT /evidence="ECO:0007829|PDB:4BQM" FT STRAND 442..444 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 445..458 FT /evidence="ECO:0007829|PDB:4BQM" FT HELIX 485..496 FT /evidence="ECO:0007829|PDB:5U0K" FT HELIX 499..506 FT /evidence="ECO:0007829|PDB:5U0K" FT TURN 507..509 FT /evidence="ECO:0007829|PDB:5U0K" FT HELIX 522..529 FT /evidence="ECO:0007829|PDB:5U0K" FT HELIX 532..540 FT /evidence="ECO:0007829|PDB:5U0K" FT HELIX 556..562 FT /evidence="ECO:0007829|PDB:5U0K" FT HELIX 566..578 FT /evidence="ECO:0007829|PDB:5U0K" SQ SEQUENCE 602 AA; 66323 MW; 6D0E1EFF01BC3843 CRC64; MRSMKALQKA LSRAGSHCGR GGWGHPSRSP LLGGGVRHHL SEAAAQGRET PHSHQPQHQD HDSSESGMLS RLGDLLFYTI AEGQERIPIH KFTTALKATG LQTSDPRLRD CMSEMHRVVQ ESSSGGLLDR DLFRKCVSSN IVLLTQAFRK KFVIPDFEEF TGHVDRIFED VKELTGGKVA AYIPQLAKSN PDLWGVSLCT VDGQRHSVGH TKIPFCLQSC VKPLTYAISI STLGTDYVHK FVGKEPSGLR YNKLSLNEEG IPHNPMVNAG AIVVSSLIKM DCNKAEKFDF VLQYLNKMAG NEYMGFSNAT FQSEKETGDR NYAIGYYLKE KKCFPKGVDM MAALDLYFQL CSVEVTCESG SVMAATLANG GICPITGESV LSAEAVRNTL SLMHSCGMYD FSGQFAFHVG LPAKSAVSGA ILLVVPNVMG MMCLSPPLDK LGNSHRGTSF CQKLVSLFNF HNYDNLRHCA RKLDPRREGA EIRNKTVVNL LFAAYSGDVS ALRRFALSAM DMEQKDYDSR TALHVAAAEG HIEVVKFLIE ACKVNPFAKD RWGNIPLDDA VQFNHLEVVK LLQDYQDSYT LSETQAEAAA EALSKENLES MV //