PSME4_HUMAN
ID PSME4_HUMAN Reviewed; 1843 AA.
AC Q14997; Q1XBG4; Q1XBG5; Q1XBG6; Q2M1Z0; Q6IPR2; Q86XF8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Proteasome activator complex subunit 4;
DE AltName: Full=Proteasome activator PA200;
GN Name=PSME4; Synonyms=KIAA0077;
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] (ISOFORMS 2 AND 3), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1-1210 (ISOFORM 1).
RA Blickwedehl J., McEvoy S., Wong I., Kousis P., Cresswell P., Liang P.,
RA Bangia N.;
RT "Proteasomes and Proteasome Activator 200kD (PA200) accumulate on chromatin
RT in response to ionizing radiation.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 104-1843 (ISOFORM 1).
RC TISSUE=Brain, Mammary gland, and Skeletal muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-1843 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [4]
RP IDENTIFICATION, FUNCTION, SUBUNIT, INTERACTION WITH PROTEASOMES 20S AND
RP 26S, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=12093752; DOI=10.1093/emboj/cdf333;
RA Ustrell V., Hoffman L., Pratt G., Rechsteiner M.;
RT "PA200, a nuclear proteasome activator involved in DNA repair.";
RL EMBO J. 21:3516-3525(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP FUNCTION.
RX PubMed=18845680; DOI=10.1073/pnas.0803145105;
RA Blickwedehl J., Agarwal M., Seong C., Pandita R.K., Melendy T., Sung P.,
RA Pandita T.K., Bangia N.;
RT "Role for proteasome activator PA200 and postglutamyl proteasome activity
RT in genomic stability.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:16165-16170(2008).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=22550082; DOI=10.1158/1541-7786.mcr-11-0493-t;
RA Blickwedehl J., Olejniczak S., Cummings R., Sarvaiya N., Mantilla A.,
RA Chanan-Khan A., Pandita T.K., Schmidt M., Thompson C.B., Bangia N.;
RT "The proteasome activator PA200 regulates tumor cell responsiveness to
RT glutamine and resistance to ionizing radiation.";
RL Mol. Cancer Res. 10:937-944(2012).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF 1716-ASN-PHE-1717.
RX PubMed=23706739; DOI=10.1016/j.cell.2013.04.032;
RA Qian M.X., Pang Y., Liu C.H., Haratake K., Du B.Y., Ji D.Y., Wang G.F.,
RA Zhu Q.Q., Song W., Yu Y., Zhang X.X., Huang H.T., Miao S., Chen L.B.,
RA Zhang Z.H., Liang Y.N., Liu S., Cha H., Yang D., Zhai Y., Komatsu T.,
RA Tsuruta F., Li H., Cao C., Li W., Li G.H., Cheng Y., Chiba T., Wang L.,
RA Goldberg A.L., Shen Y., Qiu X.B.;
RT "Acetylation-mediated proteasomal degradation of core histones during DNA
RT repair and spermatogenesis.";
RL Cell 153:1012-1024(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1121; SER-1614 AND SER-1746,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Associated component of the proteasome that specifically
CC recognizes acetylated histones and promotes ATP- and ubiquitin-
CC independent degradation of core histones during spermatogenesis and DNA
CC damage response. Recognizes and binds acetylated histones via its
CC bromodomain-like (BRDL) region and activates the proteasome by opening
CC the gated channel for substrate entry. Binds to the core proteasome via
CC its C-terminus, which occupies the same binding sites as the
CC proteasomal ATPases, opening the closed structure of the proteasome via
CC an active gating mechanism. Component of the spermatoproteasome, a form
CC of the proteasome specifically found in testis: binds to acetylated
CC histones and promotes degradation of histones, thereby participating
CC actively to the exchange of histones during spermatogenesis. Also
CC involved in DNA damage response in somatic cells, by promoting
CC degradation of histones following DNA double-strand breaks.
CC {ECO:0000269|PubMed:12093752, ECO:0000269|PubMed:18845680,
CC ECO:0000269|PubMed:22550082, ECO:0000269|PubMed:23706739}.
CC -!- SUBUNIT: Homodimer. Interacts with the 20S and 26S proteasomes.
CC Component of the spermatoproteasome, a form of the proteasome
CC specifically found in testis. {ECO:0000269|PubMed:12093752}.
CC -!- INTERACTION:
CC Q14997; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-1236916, EBI-739580;
CC Q14997; Q86Y26: NUTM1; NbExp=3; IntAct=EBI-1236916, EBI-10178410;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:12093752}. Nucleus speckle {ECO:0000250}.
CC Note=Found in nuclear foci following treatment with ionizing radiation,
CC but not with ultraviolet irradiation or H(2)O(2).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q14997-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14997-2; Sequence=VSP_023878;
CC Name=3;
CC IsoId=Q14997-3; Sequence=VSP_023877, VSP_023879;
CC Name=4;
CC IsoId=Q14997-4; Sequence=VSP_023876;
CC -!- DOMAIN: The bromodomain-like (BRDL) region specifically recognizes and
CC binds acetylated histones. {ECO:0000269|PubMed:23706739}.
CC -!- SIMILARITY: Belongs to the BLM10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI12170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI13669.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY894754; AAX83869.1; -; mRNA.
DR EMBL; AY894755; AAX83870.1; -; mRNA.
DR EMBL; AY894756; AAX83871.1; -; mRNA.
DR EMBL; BC043602; AAH43602.1; -; mRNA.
DR EMBL; BC071768; AAH71768.1; -; mRNA.
DR EMBL; BC112169; AAI12170.1; ALT_INIT; mRNA.
DR EMBL; BC113668; AAI13669.1; ALT_INIT; mRNA.
DR EMBL; D38521; BAA07526.1; -; mRNA.
DR CCDS; CCDS33197.2; -. [Q14997-1]
DR RefSeq; NP_055429.2; NM_014614.2. [Q14997-1]
DR PDB; 6KWX; EM; 3.75 A; A=1-1843.
DR PDB; 6KWY; EM; 2.72 A; c=1-1843.
DR PDB; 6REY; EM; 3.00 A; c/d=1-1843.
DR PDBsum; 6KWX; -.
DR PDBsum; 6KWY; -.
DR PDBsum; 6REY; -.
DR AlphaFoldDB; Q14997; -.
DR SMR; Q14997; -.
DR BioGRID; 116807; 64.
DR DIP; DIP-38203N; -.
DR IntAct; Q14997; 32.
DR MINT; Q14997; -.
DR STRING; 9606.ENSP00000384211; -.
DR GlyGen; Q14997; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14997; -.
DR PhosphoSitePlus; Q14997; -.
DR BioMuta; PSME4; -.
DR DMDM; 134034993; -.
DR EPD; Q14997; -.
DR jPOST; Q14997; -.
DR MassIVE; Q14997; -.
DR MaxQB; Q14997; -.
DR PaxDb; Q14997; -.
DR PeptideAtlas; Q14997; -.
DR PRIDE; Q14997; -.
DR ProteomicsDB; 60286; -. [Q14997-1]
DR ProteomicsDB; 60287; -. [Q14997-2]
DR ProteomicsDB; 60288; -. [Q14997-3]
DR ProteomicsDB; 60289; -. [Q14997-4]
DR Antibodypedia; 30226; 110 antibodies from 22 providers.
DR DNASU; 23198; -.
DR Ensembl; ENST00000404125.6; ENSP00000384211.1; ENSG00000068878.15. [Q14997-1]
DR GeneID; 23198; -.
DR KEGG; hsa:23198; -.
DR MANE-Select; ENST00000404125.6; ENSP00000384211.1; NM_014614.3; NP_055429.2.
DR UCSC; uc002rxp.2; human. [Q14997-1]
DR CTD; 23198; -.
DR DisGeNET; 23198; -.
DR GeneCards; PSME4; -.
DR HGNC; HGNC:20635; PSME4.
DR HPA; ENSG00000068878; Tissue enhanced (skeletal).
DR MIM; 607705; gene.
DR neXtProt; NX_Q14997; -.
DR OpenTargets; ENSG00000068878; -.
DR PharmGKB; PA134872587; -.
DR VEuPathDB; HostDB:ENSG00000068878; -.
DR eggNOG; KOG1851; Eukaryota.
DR GeneTree; ENSGT00390000011433; -.
DR HOGENOM; CLU_000772_2_0_1; -.
DR InParanoid; Q14997; -.
DR OMA; GKDWSDE; -.
DR OrthoDB; 83617at2759; -.
DR PhylomeDB; Q14997; -.
DR TreeFam; TF106237; -.
DR PathwayCommons; Q14997; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q14997; -.
DR BioGRID-ORCS; 23198; 18 hits in 1086 CRISPR screens.
DR ChiTaRS; PSME4; human.
DR GeneWiki; PSME4; -.
DR GenomeRNAi; 23198; -.
DR Pharos; Q14997; Tbio.
DR PRO; PR:Q14997; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q14997; protein.
DR Bgee; ENSG00000068878; Expressed in sperm and 203 other tissues.
DR ExpressionAtlas; Q14997; baseline and differential.
DR Genevisible; Q14997; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0016504; F:peptidase activator activity; ISS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032430; Blm10_mid.
DR InterPro; IPR035309; PSME4.
DR InterPro; IPR021843; PSME4_C.
DR PANTHER; PTHR32170; PTHR32170; 1.
DR Pfam; PF16507; BLM10_mid; 1.
DR Pfam; PF11919; DUF3437; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1..1843
FT /note="Proteasome activator complex subunit 4"
FT /id="PRO_0000280718"
FT REPEAT 475..519
FT /note="HEAT 1"
FT REPEAT 998..1037
FT /note="HEAT 2"
FT REPEAT 1179..1217
FT /note="HEAT 3"
FT REPEAT 1354..1392
FT /note="HEAT 4"
FT REPEAT 1636..1674
FT /note="HEAT 5"
FT REPEAT 1680..1718
FT /note="HEAT 6"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1650..1738
FT /note="Bromodomain-like (BRDL)"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1628
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023876"
FT VAR_SEQ 1..856
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023877"
FT VAR_SEQ 1..625
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023878"
FT VAR_SEQ 857..871
FT /note="YDLSRENHREVIATV -> MGENLAKKIMFFLLI (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023879"
FT VARIANT 872
FT /note="I -> V (in dbSNP:rs2302878)"
FT /id="VAR_031189"
FT VARIANT 1371
FT /note="S -> T (in dbSNP:rs805408)"
FT /id="VAR_031190"
FT VARIANT 1825
FT /note="T -> A (in dbSNP:rs35903236)"
FT /id="VAR_059755"
FT MUTAGEN 1716..1717
FT /note="NF->TS: Abolihes binding to acetylated histones."
FT /evidence="ECO:0000269|PubMed:23706739"
FT CONFLICT 217
FT /note="F -> V (in Ref. 1; AAX83871)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="C -> R (in Ref. 1; AAX83871)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="N -> S (in Ref. 1; AAX83871)"
FT /evidence="ECO:0000305"
FT CONFLICT 1401
FT /note="L -> F (in Ref. 2; AAH43602)"
FT /evidence="ECO:0000305"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 43..65
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 250..265
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:6REY"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 350..371
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 390..408
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 415..427
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 429..438
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 451..461
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 464..467
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 481..487
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 497..507
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 508..513
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:6REY"
FT HELIX 531..537
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 540..543
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 549..559
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 577..583
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 584..595
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 599..615
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 623..637
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 639..657
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 661..665
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 672..683
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 689..691
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 696..699
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 702..705
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 711..713
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 715..729
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 743..746
FT /evidence="ECO:0007829|PDB:6REY"
FT TURN 747..749
FT /evidence="ECO:0007829|PDB:6REY"
FT HELIX 752..754
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 774..787
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 789..799
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 807..823
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 825..827
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 837..839
FT /evidence="ECO:0007829|PDB:6REY"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 864..882
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 889..900
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 904..906
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 908..924
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 932..934
FT /evidence="ECO:0007829|PDB:6REY"
FT HELIX 937..953
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 963..975
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 976..978
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 980..994
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1001..1003
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1005..1008
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1009..1012
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1014..1016
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1021..1032
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1035..1037
FT /evidence="ECO:0007829|PDB:6REY"
FT STRAND 1040..1042
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1044..1046
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1049..1058
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1062..1064
FT /evidence="ECO:0007829|PDB:6REY"
FT HELIX 1070..1086
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1100..1105
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1122..1126
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1127..1135
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1138..1154
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1161..1172
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1177..1179
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1183..1191
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1198..1214
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1221..1224
FT /evidence="ECO:0007829|PDB:6REY"
FT TURN 1226..1228
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1240..1242
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1244..1246
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1247..1249
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1260..1264
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1271..1273
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1281..1286
FT /evidence="ECO:0007829|PDB:6REY"
FT TURN 1289..1291
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1299..1302
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1306..1313
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1316..1325
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1332..1334
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1339..1351
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1356..1367
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1374..1389
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1390..1392
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1395..1414
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1418..1420
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1421..1431
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1433..1435
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1437..1439
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1442..1447
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1451..1453
FT /evidence="ECO:0007829|PDB:6REY"
FT HELIX 1460..1474
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1475..1477
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1480..1490
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1491..1493
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1494..1496
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1499..1512
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1530..1540
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1542..1544
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1568..1584
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1585..1587
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1588..1590
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1596..1599
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1600..1604
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1616..1618
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1619..1630
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1636..1638
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1639..1648
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1651..1653
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1655..1670
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1673..1677
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1680..1693
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1699..1714
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1722..1732
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1742..1744
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1756..1771
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1781..1789
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 1792..1794
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1798..1812
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1817..1820
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1821..1823
FT /evidence="ECO:0007829|PDB:6KWY"
FT HELIX 1826..1833
FT /evidence="ECO:0007829|PDB:6KWY"
FT TURN 1840..1842
FT /evidence="ECO:0007829|PDB:6REY"
SQ SEQUENCE 1843 AA; 211334 MW; 2D2C3A594E4FA4E7 CRC64;
MEPAERAGVG EPPEPGGRPE PGPRGFVPQK EIVYNKLLPY AERLDAESDL QLAQIKCNLG
RAVQLQELWP GGLFWTRKLS TYIRLYGRKF SKEDHVLFIK LLYELVSIPK LEISMMQGFA
RLLINLLKKK ELLSRADLEL PWRPLYDMVE RILYSKTEHL GLNWFPNSVE NILKTLVKSC
RPYFPADATA EMLEEWRPLM CPFDVTMQKA ITYFEIFLPT SLPPELHHKG FKLWFDELIG
LWVSVQNLPQ WEGQLVNLFA RLATDNIGYI DWDPYVPKIF TRILRSLNLP VGSSQVLVPR
FLTNAYDIGH AVIWITAMMG GPSKLVQKHL AGLFNSITSF YHPSNNGRWL NKLMKLLQRL
PNSVVRRLHR ERYKKPSWLT PVPDSHKLTD QDVTDFVQCI IQPVLLAMFS KTGSLEAAQA
LQNLALMRPE LVIPPVLERT YPALETLTEP HQLTATLSCV IGVARSLVSG GRWFPEGPTH
MLPLLMRALP GVDPNDFSKC MITFQFIATF STLVPLVDCS SVLQERNDLT EVERELCSAT
AEFEDFVLQF MDRCFGLIES STLEQTREET ETEKMTHLES LVELGLSSTF STILTQCSKE
IFMVALQKVF NFSTSHIFET RVAGRMVADM CRAAVKCCPE ESLKLFVPHC CSVITQLTMN
DDVLNDEELD KELLWNLQLL SEITRVDGRK LLLYREQLVK ILQRTLHLTC KQGYTLSCNL
LHHLLRSTTL IYPTEYCSVP GGFDKPPSEY FPIKDWGKPG DLWNLGIQWH VPSSEEVSFA
FYLLDSFLQP ELVKLQHCGD GKLEMSRDDI LQSLTIVHNC LIGSGNLLPP LKGEPVTNLV
PSMVSLEETK LYTGLEYDLS RENHREVIAT VIRKLLNHIL DNSEDDTKSL FLIIKIIGDL
LQFQGSHKHE FDSRWKSFNL VKKSMENRLH GKKQHIRALL IDRVMLQHEL RTLTVEGCEY
KKIHQDMIRD LLRLSTSSYS QVRNKAQQTF FAALGAYNFC CRDIIPLVLE FLRPDRQGVT
QQQFKGALYC LLGNHSGVCL ANLHDWDCIV QTWPAIVSSG LSQAMSLEKP SIVRLFDDLA
EKIHRQYETI GLDFTIPKSC VEIAELLQQS KNPSINQILL SPEKIKEGIK RQQEKNADAL
RNYENLVDTL LDGVEQRNLP WKFEHIGIGL LSLLLRDDRV LPLRAIRFFV ENLNHDAIVV
RKMAISAVAG ILKQLKRTHK KLTINPCEIS GCPKPTQIIA GDRPDNHWLH YDSKTIPRTK
KEWESSCFVE KTHWGYYTWP KNMVVYAGVE EQPKLGRSRE DMTEAEQIIF DHFSDPKFVE
QLITFLSLED RKGKDKFNPR RFCLFKGIFR NFDDAFLPVL KPHLEHLVAD SHESTQRCVA
EIIAGLIRGS KHWTFEKVEK LWELLCPLLR TALSNITVET YNDWGACIAT SCESRDPRKL
HWLFELLLES PLSGEGGSFV DACRLYVLQG GLAQQEWRVP ELLHRLLKYL EPKLTQVYKN
VRERIGSVLT YIFMIDVSLP NTTPTISPHV PEFTARILEK LKPLMDVDEE IQNHVMEENG
IGEEDERTQG IKLLKTILKW LMASAGRSFS TAVTEQLQLL PLFFKIAPVE NDNSYDELKR
DAKLCLSLMS QGLLYPHQVP LVLQVLKQTA RSSSWHARYT VLTYLQTMVF YNLFIFLNNE
DAVKDIRWLV ISLLEDEQLE VREMAATTLS GLLQCNFLTM DSPMQIHFEQ LCKTKLPKKR
KRDPGSVGDT IPSAELVKRH AGVLGLGACV LSSPYDVPTW MPQLLMNLSA HLNDPQPIEM
TVKKTLSNFR RTHHDNWQEH KQQFTDDQLL VLTDLLVSPC YYA
