GenomeNet

Database: UniProt/SWISS-PROT
Entry: GABT_HUMAN
LinkDB: GABT_HUMAN
Original site: 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   05-DEC-2018, entry version 178.
DE   RecName: Full=4-aminobutyrate aminotransferase, mitochondrial;
DE            EC=2.6.1.19;
DE   AltName: Full=(S)-3-amino-2-methylpropionate transaminase;
DE            EC=2.6.1.22;
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; Synonyms=GABAT;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   brain 4-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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 36-485, AND PARTIAL PROTEIN SEQUENCE.
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, AND MUTAGENESIS OF CYS-321.
RX   PubMed=15528998;
RA   Yoon C.S., Kim D.W., Jang S.H., Lee B.R., Choi H.S., Choi S.H.,
RA   Kim S.Y., An J.J., Kwon O.S., Kang T.C., Won M.H., Cho S.W., Lee K.S.,
RA   Park J., Eum W.S., Choi S.Y.;
RT   "Cysteine-321 of human brain GABA transaminase is involved in
RT   intersubunit 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.,
RA   Buerckstuemmer T., 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   VARIANT GABATD LYS-220.
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-
CC       beta-aminoisobutyrate to succinate semialdehyde and methylmalonate
CC       semialdehyde, respectively. Can also convert delta-aminovalerate
CC       and beta-alanine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate +
CC         succinate semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888;
CC         EC=2.6.1.19;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-
CC         methyl-3-oxopropanoate + L-glutamate; Xref=Rhea:RHEA:13993,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57700,
CC         ChEBI:CHEBI:58655; EC=2.6.1.22;
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:49601;
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.
CC       {ECO:0000269|PubMed:15528998}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- TISSUE SPECIFICITY: Liver > pancreas > brain > kidney > heart >
CC       placenta.
CC   -!- DISEASE: GABA transaminase deficiency (GABATD) [MIM:613163]: An
CC       enzymatic deficiency resulting in psychomotor retardation,
CC       hypotonia, hyperreflexia, lethargy, refractory seizures, and EEG
CC       abnormalities. {ECO:0000269|PubMed:10407778}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=ABAT+%40+GABAT";
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   UniGene; Hs.336768; -.
DR   ProteinModelPortal; P80404; -.
DR   SMR; P80404; -.
DR   BioGrid; 106536; 38.
DR   IntAct; P80404; 2.
DR   MINT; P80404; -.
DR   STRING; 9606.ENSP00000268251; -.
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; L-Alanine.
DR   DrugBank; DB00142; L-Glutamic Acid.
DR   DrugBank; DB00780; Phenelzine.
DR   DrugBank; DB00114; Pyridoxal Phosphate.
DR   DrugBank; DB00119; Pyruvic acid.
DR   DrugBank; DB00313; Valproic Acid.
DR   DrugBank; DB01080; Vigabatrin.
DR   GuidetoPHARMACOLOGY; 2464; -.
DR   iPTMnet; P80404; -.
DR   PhosphoSitePlus; P80404; -.
DR   SwissPalm; P80404; -.
DR   BioMuta; ABAT; -.
DR   DMDM; 48429239; -.
DR   EPD; P80404; -.
DR   PaxDb; P80404; -.
DR   PeptideAtlas; P80404; -.
DR   PRIDE; P80404; -.
DR   ProteomicsDB; 57683; -.
DR   DNASU; 18; -.
DR   Ensembl; ENST00000268251; ENSP00000268251; ENSG00000183044.
DR   Ensembl; ENST00000396600; ENSP00000379845; ENSG00000183044.
DR   Ensembl; ENST00000425191; ENSP00000411916; ENSG00000183044.
DR   GeneID; 18; -.
DR   KEGG; hsa:18; -.
DR   CTD; 18; -.
DR   DisGeNET; 18; -.
DR   EuPathDB; HostDB:ENSG00000183044.11; -.
DR   GeneCards; ABAT; -.
DR   HGNC; HGNC:23; ABAT.
DR   HPA; HPA041528; -.
DR   HPA; HPA041690; -.
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   eggNOG; KOG1405; Eukaryota.
DR   eggNOG; COG0160; LUCA.
DR   GeneTree; ENSGT00550000074885; -.
DR   HOVERGEN; HBG000634; -.
DR   InParanoid; P80404; -.
DR   KO; K13524; -.
DR   PhylomeDB; P80404; -.
DR   TreeFam; TF105021; -.
DR   BioCyc; MetaCyc:HS02477-MONOMER; -.
DR   Reactome; R-HSA-916853; Degradation of GABA.
DR   SABIO-RK; P80404; -.
DR   ChiTaRS; ABAT; human.
DR   GenomeRNAi; 18; -.
DR   PRO; PR:P80404; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   Bgee; ENSG00000183044; Expressed in 228 organ(s), highest expression level in substantia nigra.
DR   CleanEx; HS_ABAT; -.
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:0003867; F:4-aminobutyrate transaminase activity; IBA:GO_Central.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
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:0042803; F:protein homodimerization activity; IPI:UniProtKB.
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: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   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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond; Iron;
KW   Iron-sulfur; Metal-binding; Mitochondrion;
KW   Neurotransmitter degradation; Polymorphism; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT       1     28       Mitochondrion.
FT   CHAIN        29    500       4-aminobutyrate aminotransferase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000001249.
FT   REGION      164    165       Pyridoxal phosphate binding.
FT                                {ECO:0000250|UniProtKB:P80147}.
FT   METAL       163    163       Iron-sulfur (2Fe-2S); shared with dimeric
FT                                partner. {ECO:0000250|UniProtKB:P80147}.
FT   METAL       166    166       Iron-sulfur (2Fe-2S); shared with dimeric
FT                                partner. {ECO:0000250|UniProtKB:P80147}.
FT   BINDING     220    220       Substrate.
FT                                {ECO:0000250|UniProtKB:P80147}.
FT   BINDING     381    381       Pyridoxal phosphate; shared with dimeric
FT                                partner. {ECO:0000250|UniProtKB:P80147}.
FT   MOD_RES     231    231       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     252    252       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     252    252       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     279    279       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     318    318       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     357    357       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250|UniProtKB:P80147}.
FT   MOD_RES     413    413       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     413    413       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     452    452       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     470    470       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   DISULFID    321    321       Interchain.
FT   VARIANT      56     56       Q -> R (in dbSNP:rs1731017).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_018979.
FT   VARIANT     220    220       R -> K (in GABATD; 25% reduction in
FT                                activity; dbSNP:rs121434578).
FT                                {ECO:0000269|PubMed:10407778}.
FT                                /FTId=VAR_008883.
FT   MUTAGEN     321    321       C->M,S,A,G,K: Loss of activity.
FT                                {ECO:0000269|PubMed:15528998}.
FT   CONFLICT     17     17       S -> T (in Ref. 1; AAA74449).
FT                                {ECO:0000305}.
FT   CONFLICT    109    109       H -> D (in Ref. 1; AAA74449).
FT                                {ECO:0000305}.
FT   CONFLICT    113    113       L -> V (in Ref. 1; AAA74449).
FT                                {ECO:0000305}.
FT   CONFLICT    132    132       G -> E (in Ref. 1; AAA74449).
FT                                {ECO:0000305}.
FT   CONFLICT    155    171       MSQLITMACGSCSNENA -> CPSSSPWPACPAPMKTT
FT                                (in Ref. 2; AAB38510). {ECO:0000305}.
FT   CONFLICT    191    191       Q -> K (in Ref. 1; AAA74449).
FT                                {ECO:0000305}.
FT   CONFLICT    204    204       G -> W (in Ref. 1; AAA74449).
FT                                {ECO:0000305}.
FT   CONFLICT    216    216       A -> S (in Ref. 1; AAA74449).
FT                                {ECO:0000305}.
FT   CONFLICT    247    247       P -> T (in Ref. 2; AAB38510).
FT                                {ECO:0000305}.
FT   CONFLICT    268    268       R -> G (in Ref. 1; AAA74449).
FT                                {ECO:0000305}.
FT   CONFLICT    320    320       G -> C (in Ref. 1; AAA74449).
FT                                {ECO:0000305}.
FT   CONFLICT    366    366       H -> L (in Ref. 1; AAA74449).
FT                                {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
//
DBGET integrated database retrieval system