RPC4_HUMAN
ID RPC4_HUMAN Reviewed; 398 AA.
AC P05423; Q6FI28; Q9BPV7; Q9BPZ1; Q9BXB3;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC4;
DE Short=RNA polymerase III subunit C4;
DE AltName: Full=DNA-directed RNA polymerase III subunit D;
DE AltName: Full=Protein BN51;
DE AltName: Full=RNA polymerase III 47 kDa subunit;
DE AltName: Full=RPC53 homolog;
GN Name=POLR3D; Synonyms=BN51, BN51T;
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].
RX PubMed=3683386; DOI=10.1128/mcb.7.10.3386-3393.1987;
RA Ittmann M., Greco A., Basilico C.;
RT "Isolation of the human gene that complements a temperature-sensitive cell
RT cycle mutation in BHK cells.";
RL Mol. Cell. Biol. 7:3386-3393(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE RNA POL III COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH POLR3E.
RX PubMed=12391170; DOI=10.1128/mcb.22.22.8044-8055.2002;
RA Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.;
RT "Characterization of human RNA polymerase III identifies orthologues for
RT Saccharomyces cerevisiae RNA polymerase III subunits.";
RL Mol. Cell. Biol. 22:8044-8055(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Lymph;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-50.
RX PubMed=11279001; DOI=10.1074/jbc.m100088200;
RA Chong S.S., Hu P., Hernandez N.;
RT "Reconstitution of transcription from the human U6 small nuclear RNA
RT promoter with eight recombinant polypeptides and a partially purified RNA
RT polymerase III complex.";
RL J. Biol. Chem. 276:20727-20734(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RA Ittmann M.;
RT "Promoter structure and cell cycle control of the BN51 cell cycle gene,
RT which encodes a subunit of RNA polymerase III.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=19631370; DOI=10.1016/j.cell.2009.06.015;
RA Chiu Y.-H., Macmillan J.B., Chen Z.J.;
RT "RNA polymerase III detects cytosolic DNA and induces type I interferons
RT through the RIG-I pathway.";
RL Cell 138:576-591(2009).
RN [8]
RP FUNCTION.
RX PubMed=19609254; DOI=10.1038/ni.1779;
RA Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A.,
RA Hornung V.;
RT "RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA
RT polymerase III-transcribed RNA intermediate.";
RL Nat. Immunol. 10:1065-1072(2009).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP 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).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-95; ARG-97 AND ARG-99, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA 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).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-141; LYS-206; LYS-220 AND
RP LYS-302, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-141; LYS-220; LYS-285 AND
RP LYS-302, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-141; LYS-220; LYS-302 AND
RP LYS-396, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-78; LYS-141; LYS-152;
RP LYS-160; LYS-190; LYS-199; LYS-206; LYS-220; LYS-285; LYS-302; LYS-310 AND
RP LYS-396, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Specific peripheric component of RNA polymerase III which synthesizes
CC small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and
CC limiting infection by intracellular bacteria and DNA viruses. Acts as
CC nuclear and cytosolic DNA sensor involved in innate immune response.
CC Can sense non-self dsDNA that serves as template for transcription into
CC dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-
CC Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-
CC B through the RIG-I pathway (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits (By similarity). Interacts with POLR3E/RPC5.
CC {ECO:0000250, ECO:0000269|PubMed:12391170}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the eukaryotic RPC4/POLR3D RNA polymerase
CC subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC000516; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BC003039; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M17754; AAA51838.1; -; mRNA.
DR EMBL; AY092086; AAM18216.1; -; mRNA.
DR EMBL; CR536509; CAG38747.1; -; mRNA.
DR EMBL; CR541803; CAG46602.1; -; mRNA.
DR EMBL; BC000516; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC003039; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC002603; AAH02603.1; -; mRNA.
DR EMBL; BC004484; AAH04484.1; -; mRNA.
DR EMBL; AF346574; AAK15371.1; -; mRNA.
DR EMBL; L15301; AAA72377.1; -; Genomic_DNA.
DR CCDS; CCDS34858.1; -.
DR PIR; A43700; A43700.
DR RefSeq; NP_001713.2; NM_001722.2.
DR PDB; 7A6H; EM; 3.30 A; N=1-398.
DR PDB; 7AE1; EM; 2.80 A; N=1-398.
DR PDB; 7AE3; EM; 3.10 A; N=1-398.
DR PDB; 7AEA; EM; 3.40 A; N=1-398.
DR PDB; 7AST; EM; 4.00 A; L=1-398.
DR PDB; 7D58; EM; 2.90 A; N=1-398.
DR PDB; 7D59; EM; 3.10 A; N=1-398.
DR PDB; 7DN3; EM; 3.50 A; N=1-398.
DR PDB; 7DU2; EM; 3.35 A; N=1-398.
DR PDB; 7FJI; EM; 3.60 A; N=1-398.
DR PDB; 7FJJ; EM; 3.60 A; N=1-398.
DR PDBsum; 7A6H; -.
DR PDBsum; 7AE1; -.
DR PDBsum; 7AE3; -.
DR PDBsum; 7AEA; -.
DR PDBsum; 7AST; -.
DR PDBsum; 7D58; -.
DR PDBsum; 7D59; -.
DR PDBsum; 7DN3; -.
DR PDBsum; 7DU2; -.
DR PDBsum; 7FJI; -.
DR PDBsum; 7FJJ; -.
DR AlphaFoldDB; P05423; -.
DR SMR; P05423; -.
DR BioGRID; 107129; 76.
DR DIP; DIP-56155N; -.
DR IntAct; P05423; 38.
DR MINT; P05423; -.
DR STRING; 9606.ENSP00000380904; -.
DR iPTMnet; P05423; -.
DR PhosphoSitePlus; P05423; -.
DR SwissPalm; P05423; -.
DR BioMuta; POLR3D; -.
DR DMDM; 29429159; -.
DR EPD; P05423; -.
DR jPOST; P05423; -.
DR MassIVE; P05423; -.
DR MaxQB; P05423; -.
DR PaxDb; P05423; -.
DR PeptideAtlas; P05423; -.
DR PRIDE; P05423; -.
DR ProteomicsDB; 51838; -.
DR Antibodypedia; 22571; 187 antibodies from 28 providers.
DR DNASU; 661; -.
DR Ensembl; ENST00000306433.9; ENSP00000303088.4; ENSG00000168495.13.
DR Ensembl; ENST00000397802.8; ENSP00000380904.3; ENSG00000168495.13.
DR GeneID; 661; -.
DR KEGG; hsa:661; -.
DR MANE-Select; ENST00000306433.9; ENSP00000303088.4; NM_001722.3; NP_001713.2.
DR UCSC; uc003xbl.4; human.
DR CTD; 661; -.
DR DisGeNET; 661; -.
DR GeneCards; POLR3D; -.
DR HGNC; HGNC:1080; POLR3D.
DR HPA; ENSG00000168495; Low tissue specificity.
DR MIM; 187280; gene.
DR neXtProt; NX_P05423; -.
DR OpenTargets; ENSG00000168495; -.
DR PharmGKB; PA25390; -.
DR VEuPathDB; HostDB:ENSG00000168495; -.
DR eggNOG; KOG3122; Eukaryota.
DR GeneTree; ENSGT00390000013948; -.
DR HOGENOM; CLU_042288_0_0_1; -.
DR InParanoid; P05423; -.
DR OMA; QAENTCT; -.
DR OrthoDB; 1381418at2759; -.
DR PhylomeDB; P05423; -.
DR PathwayCommons; P05423; -.
DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
DR Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR SignaLink; P05423; -.
DR SIGNOR; P05423; -.
DR BioGRID-ORCS; 661; 405 hits in 1084 CRISPR screens.
DR ChiTaRS; POLR3D; human.
DR GeneWiki; POLR3D; -.
DR GenomeRNAi; 661; -.
DR Pharos; P05423; Tbio.
DR PRO; PR:P05423; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P05423; protein.
DR Bgee; ENSG00000168495; Expressed in sural nerve and 135 other tissues.
DR ExpressionAtlas; P05423; baseline and differential.
DR Genevisible; P05423; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045089; P:positive regulation of innate immune response; IDA:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:UniProtKB.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IEA:InterPro.
DR InterPro; IPR007811; RPC4.
DR PANTHER; PTHR13408; PTHR13408; 1.
DR Pfam; PF05132; RNA_pol_Rpc4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antiviral defense; DNA-directed RNA polymerase;
KW Immunity; Innate immunity; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..398
FT /note="DNA-directed RNA polymerase III subunit RPC4"
FT /id="PRO_0000073967"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 97
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 99
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 190
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 206
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CONFLICT 9..18
FT /note="EPSTPGGPRP -> RPARQGPDL (in Ref. 1; AAA51838)"
FT /evidence="ECO:0000305"
FT CONFLICT 9..12
FT /note="EPST -> RPAR (in Ref. 6; AAA72377)"
FT /evidence="ECO:0000305"
FT CONFLICT 26..40
FT /note="LIGRRPAPPLTPGRL -> SSGGGGLPSPPAV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="G -> R (in Ref. 1; AAA51838)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="K -> R (in Ref. 2; AAM18216)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="P -> L (in Ref. 2; AAM18216)"
FT /evidence="ECO:0000305"
FT TURN 37..41
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 356..364
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 367..387
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 389..395
FT /evidence="ECO:0007829|PDB:7AE1"
SQ SEQUENCE 398 AA; 44396 MW; CD8AFF3257B78410 CRC64;
MSEGNAAGEP STPGGPRPLL TGARGLIGRR PAPPLTPGRL PSIRSRDLTL GGVKKKTFTP
NIISRKIKEE PKEEVTVKKE KRERDRDRQR EGHGRGRGRP EVIQSHSIFE QGPAEMMKKK
GNWDKTVDVS DMGPSHIINI KKEKRETDEE TKQILRMLEK DDFLDDPGLR NDTRNMPVQL
PLAHSGWLFK EENDEPDVKP WLAGPKEEDM EVDIPAVKVK EEPRDEEEEA KMKAPPKAAR
KTPGLPKDVS VAELLRELSL TKEEELLFLQ LPDTLPGQPP TQDIKPIKTE VQGEDGQVVL
IKQEKDREAK LAENACTLAD LTEGQVGKLL IRKSGRVQLL LGKVTLDVTM GTACSFLQEL
VSVGLGDSRT GEMTVLGHVK HKLVCSPDFE SLLDHKHR
