ID GABT_HUMAN Reviewed; 500 AA. AC P80404; A8K386; Q16260; Q8N5W2; Q96BG2; Q99800; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 3. DT 02-SEP-2026, entry version 217. DE RecName: Full=4-aminobutyrate aminotransferase, mitochondrial; DE EC=2.6.1.19 {ECO:0000269|PubMed:10407778, ECO:0000269|PubMed:15528998}; DE AltName: Full=(S)-3-amino-2-methylpropionate transaminase; DE EC=2.6.1.22 {ECO:0000250|UniProtKB:P50554}; DE AltName: Full=GABA aminotransferase; DE Short=GABA-AT; DE AltName: Full=Gamma-amino-N-butyrate transaminase; DE Short=GABA transaminase; DE Short=GABA-T; DE AltName: Full=L-AIBAT; DE Flags: Precursor; GN Name=ABAT {ECO:0000312|HGNC:HGNC:23}; Synonyms=GABAT; 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]. RC TISSUE=Brain; RX PubMed=7721088; DOI=10.1016/0378-1119(94)00858-p; RA Osei Y.D., Churchich J.E.; RT "Screening and sequence determination of a cDNA encoding the human brain 4- RT aminobutyrate aminotransferase."; RL Gene 155:185-187(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pancreatic islet; RA Medina-Kauwe L.K., Gibson K.M., Nyhan W.L., Tobin A.J.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-56. RC TISSUE=Brain, and Eye; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-485, PARTIAL PROTEIN SEQUENCE, AND TISSUE RP SPECIFICITY. RC TISSUE=Liver; RX PubMed=7851425; DOI=10.1111/j.1432-1033.1995.tb20412.x; RA de Biase D., Barra D., Simmaco M., John R.A., Bossa F.; RT "Primary structure and tissue distribution of human 4-aminobutyrate RT aminotransferase."; RL Eur. J. Biochem. 227:476-480(1995). RN [6] RP SUBUNIT, INTERCHAIN DISULFIDE BOND, MUTAGENESIS OF CYS-321, CATALYTIC RP ACTIVITY, AND FUNCTION. RX PubMed=15528998; DOI=10.1016/s1016-8478(23)13104-9; RA Yoon C.S., Kim D.W., Jang S.H., Lee B.R., Choi H.S., Choi S.H., Kim S.Y., RA An J.J., Kwon O.S., Kang T.C., Won M.H., Cho S.W., Lee K.S., Park J., RA Eum W.S., Choi S.Y.; RT "Cysteine-321 of human brain GABA transaminase is involved in intersubunit RT cross-linking."; RL Mol. Cells 18:214-219(2004). RN [7] 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 [8] 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 [9] RP VARIANT GABATD LYS-220, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=10407778; DOI=10.1023/a:1005500122231; RA Medina-Kauwe L.K., Tobin A.J., De Meirleir L., Jaeken J., Jakobs C., RA Nyhan W.L., Gibson K.M.; RT "4-aminobutyrate aminotransferase (GABA-transaminase) deficiency."; RL J. Inherit. Metab. Dis. 22:414-427(1999). CC -!- FUNCTION: Catalyzes the conversion of gamma-aminobutyrate and L-beta- CC aminoisobutyrate to succinate semialdehyde and methylmalonate CC semialdehyde, respectively (PubMed:10407778, PubMed:15528998). Can also CC convert delta-aminovalerate and beta-alanine (By similarity). CC {ECO:0000250|UniProtKB:P50554, ECO:0000269|PubMed:10407778, CC ECO:0000269|PubMed:15528998}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + CC L-glutamate; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19; CC Evidence={ECO:0000269|PubMed:10407778, ECO:0000269|PubMed:15528998}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23353; CC Evidence={ECO:0000269|PubMed:10407778, ECO:0000305|PubMed:15528998}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3- CC oxopropanoate + L-glutamate; Xref=Rhea:RHEA:13993, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57700, ChEBI:CHEBI:58655; EC=2.6.1.22; CC Evidence={ECO:0000250|UniProtKB:P50554}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13994; CC Evidence={ECO:0000250|UniProtKB:P50554}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250|UniProtKB:P80147}; CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000250|UniProtKB:P80147}; CC Note=Binds 1 [2Fe-2S] cluster per homodimer. CC {ECO:0000250|UniProtKB:P80147}; CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:15528998}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- TISSUE SPECIFICITY: Liver > pancreas > brain > kidney > heart > CC placenta. {ECO:0000269|PubMed:7851425}. CC -!- DISEASE: GABA-transaminase deficiency (GABATD) [MIM:613163]: An CC enzymatic deficiency resulting in psychomotor retardation, hypotonia, CC hyperreflexia, lethargy, refractory seizures, and EEG abnormalities. CC GABATD inheritance is autosomal recessive. CC {ECO:0000269|PubMed:10407778}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase 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; L32961; AAA74449.1; -; mRNA. DR EMBL; U80226; AAB38510.1; -; mRNA. DR EMBL; AK290501; BAF83190.1; -; mRNA. DR EMBL; BC015628; AAH15628.1; -; mRNA. DR EMBL; BC031413; AAH31413.1; -; mRNA. DR EMBL; S75578; AAD14176.1; -; mRNA. DR CCDS; CCDS10534.1; -. DR PIR; JC4022; JC4022. DR PIR; S67470; S67470. DR RefSeq; NP_000654.2; NM_000663.5. DR RefSeq; NP_001120920.1; NM_001127448.2. DR RefSeq; NP_001373529.1; NM_001386600.1. DR RefSeq; NP_001373530.1; NM_001386601.1. DR RefSeq; NP_001373531.1; NM_001386602.1. DR RefSeq; NP_001373532.1; NM_001386603.1. DR RefSeq; NP_001373533.1; NM_001386604.1. DR RefSeq; NP_065737.2; NM_020686.6. DR RefSeq; XP_047289641.1; XM_047433685.1. DR RefSeq; XP_047289642.1; XM_047433686.1. DR RefSeq; XP_047289643.1; XM_047433687.1. DR RefSeq; XP_047289644.1; XM_047433688.1. DR RefSeq; XP_054235700.1; XM_054379725.1. DR RefSeq; XP_054235701.1; XM_054379726.1. DR RefSeq; XP_054235702.1; XM_054379727.1. DR RefSeq; XP_054235703.1; XM_054379728.1. DR AlphaFoldDB; P80404; -. DR SMR; P80404; -. DR BioGRID; 106536; 77. DR CORUM; P80404; -. DR FunCoup; P80404; 818. DR IntAct; P80404; 13. DR MINT; P80404; -. DR NDEx; IQUERY-CP-ABAT; 7 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000379845; -. DR BindingDB; P80404; -. DR ChEMBL; CHEMBL2044; -. DR DrugBank; DB01699; (4e)-4-Aminohex-4-Enoic Acid. DR DrugBank; DB04235; 4-Amino Hexanoic Acid. DR DrugBank; DB14511; Acetate. DR DrugBank; DB00160; Alanine. DR DrugBank; DB17919; CPP-115 free base. DR DrugBank; DB00142; Glutamic acid. DR DrugBank; DB08849; Nipecotic acid. DR DrugBank; DB03940; Oxamic Acid. DR DrugBank; DB03560; P-Hydroxybenzaldehyde. DR DrugBank; DB00780; Phenelzine. DR DrugBank; DB00114; Pyridoxal phosphate. DR DrugBank; DB00119; Pyruvic acid. DR DrugBank; DB00313; Valproic acid. DR DrugBank; DB01080; Vigabatrin. DR DrugCentral; P80404; -. DR GuidetoPHARMACOLOGY; 2464; -. DR iPTMnet; P80404; -. DR PhosphoSitePlus; P80404; -. DR SwissPalm; P80404; -. DR BioMuta; ABAT; -. DR DMDM; 48429239; -. DR CPTAC; CPTAC-3; -. DR CPTAC; CPTAC-4; -. DR jPOST; P80404; -. DR MassIVE; P80404; -. DR PaxDb; 9606-ENSP00000379845; -. DR PeptideAtlas; P80404; -. DR ProteomicsDB; 57683; -. DR Pumba; P80404; -. DR Antibodypedia; 24533; 408 antibodies from 33 providers. DR DNASU; 18; -. DR Ensembl; ENST00000268251.13; ENSP00000268251.8; ENSG00000183044.13. DR Ensembl; ENST00000396600.6; ENSP00000379845.2; ENSG00000183044.13. DR Ensembl; ENST00000425191.6; ENSP00000411916.2; ENSG00000183044.13. DR Ensembl; ENST00000909342.1; ENSP00000579401.1; ENSG00000183044.13. DR Ensembl; ENST00000909343.1; ENSP00000579402.1; ENSG00000183044.13. DR GeneID; 18; -. DR KEGG; hsa:18; -. DR MANE-Select; ENST00000268251.13; ENSP00000268251.8; NM_020686.6; NP_065737.2. DR AGR; HGNC:23; -. DR ClinPGx; PA24372; -. DR CTD; 18; -. DR DisGeNET; 18; -. DR GeneCards; ABAT; -. DR HGNC; HGNC:23; ABAT. DR HPA; ENSG00000183044; Tissue enhanced (brain, kidney, liver, pancreas). DR MalaCards; ABAT; -. DR MIM; 137150; gene. DR MIM; 613163; phenotype. DR OpenTargets; ENSG00000183044; -. DR Orphanet; 2066; Gamma-aminobutyric acid transaminase deficiency. DR VEuPathDB; HostDB:ENSG00000183044; -. DR eggNOG; KOG1405; Eukaryota. DR GeneTree; ENSGT00550000074885; -. DR HOGENOM; CLU_016922_12_1_1; -. DR InParanoid; P80404; -. DR OMA; GLMCAFD; -. DR OrthoDB; 5419315at2759; -. DR PAN-GO; P80404; 3 GO annotations based on evolutionary models. DR PhylomeDB; P80404; -. DR BioCyc; MetaCyc:HS02477-MONOMER; -. DR BRENDA; 2.6.1.19; 2681. DR PathwayCommons; P80404; -. DR Reactome; R-HSA-916853; Degradation of GABA. DR SABIO-RK; P80404; -. DR SignaLink; P80404; -. DR Agora; ENSG00000183044; -. DR BioGRID-ORCS; 18; 10 hits in 1162 CRISPR screens. DR ChiTaRS; ABAT; human. DR GenomeRNAi; 18; -. DR Pharos; P80404; Tclin. DR PRO; PR:P80404; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P80404; protein. DR Bgee; ENSG00000183044; Expressed in Brodmann (1909) area 23 and 201 other cell types or tissues. DR ExpressionAtlas; P80404; baseline and differential. DR GO; GO:0032144; C:4-aminobutyrate transaminase complex; IDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb. DR GO; GO:0047298; F:(S)-3-amino-2-methylpropionate:2-oxoglutarate transaminase activity; ISS:UniProtKB. DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IDA:FlyBase. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB. DR GO; GO:0032145; F:succinate-semialdehyde dehydrogenase binding; ISS:UniProtKB. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0007620; P:copulation; IEA:Ensembl. DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl. DR GO; GO:0009450; P:GABA catabolic process; IBA:GO_Central. DR GO; GO:0006540; P:GABA shunt; IDA:UniProtKB. DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl. DR GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl. DR GO; GO:0033602; P:negative regulation of dopamine secretion; IEA:Ensembl. DR GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; IEA:Ensembl. DR GO; GO:0050877; P:nervous system process; ISS:UniProtKB. DR GO; GO:1904450; P:positive regulation of aspartate secretion; IEA:Ensembl. DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; IEA:Ensembl. DR GO; GO:0031652; P:positive regulation of heat generation; IEA:Ensembl. DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; IEA:Ensembl. DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl. DR GO; GO:1902722; P:positive regulation of prolactin secretion; IEA:Ensembl. DR GO; GO:0070474; P:positive regulation of uterine smooth muscle contraction; IEA:Ensembl. DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0010039; P:response to iron ion; IEA:Ensembl. DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR CDD; cd00610; OAT_like; 1. DR FunFam; 3.40.640.10:FF:000029; 4-aminobutyrate aminotransferase, mitochondrial; 1. DR FunFam; 3.90.1150.10:FF:000191; 4-aminobutyrate aminotransferase, mitochondrial; 2. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR004631; 4NH2But_aminotransferase_euk. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR00699; GABAtrns_euk; 1. DR PANTHER; PTHR43206:SF1; 4-AMINOBUTYRATE AMINOTRANSFERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43206; AMINOTRANSFERASE; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 1: Evidence at protein level; KW Acetylation; Aminotransferase; Direct protein sequencing; Disease variant; KW Disulfide bond; Iron; Iron-sulfur; Metal-binding; Mitochondrion; KW Neurotransmitter degradation; Proteomics identification; KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. FT TRANSIT 1..28 FT /note="Mitochondrion" FT CHAIN 29..500 FT /note="4-aminobutyrate aminotransferase, mitochondrial" FT /id="PRO_0000001249" FT BINDING 163 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P80147" FT BINDING 164..165 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P80147" FT BINDING 166 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P80147" FT BINDING 220 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P80147" FT BINDING 381 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P80147" FT MOD_RES 231 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P61922" FT MOD_RES 252 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P61922" FT MOD_RES 252 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P61922" FT MOD_RES 279 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P61922" FT MOD_RES 318 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P61922" FT MOD_RES 357 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250|UniProtKB:P80147" FT MOD_RES 413 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P61922" FT MOD_RES 413 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P61922" FT MOD_RES 452 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P61922" FT MOD_RES 470 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P61922" FT DISULFID 321 FT /note="Interchain" FT VARIANT 56 FT /note="Q -> R (in dbSNP:rs1731017)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_018979" FT VARIANT 220 FT /note="R -> K (in GABATD; 25% reduction in 4-aminobutyrate FT aminotransferase activity; dbSNP:rs121434578)" FT /evidence="ECO:0000269|PubMed:10407778" FT /id="VAR_008883" FT MUTAGEN 321 FT /note="C->M,S,A,G,K: Loss of 4-aminobutyrate FT aminotransferase activity." FT /evidence="ECO:0000269|PubMed:15528998" FT CONFLICT 17 FT /note="S -> T (in Ref. 1; AAA74449)" FT /evidence="ECO:0000305" FT CONFLICT 109 FT /note="H -> D (in Ref. 1; AAA74449)" FT /evidence="ECO:0000305" FT CONFLICT 113 FT /note="L -> V (in Ref. 1; AAA74449)" FT /evidence="ECO:0000305" FT CONFLICT 132 FT /note="G -> E (in Ref. 1; AAA74449)" FT /evidence="ECO:0000305" FT CONFLICT 155..171 FT /note="MSQLITMACGSCSNENA -> CPSSSPWPACPAPMKTT (in Ref. 2; FT AAB38510)" FT /evidence="ECO:0000305" FT CONFLICT 191 FT /note="Q -> K (in Ref. 1; AAA74449)" FT /evidence="ECO:0000305" FT CONFLICT 204 FT /note="G -> W (in Ref. 1; AAA74449)" FT /evidence="ECO:0000305" FT CONFLICT 216 FT /note="A -> S (in Ref. 1; AAA74449)" FT /evidence="ECO:0000305" FT CONFLICT 247 FT /note="P -> T (in Ref. 2; AAB38510)" FT /evidence="ECO:0000305" FT CONFLICT 268 FT /note="R -> G (in Ref. 1; AAA74449)" FT /evidence="ECO:0000305" FT CONFLICT 320 FT /note="G -> C (in Ref. 1; AAA74449)" FT /evidence="ECO:0000305" FT CONFLICT 366 FT /note="H -> L (in Ref. 1; AAA74449)" FT /evidence="ECO:0000305" SQ SEQUENCE 500 AA; 56439 MW; F990B0B6B77BD3F5 CRC64; MASMLLAQRL ACSFQHSYRL LVPGSRHISQ AAAKVDVEFD YDGPLMKTEV PGPRSQELMK QLNIIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSVPIGYSHP ALLKLIQQPQ NASMFVNRPA LGILPPENFV EKLRQSLLSV APKGMSQLIT MACGSCSNEN ALKTIFMWYR SKERGQRGFS QEELETCMIN QAPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS FDWPIAPFPR LKYPLEEFVK ENQQEEARCL EEVEDLIVKY RKKKKTVAGI IVEPIQSEGG DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA DVMTFSKKMM TGGFFHKEEF RPNAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLNNAAH AGKALLTGLL DLQARYPQFI SRVRGRGTFC SFDTPDDSIR NKLILIARNK GVVLGGCGDK SIRFRPTLVF RDHHAHLFLN IFSDILADFK //