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Database: UniProt
Entry: Q92830
LinkDB: Q92830
Original site: Q92830 
ID   KAT2A_HUMAN             Reviewed;         837 AA.
AC   Q92830; Q8N1A2; Q9UCW1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 3.
DT   26-NOV-2014, entry version 163.
DE   RecName: Full=Histone acetyltransferase KAT2A;
DE            EC=2.3.1.48;
DE   AltName: Full=General control of amino acid synthesis protein 5-like 2;
DE   AltName: Full=Histone acetyltransferase GCN5;
DE            Short=HsGCN5;
DE   AltName: Full=Lysine acetyltransferase 2A;
DE   AltName: Full=STAF97;
GN   Name=KAT2A; Synonyms=GCN5, GCN5L2, HGCN5;
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 [GENOMIC DNA] (ISOFORM 2), AND CHARACTERIZATION.
RC   TISSUE=Testis;
RX   PubMed=8552087;
RA   Candau R., Moore P.A., Wang L., Barlev N., Ying C.Y., Rosen C.A.,
RA   Berger S.L.;
RT   "Identification of human proteins functionally conserved with the
RT   yeast putative adaptors ADA2 and GCN5.";
RL   Mol. Cell. Biol. 16:593-602(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Liver;
RX   PubMed=9611240; DOI=10.1093/nar/26.12.2948;
RA   Smith E.R., Belote J.M., Schlitz R.L., Yang X.-J., Moore P.A.,
RA   Berger S.L., Nakatani Y., Allis C.D.;
RT   "Cloning of Drosophila GCN5: conserved features among metazoan GCN5
RT   family members.";
RL   Nucleic Acids Res. 26:2948-2954(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, Skin, and Testis;
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 [GENOMIC DNA] OF 362-837 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=8684459; DOI=10.1038/382319a0;
RA   Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.;
RT   "A p300/CBP-associated factor that competes with the adenoviral
RT   oncoprotein E1A.";
RL   Nature 382:319-324(1996).
RN   [6]
RP   SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H;
RP   KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10; TAF12 AND TAF9, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11564863; DOI=10.1128/MCB.21.20.6782-6795.2001;
RA   Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
RA   Kundu T.K., Chait B.T., Roeder R.G.;
RT   "Human STAGA complex is a chromatin-acetylating transcription
RT   coactivator that interacts with pre-mRNA splicing and DNA damage-
RT   binding factors in vivo.";
RL   Mol. Cell. Biol. 21:6782-6795(2001).
RN   [7]
RP   IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L;
RP   SUPT3H; TAF2; TAF4; TAF5; TRRAP AND TAF10.
RX   PubMed=10373431; DOI=10.1074/jbc.274.26.18285;
RA   Brand M., Yamamoto K., Staub A., Tora L.;
RT   "Identification of TATA-binding protein-free TAFII-containing complex
RT   subunits suggests a role in nucleosome acetylation and signal
RT   transduction.";
RL   J. Biol. Chem. 274:18285-18289(1999).
RN   [8]
RP   INTERACTION WITH TRRAP.
RX   PubMed=10611234; DOI=10.1128/MCB.20.2.556-562.2000;
RA   McMahon S.B., Wood M.A., Cole M.D.;
RT   "The essential cofactor TRRAP recruits the histone acetyltransferase
RT   hGCN5 to c-Myc.";
RL   Mol. Cell. Biol. 20:556-562(2000).
RN   [9]
RP   INTERACTION WITH HIV-1 TAT.
RX   PubMed=11384967; DOI=10.1074/jbc.M101385200;
RA   Col E., Caron C., Seigneurin-Berny D., Gracia J., Favier A.,
RA   Khochbin S.;
RT   "The histone acetyltransferase, hGCN5, interacts with and acetylates
RT   the HIV transactivator, Tat.";
RL   J. Biol. Chem. 276:28179-28184(2001).
RN   [10]
RP   INTERACTION WITH TAF3.
RX   PubMed=11438666; DOI=10.1128/MCB.21.15.5109-5121.2001;
RA   Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C.,
RA   Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
RT   "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155)
RT   are novel metazoan homologues of yeast TAFII47 containing a histone
RT   fold and a PHD finger.";
RL   Mol. Cell. Biol. 21:5109-5121(2001).
RN   [11]
RP   INTERACTION WITH TACC1; TACC2 AND TACC3.
RX   PubMed=14767476; DOI=10.1038/sj.onc.1207424;
RA   Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.;
RT   "The transforming acidic coiled coil proteins interact with nuclear
RT   histone acetyltransferases.";
RL   Oncogene 23:2559-2563(2004).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [13]
RP   IDENTIFICATION IN STAGA COMPLEX.
RX   PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
RA   Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S.,
RA   Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A.,
RA   Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.;
RT   "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
RT   coactivates nuclear receptors, and counteracts heterochromatin
RT   silencing.";
RL   Mol. Cell 29:92-101(2008).
RN   [14]
RP   FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX.
RX   PubMed=19103755; DOI=10.1128/MCB.01599-08;
RA   Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
RA   Lill J.R., Zha J.;
RT   "The double-histone-acetyltransferase complex ATAC is essential for
RT   mammalian development.";
RL   Mol. Cell. Biol. 29:1176-1188(2009).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [16]
RP   STRUCTURE BY NMR OF 730-832.
RX   PubMed=11090279; DOI=10.1006/jmbi.2000.4207;
RA   Hudson B.P., Martinez-Yamout M.A., Dyson H.J., Wright P.E.;
RT   "Solution structure and acetyl-lysine binding activity of the GCN5
RT   bromodomain.";
RL   J. Mol. Biol. 304:355-370(2000).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 497-662 IN COMPLEX WITH
RP   ACETYL-COA, AND ACTIVE SITE.
RX   PubMed=17410582; DOI=10.1002/prot.21407;
RA   Schuetz A., Bernstein G., Dong A., Antoshenko T., Wu H., Loppnau P.,
RA   Bochkarev A., Plotnikov A.N.;
RT   "Crystal structure of a binary complex between human GCN5 histone
RT   acetyltransferase domain and acetyl coenzyme A.";
RL   Proteins 68:403-407(2007).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 729-837.
RX   PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA   Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA   Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA   Gingras A.C., Arrowsmith C.H., Knapp S.;
RT   "Histone recognition and large-scale structural analysis of the human
RT   bromodomain family.";
RL   Cell 149:214-231(2012).
CC   -!- FUNCTION: Functions as a histone acetyltransferase (HAT) to
CC       promote transcriptional activation. Acetylation of histones gives
CC       a specific tag for epigenetic transcription activation. Has
CC       significant histone acetyltransferase activity with core histones,
CC       but not with nucleosome core particles. In case of HIV-1
CC       infection, it is recruited by the viral protein Tat. Regulates
CC       Tat's transactivating activity and may help inducing chromatin
CC       remodeling of proviral genes. Component of the ATAC complex, a
CC       complex with histone acetyltransferase activity on histones H3 and
CC       H4. {ECO:0000269|PubMed:19103755}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone].
CC   -!- SUBUNIT: Interacts with EP300, CREBBP and ADA2. Component of the
CC       TFTC-HAT complex, at least composed of TAF5L, TAF6L, TAF3, TADA3L,
CC       SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100,
CC       KAT2A/GCN5L2, TAF10 and TRRAP. Interacts with TRRAP. Component of
CC       the STAGA transcription coactivator-HAT complex, at least composed
CC       of SUPT3H, KAT2A, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10,
CC       TAF12, TRRAP and TAF9. The STAGA core complex is associated with a
CC       subcomplex required for histone deubiquitination composed of
CC       ATXN7L3, ENY2 and USP22. Interacts with and acetylates HIV-1 Tat.
CC       Component of the ADA2A-containing complex (ATAC), composed of
CC       CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101
CC       and DR1. In the complex, it probably interacts directly with
CC       CSRP2BP, MBIP and WDR5. Interacts with PML (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       O75717:WDHD1; NbExp=5; IntAct=EBI-477622, EBI-3951691;
CC       Q8IYH5:ZZZ3; NbExp=2; IntAct=EBI-477622, EBI-2795524;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=GCN5-L;
CC         IsoId=Q92830-1; Sequence=Displayed;
CC       Name=2; Synonyms=GCN5-S;
CC         IsoId=Q92830-2; Sequence=VSP_000556;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested, with most
CC       abundant expression in ovary.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 bromo domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00035}.
CC   -!- SIMILARITY: Contains 1 N-acetyltransferase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00532}.
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DR   EMBL; AF029777; AAC39769.1; -; mRNA.
DR   EMBL; CH471152; EAW60803.1; -; Genomic_DNA.
DR   EMBL; BC032743; AAH32743.1; -; mRNA.
DR   EMBL; BC039907; AAH39907.1; -; mRNA.
DR   EMBL; BC105977; AAI05978.1; -; mRNA.
DR   EMBL; U57316; AAC50641.1; -; Genomic_DNA.
DR   CCDS; CCDS11417.1; -. [Q92830-1]
DR   PIR; S71789; S71789.
DR   RefSeq; NP_066564.2; NM_021078.2. [Q92830-1]
DR   UniGene; Hs.463045; -.
DR   PDB; 1F68; NMR; -; A=730-832.
DR   PDB; 1Z4R; X-ray; 1.74 A; A=497-662.
DR   PDB; 3D7C; X-ray; 2.06 A; A/B=729-837.
DR   PDBsum; 1F68; -.
DR   PDBsum; 1Z4R; -.
DR   PDBsum; 3D7C; -.
DR   ProteinModelPortal; Q92830; -.
DR   SMR; Q92830; 497-658, 730-835.
DR   BioGrid; 108918; 105.
DR   DIP; DIP-28146N; -.
DR   IntAct; Q92830; 36.
DR   MINT; MINT-199927; -.
DR   STRING; 9606.ENSP00000225916; -.
DR   ChEMBL; CHEMBL5501; -.
DR   PhosphoSite; Q92830; -.
DR   DMDM; 209572743; -.
DR   MaxQB; Q92830; -.
DR   PaxDb; Q92830; -.
DR   PRIDE; Q92830; -.
DR   Ensembl; ENST00000225916; ENSP00000225916; ENSG00000108773. [Q92830-1]
DR   GeneID; 2648; -.
DR   KEGG; hsa:2648; -.
DR   UCSC; uc002hyx.2; human. [Q92830-1]
DR   CTD; 2648; -.
DR   GeneCards; GC17M040265; -.
DR   HGNC; HGNC:4201; KAT2A.
DR   HPA; HPA048958; -.
DR   MIM; 602301; gene.
DR   neXtProt; NX_Q92830; -.
DR   PharmGKB; PA162392664; -.
DR   eggNOG; COG5076; -.
DR   GeneTree; ENSGT00760000119099; -.
DR   HOGENOM; HOG000007151; -.
DR   InParanoid; Q92830; -.
DR   KO; K06062; -.
DR   OMA; NSPIWES; -.
DR   PhylomeDB; Q92830; -.
DR   TreeFam; TF105399; -.
DR   Reactome; REACT_118568; Pre-NOTCH Transcription and Translation.
DR   Reactome; REACT_118780; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; REACT_14835; Notch-HLH transcription pathway.
DR   Reactome; REACT_160243; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; REACT_160254; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; REACT_172610; HATs acetylate histones.
DR   Reactome; REACT_953; RNA Polymerase I Transcription Initiation.
DR   SignaLink; Q92830; -.
DR   ChiTaRS; KAT2A; human.
DR   EvolutionaryTrace; Q92830; -.
DR   GeneWiki; GCN5L2; -.
DR   GenomeRNAi; 2648; -.
DR   NextBio; 10450; -.
DR   PRO; PR:Q92830; -.
DR   Bgee; Q92830; -.
DR   CleanEx; HS_KAT2A; -.
DR   ExpressionAtlas; Q92830; baseline and differential.
DR   Genevestigator; Q92830; -.
DR   GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProt.
DR   GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0030914; C:STAGA complex; IDA:UniProtKB.
DR   GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:BHF-UCL.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0043997; F:histone acetyltransferase activity (H4-K12 specific); IEA:Ensembl.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR   GO; GO:0006325; P:chromatin organization; TAS:Reactome.
DR   GO; GO:0006338; P:chromatin remodeling; TAS:ProtInc.
DR   GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
DR   GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR   GO; GO:0044154; P:histone H3-K14 acetylation; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0022037; P:metencephalon development; IEA:Ensembl.
DR   GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR   GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.920.10; -; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR016376; Hist_acetylase_PCAF.
DR   InterPro; IPR009464; PCAF_N.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF06466; PCAF_N; 1.
DR   PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase; Alternative splicing;
KW   Bromodomain; Complete proteome; Host-virus interaction; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:22814378}.
FT   CHAIN         2    837       Histone acetyltransferase KAT2A.
FT                                /FTId=PRO_0000211202.
FT   DOMAIN      503    656       N-acetyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00532}.
FT   DOMAIN      745    815       Bromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00035}.
FT   REGION      579    581       Acetyl-CoA binding.
FT                                {ECO:0000269|PubMed:17410582}.
FT   REGION      586    592       Acetyl-CoA binding.
FT                                {ECO:0000269|PubMed:17410582}.
FT   REGION      617    620       Acetyl-CoA binding.
FT                                {ECO:0000269|PubMed:17410582}.
FT   ACT_SITE    575    575       Proton donor/acceptor.
FT                                {ECO:0000303|PubMed:17410582}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:22814378}.
FT   VAR_SEQ       1    410       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_000556.
FT   CONFLICT    116    116       E -> G (in Ref. 1; AAC39769).
FT                                {ECO:0000305}.
FT   CONFLICT    134    134       M -> I (in Ref. 1; AAC39769).
FT                                {ECO:0000305}.
FT   CONFLICT    269    269       K -> E (in Ref. 1; AAC39769).
FT                                {ECO:0000305}.
FT   STRAND      498    504       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       514    530       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       536    543       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      549    555       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      558    568       {ECO:0000244|PDB:1Z4R}.
FT   TURN        569    572       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      573    581       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       583    585       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      587    589       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       590    604       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      609    614       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       616    618       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       619    624       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      627    629       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       635    638       {ECO:0000244|PDB:1Z4R}.
FT   TURN        639    641       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      649    654       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       730    746       {ECO:0000244|PDB:3D7C}.
FT   HELIX       748    753       {ECO:0000244|PDB:3D7C}.
FT   TURN        759    761       {ECO:0000244|PDB:3D7C}.
FT   HELIX       765    768       {ECO:0000244|PDB:3D7C}.
FT   HELIX       775    783       {ECO:0000244|PDB:3D7C}.
FT   HELIX       790    807       {ECO:0000244|PDB:3D7C}.
FT   HELIX       813    831       {ECO:0000244|PDB:3D7C}.
SQ   SEQUENCE   837 AA;  93926 MW;  728CC8ACF08600EA CRC64;
     MAEPSQAPTP APAAQPRPLQ SPAPAPTPTP APSPASAPIP TPTPAPAPAP AAAPAGSTGT
     GGPGVGSGGA GSGGDPARPG LSQQQRASQR KAQVRGLPRA KKLEKLGVFS ACKANETCKC
     NGWKNPKPPT APRMDLQQPA ANLSELCRSC EHPLADHVSH LENVSEDEIN RLLGMVVDVE
     NLFMSVHKEE DTDTKQVYFY LFKLLRKCIL QMTRPVVEGS LGSPPFEKPN IEQGVLNFVQ
     YKFSHLAPRE RQTMFELSKM FLLCLNYWKL ETPAQFRQRS QAEDVATYKV NYTRWLCYCH
     VPQSCDSLPR YETTHVFGRS LLRSIFTVTR RQLLEKFRVE KDKLVPEKRT LILTHFPKFL
     SMLEEEIYGA NSPIWESGFT MPPSEGTQLV PRPASVSAAV VPSTPIFSPS MGGGSNSSLS
     LDSAGAEPMP GEKRTLPENL TLEDAKRLRV MGDIPMELVN EVMLTITDPA AMLGPETSLL
     SANAARDETA RLEERRGIIE FHVIGNSLTP KANRRVLLWL VGLQNVFSHQ LPRMPKEYIA
     RLVFDPKHKT LALIKDGRVI GGICFRMFPT QGFTEIVFCA VTSNEQVKGY GTHLMNHLKE
     YHIKHNILYF LTYADEYAIG YFKKQGFSKD IKVPKSRYLG YIKDYEGATL MECELNPRIP
     YTELSHIIKK QKEIIKKLIE RKQAQIRKVY PGLSCFKEGV RQIPVESVPG IRETGWKPLG
     KEKGKELKDP DQLYTTLKNL LAQIKSHPSA WPFMEPVKKS EAPDYYEVIR FPIDLKTMTE
     RLRSRYYVTR KLFVADLQRV IANCREYNPP DSEYCRCASA LEKFFYFKLK EGGLIDK
//
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