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Database: UniProt/SWISS-PROT
Entry: HDAC6_MOUSE
LinkDB: HDAC6_MOUSE
Original site: HDAC6_MOUSE 
ID   HDAC6_MOUSE             Reviewed;        1149 AA.
AC   Q9Z2V5; B1AUA6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   25-OCT-2017, entry version 151.
DE   RecName: Full=Histone deacetylase 6;
DE            Short=HD6;
DE            EC=3.5.1.98;
DE   AltName: Full=Histone deacetylase mHDA2;
GN   Name=Hdac6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Fetus;
RX   PubMed=9891014; DOI=10.1074/jbc.274.4.2440;
RA   Verdel A., Khochbin S.;
RT   "Identification of a new family of higher eukaryotic histone
RT   deacetylases. Coordinate expression of differentiation-dependent
RT   chromatin modifiers.";
RL   J. Biol. Chem. 274:2440-2445(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   INTERACTION WITH CBFA2T3.
RX   PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
RA   Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
RA   Downing J.R., Meyers S., Hiebert S.W.;
RT   "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
RT   with multiple histone deacetylases and binds mSin3A through its
RT   oligomerization domain.";
RL   Mol. Cell. Biol. 21:6470-6483(2001).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16933150; DOI=10.1007/s11064-006-9127-6;
RA   Southwood C.M., Peppi M., Dryden S., Tainsky M.A., Gow A.;
RT   "Microtubule deacetylases, SirT2 and HDAC6, in the nervous system.";
RL   Neurochem. Res. 32:187-195(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-43 AND SER-1148,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   FUNCTION, INTERACTION WITH CYLD AND MICROTUBULES, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19893491; DOI=10.1038/emboj.2009.317;
RA   Wickstrom S.A., Masoumi K.C., Khochbin S., Fassler R., Massoumi R.;
RT   "CYLD negatively regulates cell-cycle progression by inactivating
RT   HDAC6 and increasing the levels of acetylated tubulin.";
RL   EMBO J. 29:131-144(2010).
RN   [7]
RP   INTERACTION WITH ZMYND15.
RX   PubMed=20675388; DOI=10.1074/jbc.M110.116418;
RA   Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A.,
RA   Saunders L., Verdin E., Charo I.F.;
RT   "Zmynd15 encodes a histone deacetylase-dependent transcriptional
RT   repressor essential for spermiogenesis and male fertility.";
RL   J. Biol. Chem. 285:31418-31426(2010).
RN   [8]
RP   FUNCTION IN AUTOPHAGY, AND SUBCELLULAR LOCATION.
RX   PubMed=22819792; DOI=10.1016/j.neuint.2012.07.010;
RA   Gal J., Bang Y., Choi H.J.;
RT   "SIRT2 interferes with autophagy-mediated degradation of protein
RT   aggregates in neuronal cells under proteasome inhibition.";
RL   Neurochem. Int. 61:992-1000(2012).
RN   [9]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-32, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.O113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes (By similarity).
CC       Plays a central role in microtubule-dependent cell motility via
CC       deacetylation of tubulin. {ECO:0000250,
CC       ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:22819792}.
CC   -!- FUNCTION: In addition to its protein deacetylase activity, plays a
CC       key role in the degradation of misfolded proteins: when misfolded
CC       proteins are too abundant to be degraded by the chaperone
CC       refolding system and the ubiquitin-proteasome, mediates the
CC       transport of misfolded proteins to a cytoplasmic juxtanuclear
CC       structure called aggresome. Probably acts as an adapter that
CC       recognizes polyubiquitinated misfolded proteins and target them to
CC       the aggresome, facilitating their clearance by autophagy (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with BBIP10, DDIT3/CHOP, F-actin and HDAC11.
CC       Interacts with SIRT2 (via both phosphorylated, unphosphorylated,
CC       active or inactive forms); the interaction is necessary for the
CC       complex to interact with alpha-tubulin. Under proteasome
CC       impairment conditions, interacts with UBD via its histone
CC       deacetylase 1 and UBP-type zinc-finger regions (By similarity).
CC       Interacts with CBFA2T3, CYLD and ZMYND15. Interacts with RIPOR2;
CC       this interaction occurs during early myogenic differentiation and
CC       prevents HDAC6 to deacetylate tubulin (By similarity). Interacts
CC       with DYSF; this interaction occurs during early myogenic
CC       differentiation (By similarity). {ECO:0000250|UniProtKB:Q9UBN7,
CC       ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:19893491,
CC       ECO:0000269|PubMed:20675388}.
CC   -!- INTERACTION:
CC       P62973:- (xeno); NbExp=2; IntAct=EBI-1009256, EBI-16124826;
CC       Q80TQ2:Cyld; NbExp=3; IntAct=EBI-1009256, EBI-943859;
CC       P21146:GRK2 (xeno); NbExp=2; IntAct=EBI-1009256, EBI-1036401;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Perikaryon. Cell
CC       projection, dendrite. Cell projection, axon. Note=It is mainly
CC       cytoplasmic, where it is associated with microtubules.
CC   -!- TISSUE SPECIFICITY: Expressed in neurons of the cortex. Expressed
CC       in Purkinje cells. Detected in keratinocytes (at protein level).
CC       {ECO:0000269|PubMed:16933150, ECO:0000269|PubMed:19893491}.
CC   -!- PTM: Phosphorylated by AURKA. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. Its polyubiquitination however does not lead
CC       to its degradation (By similarity). {ECO:0000250}.
CC   -!- PTM: Sumoylated in vitro. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000305}.
DR   EMBL; AF006603; AAD09835.2; -; mRNA.
DR   EMBL; AL670169; CAM17240.1; -; Genomic_DNA.
DR   CCDS; CCDS40845.1; -.
DR   PIR; T13964; T13964.
DR   RefSeq; NP_001123888.1; NM_001130416.1.
DR   RefSeq; NP_034543.3; NM_010413.3.
DR   RefSeq; XP_006527630.1; XM_006527567.2.
DR   RefSeq; XP_017173877.1; XM_017318388.1.
DR   RefSeq; XP_017173878.1; XM_017318389.1.
DR   UniGene; Mm.29854; -.
DR   ProteinModelPortal; Q9Z2V5; -.
DR   SMR; Q9Z2V5; -.
DR   BioGrid; 200263; 41.
DR   DIP; DIP-36461N; -.
DR   IntAct; Q9Z2V5; 37.
DR   MINT; MINT-220628; -.
DR   STRING; 10090.ENSMUSP00000033501; -.
DR   BindingDB; Q9Z2V5; -.
DR   ChEMBL; CHEMBL2878; -.
DR   iPTMnet; Q9Z2V5; -.
DR   PhosphoSitePlus; Q9Z2V5; -.
DR   EPD; Q9Z2V5; -.
DR   MaxQB; Q9Z2V5; -.
DR   PaxDb; Q9Z2V5; -.
DR   PeptideAtlas; Q9Z2V5; -.
DR   PRIDE; Q9Z2V5; -.
DR   Ensembl; ENSMUST00000033501; ENSMUSP00000033501; ENSMUSG00000031161.
DR   Ensembl; ENSMUST00000115642; ENSMUSP00000111306; ENSMUSG00000031161.
DR   GeneID; 15185; -.
DR   KEGG; mmu:15185; -.
DR   UCSC; uc009snh.2; mouse.
DR   CTD; 10013; -.
DR   MGI; MGI:1333752; Hdac6.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00530000062809; -.
DR   HOGENOM; HOG000004769; -.
DR   HOVERGEN; HBG051894; -.
DR   InParanoid; Q9Z2V5; -.
DR   KO; K11407; -.
DR   OMA; QPHGFCI; -.
DR   OrthoDB; EOG091G0210; -.
DR   TreeFam; TF106173; -.
DR   BRENDA; 3.5.1.98; 3474.
DR   Reactome; R-MMU-3371511; HSF1 activation.
DR   Reactome; R-MMU-5617833; Cilium Assembly.
DR   PRO; PR:Q9Z2V5; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   Bgee; ENSMUSG00000031161; -.
DR   CleanEx; MM_HDAC6; -.
DR   ExpressionAtlas; Q9Z2V5; baseline and differential.
DR   Genevisible; Q9Z2V5; MM.
DR   GO; GO:0016235; C:aggresome; ISO:MGI.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:0005901; C:caveola; ISO:MGI.
DR   GO; GO:0044297; C:cell body; IDA:MGI.
DR   GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0030286; C:dynein complex; IEA:Ensembl.
DR   GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR   GO; GO:0016234; C:inclusion body; ISO:MGI.
DR   GO; GO:0005874; C:microtubule; ISO:MGI.
DR   GO; GO:0005875; C:microtubule associated complex; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0043234; C:protein complex; IPI:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR   GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
DR   GO; GO:0001047; F:core promoter binding; ISO:MGI.
DR   GO; GO:0070840; F:dynein complex binding; ISO:MGI.
DR   GO; GO:0004407; F:histone deacetylase activity; IDA:MGI.
DR   GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR   GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0051787; F:misfolded protein binding; ISO:MGI.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:MGI.
DR   GO; GO:0048156; F:tau protein binding; ISO:MGI.
DR   GO; GO:0042903; F:tubulin deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; IDA:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0070842; P:aggresome assembly; IGI:MGI.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR   GO; GO:0071218; P:cellular response to misfolded protein; IMP:MGI.
DR   GO; GO:0035967; P:cellular response to topologically incorrect protein; ISO:MGI.
DR   GO; GO:0048668; P:collateral sprouting; IMP:MGI.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; IMP:MGI.
DR   GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR   GO; GO:0070846; P:Hsp90 deacetylation; IMP:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; ISO:MGI.
DR   GO; GO:0032418; P:lysosome localization; ISO:MGI.
DR   GO; GO:0051646; P:mitochondrion localization; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR   GO; GO:0043242; P:negative regulation of protein complex disassembly; ISO:MGI.
DR   GO; GO:0045861; P:negative regulation of proteolysis; ISO:MGI.
DR   GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; ISO:MGI.
DR   GO; GO:0034983; P:peptidyl-lysine deacetylation; ISO:MGI.
DR   GO; GO:0070845; P:polyubiquitinated misfolded protein transport; ISO:MGI.
DR   GO; GO:0090035; P:positive regulation of chaperone-mediated protein complex assembly; ISO:MGI.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR   GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; ISO:MGI.
DR   GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0010870; P:positive regulation of receptor biosynthetic process; ISO:MGI.
DR   GO; GO:0009967; P:positive regulation of signal transduction; ISO:MGI.
DR   GO; GO:0043241; P:protein complex disassembly; IGI:MGI.
DR   GO; GO:0006476; P:protein deacetylation; IDA:MGI.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR   GO; GO:0006515; P:protein quality control by the ubiquitin-proteasome system; ISO:MGI.
DR   GO; GO:0070201; P:regulation of establishment of protein localization; IMP:MGI.
DR   GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
DR   GO; GO:0016241; P:regulation of macroautophagy; ISO:MGI.
DR   GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR   GO; GO:0010469; P:regulation of receptor activity; ISO:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0070848; P:response to growth factor; ISO:MGI.
DR   GO; GO:0051788; P:response to misfolded protein; ISO:MGI.
DR   GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR   GO; GO:0009636; P:response to toxic substance; ISO:MGI.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0090042; P:tubulin deacetylation; IDA:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:MGI.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:MGI.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.800.20; -; 2.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR10625; PTHR10625; 4.
DR   Pfam; PF00850; Hist_deacetyl; 2.
DR   Pfam; PF02148; zf-UBP; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF52768; SSF52768; 2.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell projection; Chromatin regulator;
KW   Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Methylation;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1149       Histone deacetylase 6.
FT                                /FTId=PRO_0000114704.
FT   ZN_FING    1065   1126       UBP-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00502}.
FT   REGION       87    403       Histone deacetylase 1.
FT   REGION      481    799       Histone deacetylase 2.
FT   REGION     1088   1090       Ubiquitin binding. {ECO:0000250}.
FT   REGION     1116   1123       Ubiquitin binding. {ECO:0000250}.
FT   COMPBIAS    455    460       Poly-Glu.
FT   ACT_SITE    215    215       1. {ECO:0000250}.
FT   ACT_SITE    610    610       2. {ECO:0000250}.
FT   METAL      1047   1047       Zinc 1. {ECO:0000250}.
FT   METAL      1049   1049       Zinc 1. {ECO:0000250}.
FT   METAL      1067   1067       Zinc 3. {ECO:0000250}.
FT   METAL      1070   1070       Zinc 3. {ECO:0000250}.
FT   METAL      1079   1079       Zinc 2. {ECO:0000250}.
FT   METAL      1082   1082       Zinc 2. {ECO:0000250}.
FT   METAL      1087   1087       Zinc 3. {ECO:0000250}.
FT   METAL      1094   1094       Zinc 3. {ECO:0000250}.
FT   METAL      1098   1098       Zinc 2. {ECO:0000250}.
FT   METAL      1104   1104       Zinc 2. {ECO:0000250}.
FT   METAL      1117   1117       Zinc 1. {ECO:0000250}.
FT   METAL      1120   1120       Zinc 1. {ECO:0000250}.
FT   MOD_RES      21     21       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES      32     32       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES      43     43       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     958    958       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9UBN7}.
FT   MOD_RES     961    961       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9UBN7}.
FT   MOD_RES     967    967       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9UBN7}.
FT   MOD_RES     971    971       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9UBN7}.
FT   MOD_RES     975    975       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UBN7}.
FT   MOD_RES    1148   1148       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CONFLICT    133    133       R -> W (in Ref. 1; AAD09835).
FT                                {ECO:0000305}.
FT   CONFLICT    394    394       V -> I (in Ref. 1; AAD09835).
FT                                {ECO:0000305}.
FT   CONFLICT    421    421       T -> I (in Ref. 1; AAD09835).
FT                                {ECO:0000305}.
FT   CONFLICT    532    532       D -> G (in Ref. 1; AAD09835).
FT                                {ECO:0000305}.
FT   CONFLICT    836    836       M -> S (in Ref. 1; AAD09835).
FT                                {ECO:0000305}.
FT   CONFLICT    851    851       I -> V (in Ref. 1; AAD09835).
FT                                {ECO:0000305}.
FT   CONFLICT   1126   1127       HE -> QD (in Ref. 1; AAD09835).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1149 AA;  125787 MW;  D5F73BA3F79AF520 CRC64;
     MTSTGQDSST RQRKSRHNPQ SPLQESSATL KRGGKKCAVP HSSPNLAEVK KKGKMKKLSQ
     PAEEDLVVGL QGLDLNPETR VPVGTGLVFD EQLNDFHCLW DDSFPESPER LHAIREQLIL
     EGLLGRCVSF QARFAEKEEL MLVHSLEYID LMETTQYMNE GELRVLAETY DSVYLHPNSY
     SCACLATGSV LRLVDALMGA EIRNGMAVIR PPGHHAQHNL MDGYCMFNHL AVAARYAQKK
     HRIQRVLIVD WDVHHGQGTQ FIFDQDPSVL YFSIHRYEHG RFWPHLKASN WSTIGFGQGQ
     GYTINVPWNQ TGMRDADYIA AFLHILLPVA SEFQPQLVLV AAGFDALHGD PKGEMAATPA
     GFAHLTHLLM GLAGGKLILS LEGGYNLRAL AKGVSASLHT LLGDPCPMLE SCVVPCASAQ
     TSIYCTLEAL EPFWEVLERS VETQEEDEVE EAVLEEEEEE GGWEATALPM DTWPLLQNRT
     GLVYDEKMMS HCNLWDNHHP ETPQRILRIM CHLEEVGLAA RCLILPARPA LDSELLTCHS
     AEYVEHLRTT EKMKTRDLHR EGANFDSIYI CPSTFACAKL ATGAACRLVE AVLSGEVLNG
     IAVVRPPGHH AEPNAACGFC FFNSVAVAAR HAQIIAGRAL RILIVDWDVH HGNGTQHIFE
     DDPSVLYVSL HRYDRGTFFP MGDEGASSQV GRDAGIGFTV NVPWNGPRMG DADYLAAWHR
     LVLPIAYEFN PELVLISAGF DAAQGDPLGG CQVTPEGYAH LTHLLMGLAG GRIILILEGG
     YNLASISESM AACTHSLLGD PPPQLTLLRP PQSGALVSIS EVIQVHRKYW RSLRLMKMED
     KEECSSSRLV IKKLPPTASP VSAKEMTTPK GKVPEESVRK TIAALPGKES TLGQAKSKMA
     KAVLAQGQSS EQAAKGTTLD LATSKETVGG ATTDLWASAA APENFPNQTT SVEALGETEP
     TPPASHTNKQ TTGASPLQGV TAQQSLQLGV LSTLELSREA EEAHDSEEGL LGEAAGGQDM
     NSLMLTQGFG DFNTQDVFYA VTPLSWCPHL MAVCPIPAAG LDVSQPCKTC GTVQENWVCL
     TCYQVYCSRY VNAHMVCHHE ASEHPLVLSC VDLSTWCYVC QAYVHHEDLQ DVKNAAHQNK
     FGEDMPHSH
//
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