GABT_HUMAN
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 03-AUG-2022, entry version 198.
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;
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=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate
CC semialdehyde; 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 {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}.
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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_000663.4.
DR RefSeq; NP_001120920.1; NM_001127448.1.
DR RefSeq; NP_065737.2; NM_020686.5.
DR RefSeq; XP_011520702.1; XM_011522400.2.
DR RefSeq; XP_011520703.1; XM_011522401.2.
DR AlphaFoldDB; P80404; -.
DR SMR; P80404; -.
DR BioGRID; 106536; 52.
DR IntAct; P80404; 6.
DR MINT; P80404; -.
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; DB00160; Alanine.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00780; Phenelzine.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugBank; DB00119; Pyruvic 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 EPD; P80404; -.
DR jPOST; P80404; -.
DR MassIVE; P80404; -.
DR PaxDb; P80404; -.
DR PeptideAtlas; P80404; -.
DR PRIDE; P80404; -.
DR ProteomicsDB; 57683; -.
DR Antibodypedia; 24533; 378 antibodies from 30 providers.
DR DNASU; 18; -.
DR Ensembl; ENST00000268251.13; ENSP00000268251.8; ENSG00000183044.12.
DR Ensembl; ENST00000396600.6; ENSP00000379845.2; ENSG00000183044.12.
DR Ensembl; ENST00000425191.6; ENSP00000411916.2; ENSG00000183044.12.
DR GeneID; 18; -.
DR KEGG; hsa:18; -.
DR MANE-Select; ENST00000268251.13; ENSP00000268251.8; NM_020686.6; NP_065737.2.
DR CTD; 18; -.
DR DisGeNET; 18; -.
DR GeneCards; ABAT; -.
DR HGNC; HGNC:23; ABAT.
DR HPA; ENSG00000183044; Tissue enhanced (kidney, liver, pancreas).
DR MalaCards; ABAT; -.
DR MIM; 137150; gene.
DR MIM; 613163; phenotype.
DR neXtProt; NX_P80404; -.
DR OpenTargets; ENSG00000183044; -.
DR Orphanet; 2066; Gamma-aminobutyric acid transaminase deficiency.
DR PharmGKB; PA24372; -.
DR VEuPathDB; HostDB:ENSG00000183044; -.
DR eggNOG; KOG1405; Eukaryota.
DR GeneTree; ENSGT00550000074885; -.
DR HOGENOM; CLU_016922_12_1_1; -.
DR InParanoid; P80404; -.
DR OMA; DPPDMVT; -.
DR OrthoDB; 81952at2759; -.
DR PhylomeDB; P80404; -.
DR TreeFam; TF105021; -.
DR BioCyc; MetaCyc:HS02477-MON; -.
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 BioGRID-ORCS; 18; 7 hits in 1076 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 199 other tissues.
DR ExpressionAtlas; P80404; baseline and differential.
DR Genevisible; P80404; HS.
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:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0032145; F:succinate-semialdehyde dehydrogenase binding; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0048148; P:behavioral response to cocaine; 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:0009449; P:gamma-aminobutyric acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; 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:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl.
DR GO; GO:0042135; P:neurotransmitter catabolic process; NAS: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: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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004631; 4NH2But_aminotransferase_euk.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00699; GABAtrns_euk; 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; Pyridoxal phosphate; Reference proteome;
KW 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
