2ABA_HUMAN
ID 2ABA_HUMAN Reviewed; 447 AA.
AC P63151; B2RBU8; B4E1T7; P50409; Q00007;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform;
DE AltName: Full=PP2A subunit B isoform B55-alpha;
DE AltName: Full=PP2A subunit B isoform PR55-alpha;
DE AltName: Full=PP2A subunit B isoform R2-alpha;
DE AltName: Full=PP2A subunit B isoform alpha;
GN Name=PPP2R2A;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Lung fibroblast;
RX PubMed=1849734; DOI=10.1021/bi00229a001;
RA Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J.,
RA Merlevede W., Hofsteenge J., Hemmings B.A.;
RT "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A:
RT evidence for a neuronal-specific isoform.";
RL Biochemistry 30:3589-3597(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood;
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 [6]
RP INTERACTION WITH TP53.
RX PubMed=17245430; DOI=10.1038/sj.emboj.7601519;
RA Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.;
RT "A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced
RT dephosphorylation of p53 at Thr55.";
RL EMBO J. 26:402-411(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP INTERACTION WITH IER5.
RX PubMed=25816751; DOI=10.1016/j.febslet.2015.03.019;
RA Ishikawa Y., Kawabata S., Sakurai H.;
RT "HSF1 transcriptional activity is modulated by IER5 and PP2A/B55.";
RL FEBS Lett. 589:1150-1155(2015).
RN [12]
RP INTERACTION WITH PABIR1.
RX PubMed=27588481; DOI=10.18632/oncotarget.11698;
RA Fan L., Liu M.H., Guo M., Hu C.X., Yan Z.W., Chen J., Chen G.Q., Huang Y.;
RT "FAM122A, a new endogenous inhibitor of protein phosphatase 2A.";
RL Oncotarget 7:63887-63900(2016).
RN [13]
RP INTERACTION WITH MFHAS1.
RX PubMed=28609714; DOI=10.1016/j.molimm.2017.06.017;
RA Shi Q., Xiong B., Zhong J., Wang H., Ma D., Miao C.;
RT "MFHAS1 suppresses TLR4 signaling pathway via induction of PP2A C subunit
RT cytoplasm translocation and inhibition of c-Jun dephosphorylation at
RT Thr239.";
RL Mol. Immunol. 88:79-88(2017).
RN [14]
RP INTERACTION WITH CRTC3.
RX PubMed=30611118; DOI=10.1016/j.isci.2018.12.012;
RA Sonntag T., Ostojic J., Vaughan J.M., Moresco J.J., Yoon Y.S.,
RA Yates J.R. III, Montminy M.;
RT "Mitogenic Signals Stimulate the CREB Coactivator CRTC3 through PP2A
RT Recruitment.";
RL IScience 11:134-145(2018).
RN [15]
RP FUNCTION, AND INTERACTION WITH PABIR1.
RX PubMed=33108758; DOI=10.1016/j.molcel.2020.10.008;
RA Li F., Kozono D., Deraska P., Branigan T., Dunn C., Zheng X.F., Parmar K.,
RA Nguyen H., DeCaprio J., Shapiro G.I., Chowdhury D., D'Andrea A.D.;
RT "CHK1 Inhibitor Blocks Phosphorylation of FAM122A and Promotes Replication
RT Stress.";
RL Mol. Cell 0:0-0(2020).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC and catalytic activity, and also might direct the localization of the
CC catalytic enzyme to a particular subcellular compartment. Essential for
CC serine/threonine-protein phosphatase 2A-mediated dephosphorylation of
CC WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1
CC protein levels, and promoting the G2/M checkpoint (PubMed:33108758).
CC {ECO:0000269|PubMed:33108758}.
CC -!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD (By similarity). PP2A consists of a common
CC heterodimeric core enzyme, composed of a 36 kDa catalytic subunit
CC (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit
CC A), that associates with a variety of regulatory subunits. Proteins
CC that associate with the core dimer include three families of regulatory
CC subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56
CC families), the 48 kDa variable regulatory subunit, viral proteins, and
CC cell signaling molecules (By similarity). Interacts with TP53
CC (PubMed:17245430). Interacts with IER5 (PubMed:25816751). Interacts
CC with MFHAS1; the interaction is direct (PubMed:28609714). Interacts
CC with PABIR1/FAM122A (PubMed:27588481, PubMed:33108758). Interacts with
CC CRTC3 (PubMed:30611118). {ECO:0000250, ECO:0000269|PubMed:17245430,
CC ECO:0000269|PubMed:25816751, ECO:0000269|PubMed:27588481,
CC ECO:0000269|PubMed:28609714, ECO:0000269|PubMed:30611118,
CC ECO:0000269|PubMed:33108758}.
CC -!- INTERACTION:
CC P63151; P05067: APP; NbExp=3; IntAct=EBI-1048931, EBI-77613;
CC P63151; Q8NE08: COL25A1; NbExp=3; IntAct=EBI-1048931, EBI-25836642;
CC P63151; P53355: DAPK1; NbExp=3; IntAct=EBI-1048931, EBI-358616;
CC P63151; Q9NZR2: LRP1B; NbExp=3; IntAct=EBI-1048931, EBI-1642131;
CC P63151; Q5S007: LRRK2; NbExp=4; IntAct=EBI-1048931, EBI-5323863;
CC P63151; Q15843: NEDD8; NbExp=3; IntAct=EBI-1048931, EBI-716247;
CC P63151; P30153: PPP2R1A; NbExp=17; IntAct=EBI-1048931, EBI-302388;
CC P63151; P30154: PPP2R1B; NbExp=5; IntAct=EBI-1048931, EBI-357094;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P63151-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P63151-2; Sequence=VSP_043100;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC {ECO:0000269|PubMed:1849734}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
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DR EMBL; M64929; AAA36490.1; -; mRNA.
DR EMBL; AK303981; BAG64899.1; -; mRNA.
DR EMBL; AK314823; BAG37345.1; -; mRNA.
DR EMBL; AC022911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63578.1; -; Genomic_DNA.
DR EMBL; BC041071; AAH41071.1; -; mRNA.
DR CCDS; CCDS34867.1; -. [P63151-1]
DR CCDS; CCDS55213.1; -. [P63151-2]
DR PIR; A38351; A38351.
DR RefSeq; NP_001171062.1; NM_001177591.1. [P63151-2]
DR RefSeq; NP_002708.1; NM_002717.3. [P63151-1]
DR PDB; 3DW8; X-ray; 2.85 A; B/E=1-447.
DR PDBsum; 3DW8; -.
DR AlphaFoldDB; P63151; -.
DR SMR; P63151; -.
DR BioGRID; 111512; 216.
DR CORUM; P63151; -.
DR DIP; DIP-29398N; -.
DR IntAct; P63151; 104.
DR MINT; P63151; -.
DR STRING; 9606.ENSP00000325074; -.
DR BindingDB; P63151; -.
DR ChEMBL; CHEMBL4284; -.
DR DrugBank; DB02506; 2,6,8-Trimethyl-3-Amino-9-Benzyl-9-Methoxynonanoic Acid.
DR iPTMnet; P63151; -.
DR PhosphoSitePlus; P63151; -.
DR SwissPalm; P63151; -.
DR BioMuta; PPP2R2A; -.
DR DMDM; 52783535; -.
DR EPD; P63151; -.
DR jPOST; P63151; -.
DR MassIVE; P63151; -.
DR MaxQB; P63151; -.
DR PaxDb; P63151; -.
DR PeptideAtlas; P63151; -.
DR PRIDE; P63151; -.
DR ProteomicsDB; 57497; -.
DR ProteomicsDB; 57498; -. [P63151-2]
DR Antibodypedia; 22918; 230 antibodies from 31 providers.
DR DNASU; 5520; -.
DR Ensembl; ENST00000315985.7; ENSP00000325074.7; ENSG00000221914.11. [P63151-2]
DR Ensembl; ENST00000380737.8; ENSP00000370113.3; ENSG00000221914.11. [P63151-1]
DR GeneID; 5520; -.
DR KEGG; hsa:5520; -.
DR MANE-Select; ENST00000380737.8; ENSP00000370113.3; NM_002717.4; NP_002708.1.
DR UCSC; uc003xeu.4; human. [P63151-1]
DR CTD; 5520; -.
DR DisGeNET; 5520; -.
DR GeneCards; PPP2R2A; -.
DR HGNC; HGNC:9304; PPP2R2A.
DR HPA; ENSG00000221914; Low tissue specificity.
DR MIM; 604941; gene.
DR neXtProt; NX_P63151; -.
DR OpenTargets; ENSG00000221914; -.
DR PharmGKB; PA33668; -.
DR VEuPathDB; HostDB:ENSG00000221914; -.
DR eggNOG; KOG1354; Eukaryota.
DR GeneTree; ENSGT00950000182864; -.
DR HOGENOM; CLU_021713_3_3_1; -.
DR InParanoid; P63151; -.
DR OMA; TQQGHHL; -.
DR OrthoDB; 810409at2759; -.
DR PhylomeDB; P63151; -.
DR TreeFam; TF105553; -.
DR PathwayCommons; P63151; -.
DR Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P63151; -.
DR SIGNOR; P63151; -.
DR BioGRID-ORCS; 5520; 192 hits in 1100 CRISPR screens.
DR ChiTaRS; PPP2R2A; human.
DR EvolutionaryTrace; P63151; -.
DR GeneWiki; PPP2R2A; -.
DR GenomeRNAi; 5520; -.
DR Pharos; P63151; Tchem.
DR PRO; PR:P63151; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P63151; protein.
DR Bgee; ENSG00000221914; Expressed in calcaneal tendon and 204 other tissues.
DR ExpressionAtlas; P63151; baseline and differential.
DR Genevisible; P63151; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR000009; PP2A_PR55.
DR InterPro; IPR018067; PP2A_PR55_CS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11871; PTHR11871; 1.
DR PIRSF; PIRSF037309; PP2A_PR55; 1.
DR PRINTS; PR00600; PP2APR55.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS01024; PR55_1; 1.
DR PROSITE; PS01025; PR55_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Reference proteome;
KW Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..447
FT /note="Serine/threonine-protein phosphatase 2A 55 kDa
FT regulatory subunit B alpha isoform"
FT /id="PRO_0000071415"
FT REPEAT 26..65
FT /note="WD 1"
FT REPEAT 91..132
FT /note="WD 2"
FT REPEAT 175..213
FT /note="WD 3"
FT REPEAT 224..264
FT /note="WD 4"
FT REPEAT 283..321
FT /note="WD 5"
FT REPEAT 338..379
FT /note="WD 6"
FT REPEAT 414..446
FT /note="WD 7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..2
FT /note="MA -> MFPKFSLRSMFH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043100"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3DW8"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:3DW8"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 119..132
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 156..172
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 207..216
FT /evidence="ECO:0007829|PDB:3DW8"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:3DW8"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:3DW8"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 297..312
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:3DW8"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:3DW8"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:3DW8"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:3DW8"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:3DW8"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:3DW8"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:3DW8"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:3DW8"
SQ SEQUENCE 447 AA; 51692 MW; F4D407FF7ADA4ED6 CRC64;
MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE
NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK
LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI
NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN
TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM
MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG
SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL
HTAWHPKENI IAVATTNNLY IFQDKVN
