GenomeNet

Database: UniProt
Entry: Q8N5Z0
LinkDB: Q8N5Z0
Original site: Q8N5Z0 
ID   AADAT_HUMAN             Reviewed;         425 AA.
AC   Q8N5Z0; B3KP84; Q9UL02;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   17-JUN-2020, entry version 158.
DE   RecName: Full=Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial;
DE            Short=KAT/AadAT;
DE   AltName: Full=2-aminoadipate aminotransferase;
DE   AltName: Full=2-aminoadipate transaminase;
DE            EC=2.6.1.39;
DE   AltName: Full=Alpha-aminoadipate aminotransferase;
DE            Short=AadAT;
DE   AltName: Full=Kynurenine aminotransferase II;
DE   AltName: Full=Kynurenine--oxoglutarate aminotransferase II;
DE   AltName: Full=Kynurenine--oxoglutarate transaminase 2;
DE            EC=2.6.1.7;
DE   AltName: Full=Kynurenine--oxoglutarate transaminase II;
DE   Flags: Precursor;
GN   Name=AADAT; Synonyms=KAT2;
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).
RC   TISSUE=Brain;
RA   Gatti S., Breton J., Mostardini M., Mosca M., Tarroni P., Schwarcz R.,
RA   Speciale C., Okuno E., Toma S., Benatti L.;
RT   "Cloning of human L-kynurenine/alpha-aminoadipate aminotransferase cDNA
RT   from brain tissue.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=12126930; DOI=10.1016/s1096-7192(02)00037-9;
RA   Goh D.L.M., Patel A., Thomas G.H., Salomons G.S., Schor D.S.M., Jakobs C.,
RA   Geraghty M.T.;
RT   "Characterization of the human gene encoding alpha-aminoadipate
RT   aminotransferase (AADAT).";
RL   Mol. Genet. Metab. 76:172-180(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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] (ISOFORM 2).
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   [5]
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   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH 2-OXOGLUTARATE,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP   SUBUNIT, AND FUNCTION.
RX   PubMed=18620547; DOI=10.1042/bsr20080085;
RA   Han Q., Cai T., Tagle D.A., Robinson H., Li J.;
RT   "Substrate specificity and structure of human aminoadipate
RT   aminotransferase/kynurenine aminotransferase II.";
RL   Biosci. Rep. 28:205-215(2008).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP   AND KYRUNENINE, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX   PubMed=18056995; DOI=10.1074/jbc.m708358200;
RA   Han Q., Robinson H., Li J.;
RT   "Crystal structure of human kynurenine aminotransferase II.";
RL   J. Biol. Chem. 283:3567-3573(2008).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP   SUBUNIT, AND COFACTOR.
RX   PubMed=18056996; DOI=10.1074/jbc.m707925200;
RA   Rossi F., Garavaglia S., Montalbano V., Walsh M.A., Rizzi M.;
RT   "Crystal structure of human kynurenine aminotransferase II, a drug target
RT   for the treatment of schizophrenia.";
RL   J. Biol. Chem. 283:3559-3566(2008).
CC   -!- FUNCTION: Transaminase with broad substrate specificity. Has
CC       transaminase activity towards aminoadipate, kynurenine, methionine and
CC       glutamate. Shows activity also towards tryptophan, aspartate and
CC       hydroxykynurenine. Accepts a variety of oxo-acids as amino-group
CC       acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid,
CC       phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use
CC       glyoxylate as amino-group acceptor (in vitro).
CC       {ECO:0000269|PubMed:18620547}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-kynurenine = 4-(2-aminophenyl)-2,4-
CC         dioxobutanoate + L-glutamate; Xref=Rhea:RHEA:20964,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC         ChEBI:CHEBI:58147; EC=2.6.1.7;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-
CC         glutamate; Xref=Rhea:RHEA:12601, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57499, ChEBI:CHEBI:58672; EC=2.6.1.39;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:12126930, ECO:0000269|PubMed:18056995,
CC         ECO:0000269|PubMed:18056996};
CC   -!- ACTIVITY REGULATION: Kynurenine transaminase activity is competitively
CC       inhibited by aminoadipate, asparagine, glutamate, histidine, cysteine,
CC       lysine, 3-hydroxy-kynurenine and phenylalanine.
CC       {ECO:0000269|PubMed:18620547}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.9 mM for aminoadipate {ECO:0000269|PubMed:18620547};
CC         KM=4.7 mM for kynurenine {ECO:0000269|PubMed:18620547};
CC         KM=1.7 mM for methionine {ECO:0000269|PubMed:18620547};
CC         KM=1.6 mM for glutamate {ECO:0000269|PubMed:18620547};
CC         KM=1.8 mM for tyrosine {ECO:0000269|PubMed:18620547};
CC         KM=1.2 mM for 2-oxoglutarate {ECO:0000269|PubMed:18620547};
CC         KM=1.5 mM for 2-oxocaproic acid {ECO:0000269|PubMed:18620547};
CC         KM=1.8 mM for phenylpyruvate {ECO:0000269|PubMed:18620547};
CC         KM=1.4 mM for ino-3-pyruvate {ECO:0000269|PubMed:18620547};
CC       pH dependence:
CC         Optimum pH is 7-9. {ECO:0000269|PubMed:18620547};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:18620547};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 4/6.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18056995,
CC       ECO:0000269|PubMed:18056996, ECO:0000269|PubMed:18620547}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8N5Z0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N5Z0-2; Sequence=VSP_009874;
CC   -!- TISSUE SPECIFICITY: Higher expression in the liver. Also found in
CC       heart, brain, kidney, pancreas, prostate, testis and ovary.
CC   -!- MISCELLANEOUS: [Isoform 1]: May be due to a competing donor splice
CC       site.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
DR   EMBL; AF097994; AAF04623.1; -; mRNA.
DR   EMBL; AF481738; AAM09683.1; -; mRNA.
DR   EMBL; AK055952; BAG51596.1; -; mRNA.
DR   EMBL; BC031068; AAH31068.1; -; mRNA.
DR   CCDS; CCDS3814.1; -. [Q8N5Z0-1]
DR   CCDS; CCDS75209.1; -. [Q8N5Z0-2]
DR   RefSeq; NP_001273611.1; NM_001286682.1. [Q8N5Z0-2]
DR   RefSeq; NP_001273612.1; NM_001286683.1. [Q8N5Z0-1]
DR   RefSeq; NP_057312.1; NM_016228.3. [Q8N5Z0-1]
DR   RefSeq; NP_872603.1; NM_182662.1. [Q8N5Z0-1]
DR   PDB; 2QLR; X-ray; 2.30 A; A/B/C/D=1-425.
DR   PDB; 2R2N; X-ray; 1.95 A; A/B/C/D=1-425.
DR   PDB; 2VGZ; X-ray; 2.30 A; A/B=2-425.
DR   PDB; 2XH1; X-ray; 2.10 A; A/B=1-425.
DR   PDB; 3DC1; X-ray; 2.50 A; A/B/C/D=1-425.
DR   PDB; 3UE8; X-ray; 3.22 A; A/B=1-425.
DR   PDB; 4GDY; X-ray; 2.89 A; A/B=1-425.
DR   PDB; 4GE4; X-ray; 2.41 A; A/B=1-425.
DR   PDB; 4GE7; X-ray; 2.10 A; A/B=1-425.
DR   PDB; 4GE9; X-ray; 2.43 A; A/B/C/D=1-425.
DR   PDB; 4GEB; X-ray; 2.15 A; A/B=1-425.
DR   PDB; 5EFS; X-ray; 1.83 A; A=1-425.
DR   PDB; 5EUN; X-ray; 1.82 A; A=1-425.
DR   PDB; 5TF5; X-ray; 1.81 A; A/B=1-425.
DR   PDB; 6D0A; X-ray; 1.47 A; A=1-425.
DR   PDB; 6T8P; X-ray; 2.02 A; A/B=1-425.
DR   PDB; 6T8Q; X-ray; 2.51 A; A=1-425.
DR   PDBsum; 2QLR; -.
DR   PDBsum; 2R2N; -.
DR   PDBsum; 2VGZ; -.
DR   PDBsum; 2XH1; -.
DR   PDBsum; 3DC1; -.
DR   PDBsum; 3UE8; -.
DR   PDBsum; 4GDY; -.
DR   PDBsum; 4GE4; -.
DR   PDBsum; 4GE7; -.
DR   PDBsum; 4GE9; -.
DR   PDBsum; 4GEB; -.
DR   PDBsum; 5EFS; -.
DR   PDBsum; 5EUN; -.
DR   PDBsum; 5TF5; -.
DR   PDBsum; 6D0A; -.
DR   PDBsum; 6T8P; -.
DR   PDBsum; 6T8Q; -.
DR   SMR; Q8N5Z0; -.
DR   BioGRID; 119346; 21.
DR   IntAct; Q8N5Z0; 1.
DR   STRING; 9606.ENSP00000423190; -.
DR   BindingDB; Q8N5Z0; -.
DR   ChEMBL; CHEMBL2046259; -.
DR   DrugBank; DB00142; Glutamic acid.
DR   DrugBank; DB00114; Pyridoxal phosphate.
DR   iPTMnet; Q8N5Z0; -.
DR   PhosphoSitePlus; Q8N5Z0; -.
DR   BioMuta; AADAT; -.
DR   DMDM; 46395904; -.
DR   EPD; Q8N5Z0; -.
DR   jPOST; Q8N5Z0; -.
DR   MassIVE; Q8N5Z0; -.
DR   MaxQB; Q8N5Z0; -.
DR   PaxDb; Q8N5Z0; -.
DR   PeptideAtlas; Q8N5Z0; -.
DR   PRIDE; Q8N5Z0; -.
DR   ProteomicsDB; 72114; -. [Q8N5Z0-1]
DR   ProteomicsDB; 72115; -. [Q8N5Z0-2]
DR   Antibodypedia; 17143; 313 antibodies.
DR   DNASU; 51166; -.
DR   Ensembl; ENST00000337664; ENSP00000336808; ENSG00000109576. [Q8N5Z0-1]
DR   Ensembl; ENST00000353187; ENSP00000226840; ENSG00000109576. [Q8N5Z0-1]
DR   Ensembl; ENST00000509167; ENSP00000423190; ENSG00000109576. [Q8N5Z0-2]
DR   Ensembl; ENST00000515480; ENSP00000423341; ENSG00000109576. [Q8N5Z0-1]
DR   GeneID; 51166; -.
DR   KEGG; hsa:51166; -.
DR   UCSC; uc003isr.4; human. [Q8N5Z0-1]
DR   CTD; 51166; -.
DR   DisGeNET; 51166; -.
DR   EuPathDB; HostDB:ENSG00000109576.13; -.
DR   GeneCards; AADAT; -.
DR   HGNC; HGNC:17929; AADAT.
DR   HPA; ENSG00000109576; Tissue enriched (liver).
DR   MIM; 611754; gene.
DR   neXtProt; NX_Q8N5Z0; -.
DR   OpenTargets; ENSG00000109576; -.
DR   PharmGKB; PA24364; -.
DR   eggNOG; KOG0634; Eukaryota.
DR   eggNOG; COG1167; LUCA.
DR   GeneTree; ENSGT00390000004594; -.
DR   HOGENOM; CLU_017584_0_6_1; -.
DR   InParanoid; Q8N5Z0; -.
DR   KO; K00825; -.
DR   OMA; MRLNFTY; -.
DR   OrthoDB; 1241781at2759; -.
DR   PhylomeDB; Q8N5Z0; -.
DR   TreeFam; TF328598; -.
DR   BioCyc; MetaCyc:HS03239-MONOMER; -.
DR   BRENDA; 2.6.1.39; 2681.
DR   BRENDA; 2.6.1.7; 2681.
DR   Reactome; R-HSA-71064; Lysine catabolism.
DR   Reactome; R-HSA-71240; Tryptophan catabolism.
DR   SABIO-RK; Q8N5Z0; -.
DR   UniPathway; UPA00868; UER00838.
DR   BioGRID-ORCS; 51166; 12 hits in 786 CRISPR screens.
DR   ChiTaRS; AADAT; human.
DR   EvolutionaryTrace; Q8N5Z0; -.
DR   GenomeRNAi; 51166; -.
DR   Pharos; Q8N5Z0; Tchem.
DR   PRO; PR:Q8N5Z0; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q8N5Z0; protein.
DR   Bgee; ENSG00000109576; Expressed in right lobe of liver and 147 other tissues.
DR   ExpressionAtlas; Q8N5Z0; baseline and differential.
DR   Genevisible; Q8N5Z0; HS.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0047536; F:2-aminoadipate transaminase activity; IDA:UniProtKB.
DR   GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB.
DR   GO; GO:1901605; P:alpha-amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IDA:UniProtKB.
DR   GO; GO:0070189; P:kynurenine metabolic process; IDA:UniProtKB.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006554; P:lysine catabolic process; TAS:Reactome.
DR   GO; GO:0006569; P:tryptophan catabolic process; TAS:Reactome.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Aminotransferase;
KW   Mitochondrion; Polymorphism; Pyridoxal phosphate; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..425
FT                   /note="Kynurenine/alpha-aminoadipate aminotransferase,
FT                   mitochondrial"
FT                   /id="PRO_0000020602"
FT   BINDING         20
FT                   /note="Substrate"
FT   BINDING         74
FT                   /note="Substrate"
FT   BINDING         142
FT                   /note="Substrate"
FT   BINDING         202
FT                   /note="Substrate"
FT   BINDING         399
FT                   /note="Substrate"
FT   MOD_RES         69
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT   MOD_RES         179
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT   MOD_RES         263
FT                   /note="N6-(pyridoxal phosphate)lysine; alternate"
FT   MOD_RES         263
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT   MOD_RES         263
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT   MOD_RES         339
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT   MOD_RES         339
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT   MOD_RES         367
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT   MOD_RES         367
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT   MOD_RES         422
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT   VAR_SEQ         23
FT                   /note="T -> SEKRA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_009874"
FT   VARIANT         243
FT                   /note="V -> I (in dbSNP:rs56350236)"
FT                   /id="VAR_061005"
FT   CONFLICT        103
FT                   /note="P -> Q (in Ref. 4; AAH31068)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380
FT                   /note="L -> S (in Ref. 3; BAG51596)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..6
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           9..13
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           19..21
FT                   /evidence="ECO:0000244|PDB:2R2N"
FT   HELIX           23..27
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           43..45
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          51..53
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   TURN            56..58
FT                   /evidence="ECO:0000244|PDB:4GEB"
FT   STRAND          61..63
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           65..71
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           81..95
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   TURN            98..101
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           104..106
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          109..116
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           117..128
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          134..137
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           143..149
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           150..152
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          155..158
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           168..175
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           180..184
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           186..188
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          193..196
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   TURN            202..204
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           210..223
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          226..230
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   TURN            232..235
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          239..241
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           247..249
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          251..253
FT                   /evidence="ECO:0000244|PDB:5TF5"
FT   STRAND          255..261
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   TURN            262..265
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   TURN            267..270
FT                   /evidence="ECO:0000244|PDB:4GE9"
FT   STRAND          272..277
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           278..289
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   TURN            290..292
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          293..295
FT                   /evidence="ECO:0000244|PDB:4GE7"
FT   HELIX           297..340
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   TURN            341..344
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          345..347
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          351..360
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   HELIX           368..371
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   TURN            372..378
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          381..383
FT                   /evidence="ECO:0000244|PDB:4GDY"
FT   HELIX           384..387
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   STRAND          388..390
FT                   /evidence="ECO:0000244|PDB:5TF5"
FT   STRAND          391..393
FT                   /evidence="ECO:0000244|PDB:3UE8"
FT   STRAND          397..401
FT                   /evidence="ECO:0000244|PDB:6D0A"
FT   TURN            402..404
FT                   /evidence="ECO:0000244|PDB:3UE8"
FT   HELIX           407..422
FT                   /evidence="ECO:0000244|PDB:6D0A"
SQ   SEQUENCE   425 AA;  47352 MW;  448CCAAB2173A7BA CRC64;
     MNYARFITAA SAARNPSPIR TMTDILSRGP KSMISLAGGL PNPNMFPFKT AVITVENGKT
     IQFGEEMMKR ALQYSPSAGI PELLSWLKQL QIKLHNPPTI HYPPSQGQMD LCVTSGSQQG
     LCKVFEMIIN PGDNVLLDEP AYSGTLQSLH PLGCNIINVA SDESGIVPDS LRDILSRWKP
     EDAKNPQKNT PKFLYTVPNG NNPTGNSLTS ERKKEIYELA RKYDFLIIED DPYYFLQFNK
     FRVPTFLSMD VDGRVIRADS FSKIISSGLR IGFLTGPKPL IERVILHIQV STLHPSTFNQ
     LMISQLLHEW GEEGFMAHVD RVIDFYSNQK DAILAAADKW LTGLAEWHVP AAGMFLWIKV
     KGINDVKELI EEKAVKMGVL MLPGNAFYVD SSAPSPYLRA SFSSASPEQM DVAFQVLAQL
     IKESL
//
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