RPA49_HUMAN
ID RPA49_HUMAN Reviewed; 419 AA.
AC Q9GZS1; Q5VZT3; Q8NBA9; Q96L20;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA49;
DE Short=RNA polymerase I subunit A49;
DE AltName: Full=DNA-directed RNA polymerase I subunit E;
DE AltName: Full=RNA polymerase I-associated factor 1;
DE AltName: Full=RNA polymerase I-associated factor 53 {ECO:0000303|PubMed:24207024};
GN Name=POLR1E; Synonyms=PAF53 {ECO:0000303|PubMed:24207024}, PRAF1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LYS-383.
RC TISSUE=Cervix, and Lung;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [6]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=16809778; DOI=10.1128/mcb.00230-06;
RA Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J.,
RA Zomerdijk J.C.B.M.;
RT "RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation
RT of transcription by upstream binding factor.";
RL Mol. Cell. Biol. 26:5436-5448(2006).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 ASSOCIATION WITH THE RNA POLYMERASE I COMPLEX, AND INTERACTION WITH PWP1.
RX PubMed=29065309; DOI=10.1016/j.devcel.2017.09.022;
RA Liu Y., Mattila J., Ventelae S., Yadav L., Zhang W., Lamichane N.,
RA Sundstroem J., Kauko O., Grenman R., Varjosalo M., Westermarck J.,
RA Hietakangas V.;
RT "PWP1 Mediates Nutrient-Dependent Growth Control through Nucleolar
RT Regulation of Ribosomal Gene Expression.";
RL Dev. Cell 43:240-252(2017).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-373, AND MUTAGENESIS OF
RP LYS-373.
RX PubMed=24207024; DOI=10.1016/j.molcel.2013.10.010;
RA Chen S., Seiler J., Santiago-Reichelt M., Felbel K., Grummt I., Voit R.;
RT "Repression of RNA polymerase I upon stress is caused by inhibition of RNA-
RT dependent deacetylation of PAF53 by SIRT7.";
RL Mol. Cell 52:303-313(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase I which synthesizes ribosomal RNA
CC precursors (PubMed:24207024). Appears to be involved in the formation
CC of the initiation complex at the promoter by mediating the interaction
CC between Pol I and UBTF/UBF (PubMed:24207024).
CC {ECO:0000269|PubMed:24207024}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits (PubMed:16809778, PubMed:29065309). Interacts
CC with POLR1G (By similarity). Also binds UBTF/UBF (By similarity).
CC Interacts with PWP1 (PubMed:29065309). {ECO:0000250|UniProtKB:Q8K202,
CC ECO:0000269|PubMed:16809778, ECO:0000269|PubMed:29065309}.
CC -!- INTERACTION:
CC Q9GZS1; Q92876: KLK6; NbExp=3; IntAct=EBI-359458, EBI-2432309;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:24207024}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q9GZS1-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9GZS1-1; Sequence=VSP_059915;
CC -!- PTM: Acetylated at Lys-373 by CREBBP/CBP, leading to decreased RNA
CC polymerase I transcription (PubMed:24207024). In normal conditions,
CC deacetylated by SIRT7, promoting the association of RNA polymerase I
CC with the rDNA promoter region and coding region (PubMed:24207024). In
CC response to stress, SIRT7 is released from nucleoli leading to
CC hyperacetylation of POLR1E/PAF53 and decreased association of RNA
CC polymerase I with the rDNA promoter region (PubMed:24207024).
CC {ECO:0000269|PubMed:24207024}.
CC -!- MISCELLANEOUS: [Isoform 1]: Dubious isoform produced through intron
CC retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPA49/POLR1E RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; AK023452; BAB14579.1; -; mRNA.
DR EMBL; AK024032; BAB14791.1; -; mRNA.
DR EMBL; AK091294; BAC03629.1; -; mRNA.
DR EMBL; CR457313; CAG33594.1; -; mRNA.
DR EMBL; AL158156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001337; AAH01337.1; -; mRNA.
DR EMBL; BC014331; AAH14331.1; -; mRNA.
DR CCDS; CCDS6611.1; -. [Q9GZS1-2]
DR RefSeq; NP_001269695.1; NM_001282766.1.
DR RefSeq; NP_071935.1; NM_022490.2. [Q9GZS1-2]
DR RefSeq; XP_005251604.1; XM_005251547.2.
DR PDB; 7OB9; EM; 2.70 A; M=1-419.
DR PDB; 7OBA; EM; 3.10 A; M=1-419.
DR PDB; 7OBB; EM; 3.30 A; M=1-419.
DR PDB; 7VBA; EM; 2.89 A; M=1-419.
DR PDB; 7VBB; EM; 2.81 A; M=1-419.
DR PDB; 7VBC; EM; 3.01 A; M=1-419.
DR PDBsum; 7OB9; -.
DR PDBsum; 7OBA; -.
DR PDBsum; 7OBB; -.
DR PDBsum; 7VBA; -.
DR PDBsum; 7VBB; -.
DR PDBsum; 7VBC; -.
DR AlphaFoldDB; Q9GZS1; -.
DR SMR; Q9GZS1; -.
DR BioGRID; 122173; 311.
DR CORUM; Q9GZS1; -.
DR DIP; DIP-27546N; -.
DR IntAct; Q9GZS1; 28.
DR MINT; Q9GZS1; -.
DR STRING; 9606.ENSP00000367029; -.
DR iPTMnet; Q9GZS1; -.
DR PhosphoSitePlus; Q9GZS1; -.
DR SwissPalm; Q9GZS1; -.
DR BioMuta; POLR1E; -.
DR DMDM; 62901107; -.
DR SWISS-2DPAGE; Q9GZS1; -.
DR CPTAC; CPTAC-1634; -.
DR EPD; Q9GZS1; -.
DR jPOST; Q9GZS1; -.
DR MassIVE; Q9GZS1; -.
DR MaxQB; Q9GZS1; -.
DR PaxDb; Q9GZS1; -.
DR PeptideAtlas; Q9GZS1; -.
DR PRIDE; Q9GZS1; -.
DR ProteomicsDB; 80124; -. [Q9GZS1-1]
DR ProteomicsDB; 80125; -. [Q9GZS1-2]
DR Antibodypedia; 12019; 165 antibodies from 27 providers.
DR DNASU; 64425; -.
DR Ensembl; ENST00000377792.3; ENSP00000367023.3; ENSG00000137054.16. [Q9GZS1-1]
DR Ensembl; ENST00000377798.9; ENSP00000367029.4; ENSG00000137054.16. [Q9GZS1-2]
DR GeneID; 64425; -.
DR KEGG; hsa:64425; -.
DR MANE-Select; ENST00000377798.9; ENSP00000367029.4; NM_022490.4; NP_071935.1.
DR UCSC; uc003zzy.2; human. [Q9GZS1-2]
DR CTD; 64425; -.
DR DisGeNET; 64425; -.
DR GeneCards; POLR1E; -.
DR HGNC; HGNC:17631; POLR1E.
DR HPA; ENSG00000137054; Low tissue specificity.
DR neXtProt; NX_Q9GZS1; -.
DR OpenTargets; ENSG00000137054; -.
DR PharmGKB; PA142671136; -.
DR VEuPathDB; HostDB:ENSG00000137054; -.
DR eggNOG; KOG4183; Eukaryota.
DR GeneTree; ENSGT00390000018004; -.
DR HOGENOM; CLU_034953_0_0_1; -.
DR InParanoid; Q9GZS1; -.
DR OMA; DVYPFDE; -.
DR OrthoDB; 800331at2759; -.
DR PhylomeDB; Q9GZS1; -.
DR TreeFam; TF331685; -.
DR PathwayCommons; Q9GZS1; -.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR SignaLink; Q9GZS1; -.
DR SIGNOR; Q9GZS1; -.
DR BioGRID-ORCS; 64425; 609 hits in 1093 CRISPR screens.
DR GeneWiki; POLR1E; -.
DR GenomeRNAi; 64425; -.
DR Pharos; Q9GZS1; Tbio.
DR PRO; PR:Q9GZS1; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9GZS1; protein.
DR Bgee; ENSG00000137054; Expressed in body of pancreas and 145 other tissues.
DR ExpressionAtlas; Q9GZS1; baseline and differential.
DR Genevisible; Q9GZS1; HS.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; ISS:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0001179; F:RNA polymerase I general transcription initiation factor binding; IEA:Ensembl.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IBA:GO_Central.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IBA:GO_Central.
DR InterPro; IPR009668; RNA_pol-assoc_fac_A49-like.
DR PANTHER; PTHR14440; PTHR14440; 1.
DR Pfam; PF06870; RNA_pol_I_A49; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW DNA-directed RNA polymerase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription.
FT CHAIN 1..419
FT /note="DNA-directed RNA polymerase I subunit RPA49"
FT /id="PRO_0000073956"
FT REGION 397..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 373
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:24207024"
FT VAR_SEQ 1..25
FT /note="MAAEVLPSARWQYCGAPDGSQRAVL -> MYQASAVSLLPRDIPSCHSPSPG
FT FSHLPTSSSQLAPDLLQFPLGQDPSFLAIPILTLPPSDSLVPPYIVWYIVWPSALISFL
FT GCTLT (in isoform 1)"
FT /id="VSP_059915"
FT VARIANT 192
FT /note="D -> H (in dbSNP:rs7863488)"
FT /id="VAR_022372"
FT VARIANT 356
FT /note="V -> M (in dbSNP:rs7867180)"
FT /id="VAR_022373"
FT VARIANT 383
FT /note="R -> K (in dbSNP:rs10814571)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_022374"
FT MUTAGEN 373
FT /note="K->R: Decreased acetylation."
FT /evidence="ECO:0000269|PubMed:24207024"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:7OBB"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 98..111
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 272..276
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 330..347
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 365..374
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:7OB9"
FT CONFLICT Q9GZS1-1:56
FT /note="T -> A (in Ref. 1; BAC03629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 47260 MW; AB9EF3B9E8230053 CRC64;
MAAEVLPSAR WQYCGAPDGS QRAVLVQFSN GKLQSPGNMR FTLYENKDST NPRKRNQRIL
AAETDRLSYV GNNFGTGALK CNTLCRHFVG ILNKTSGQME VYDAELFNMQ PLFSDVSVES
ELALESQTKT YREKMDSCIE AFGTTKQKRA LNTRRMNRVG NESLNRAVAK AAETIIDTKG
VTALVSDAIH NDLQDDSLYL PPCYDDAAKP EDVYKFEDLL SPAEYEALQS PSEAFRNVTS
EEILKMIEEN SHCTFVIEAL KSLPSDVESR DRQARCIWFL DTLIKFRAHR VVKRKSALGP
GVPHIINTKL LKHFTCLTYN NGRLRNLISD SMKAKITAYV IILALHIHDF QIDLTVLQRD
LKLSEKRMME IAKAMRLKIS KRRVSVAAGS EEDHKLGTLS LPLPPAQTSD RLAKRRKIT
