2AAA_MOUSE
ID 2AAA_MOUSE Reviewed; 589 AA.
AC Q76MZ3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;
DE AltName: Full=PP2A subunit A isoform PR65-alpha;
DE AltName: Full=PP2A subunit A isoform R1-alpha;
GN Name=Ppp2r1a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=10100624; DOI=10.1016/s0014-5793(99)00189-1;
RA Nanahoshi M., Tsujishita Y., Tokunaga C., Inui S., Sakaguchi N., Hara K.,
RA Yonezawa K.;
RT "Alpha4 protein as a common regulator of type 2A-related serine/threonine
RT protein phosphatases.";
RL FEBS Lett. 446:108-112(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP INTERACTION WITH ADCY8.
RX PubMed=16258073; DOI=10.1124/mol.105.018275;
RA Crossthwaite A.J., Ciruela A., Rayner T.F., Cooper D.M.;
RT "A direct interaction between the N terminus of adenylyl cyclase AC8 and
RT the catalytic subunit of protein phosphatase 2A.";
RL Mol. Pharmacol. 69:608-617(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH FOXO1.
RX PubMed=22417654; DOI=10.1042/bj20111606;
RA Yan L., Guo S., Brault M., Harmon J., Robertson R.P., Hamid R., Stein R.,
RA Yang E.;
RT "The B55alpha-containing PP2A holoenzyme dephosphorylates FOXO1 in islet
RT beta-cells under oxidative stress.";
RL Biochem. J. 444:239-247(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
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).
CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a
CC scaffolding molecule to coordinate the assembly of the catalytic
CC subunit and a variable regulatory B subunit (PubMed:10100624). Upon
CC interaction with GNA12 promotes dephosphorylation of microtubule
CC associated protein TAU/MAPT (By similarity). Required for proper
CC chromosome segregation and for centromeric localization of SGO1 in
CC mitosis (By similarity). {ECO:0000250|UniProtKB:P30153,
CC ECO:0000269|PubMed:10100624}.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa
CC constant regulatory subunit (PR65 or subunit A), that associates with a
CC variety of regulatory subunits. Proteins that associate with the core
CC dimer include three families of regulatory subunits B (the
CC R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48
CC kDa variable regulatory subunit, viral proteins, and cell signaling
CC molecules. Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with FOXO1; the
CC interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation
CC sites (PubMed:22417654). Interacts with IPO9 (By similarity). Interacts
CC with TP53 and SGO1 (By similarity). Interacts with PLA2G16; this
CC interaction might decrease PP2A activity (By similarity). Interacts
CC with CTTNBP2NL (By similarity). Interacts with GNA12; the interaction
CC promotes protein phosphatase 2A activation causing dephosphorylation of
CC MAPT (By similarity).Interacts with CIP2A; this interaction stabilizes
CC CIP2A (By similarity). Interacts with PABIR1/FAM122A (By similarity).
CC Interacts with ADCY8; antagonizes interaction between ADCY8 and
CC calmodulin (PubMed:16258073). Interacts with CRTC3 (when phosphorylated
CC at 'Ser-391') (PubMed:30611118). Interacts with SPRY2 (By similarity).
CC {ECO:0000250|UniProtKB:P30153, ECO:0000250|UniProtKB:Q32PI5,
CC ECO:0000269|PubMed:16258073, ECO:0000269|PubMed:22417654,
CC ECO:0000269|PubMed:30611118}.
CC -!- INTERACTION:
CC Q76MZ3; P63330: Ppp2ca; NbExp=3; IntAct=EBI-400413, EBI-397144;
CC Q76MZ3; O56327; Xeno; NbExp=2; IntAct=EBI-400413, EBI-15646000;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q32PI5}. Nucleus
CC {ECO:0000250|UniProtKB:P30153}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:P30153}. Lateral cell membrane
CC {ECO:0000250|UniProtKB:P30153}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P30153}. Note=Centromeric localization requires
CC the presence of BUB1. {ECO:0000250|UniProtKB:P30153}.
CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices joined
CC by a hydrophilic region, the intrarepeat loop. The repeat units may be
CC arranged laterally to form a rod-like structure.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC {ECO:0000305}.
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DR EMBL; AB021743; BAA75478.1; -; mRNA.
DR EMBL; AK054239; BAC35700.1; -; mRNA.
DR EMBL; AK078135; BAC37143.1; -; mRNA.
DR EMBL; BC006606; AAH06606.1; -; mRNA.
DR CCDS; CCDS28432.1; -.
DR RefSeq; NP_058587.1; NM_016891.3.
DR PDB; 2IAE; X-ray; 3.50 A; A/D=1-589.
DR PDB; 2PF4; X-ray; 3.10 A; A/B/C/D=1-589.
DR PDB; 3FGA; X-ray; 2.70 A; A=2-589.
DR PDB; 6EF4; X-ray; 3.40 A; A=1-589.
DR PDBsum; 2IAE; -.
DR PDBsum; 2PF4; -.
DR PDBsum; 3FGA; -.
DR PDBsum; 6EF4; -.
DR AlphaFoldDB; Q76MZ3; -.
DR SMR; Q76MZ3; -.
DR BioGRID; 206176; 156.
DR CORUM; Q76MZ3; -.
DR DIP; DIP-29429N; -.
DR IntAct; Q76MZ3; 143.
DR MINT; Q76MZ3; -.
DR STRING; 10090.ENSMUSP00000007708; -.
DR BindingDB; Q76MZ3; -.
DR ChEMBL; CHEMBL3557; -.
DR iPTMnet; Q76MZ3; -.
DR PhosphoSitePlus; Q76MZ3; -.
DR SwissPalm; Q76MZ3; -.
DR REPRODUCTION-2DPAGE; Q76MZ3; -.
DR EPD; Q76MZ3; -.
DR jPOST; Q76MZ3; -.
DR MaxQB; Q76MZ3; -.
DR PaxDb; Q76MZ3; -.
DR PeptideAtlas; Q76MZ3; -.
DR PRIDE; Q76MZ3; -.
DR ProteomicsDB; 285889; -.
DR Antibodypedia; 4348; 392 antibodies from 42 providers.
DR DNASU; 51792; -.
DR Ensembl; ENSMUST00000007708; ENSMUSP00000007708; ENSMUSG00000007564.
DR GeneID; 51792; -.
DR KEGG; mmu:51792; -.
DR UCSC; uc008aqi.1; mouse.
DR CTD; 5518; -.
DR MGI; MGI:1926334; Ppp2r1a.
DR VEuPathDB; HostDB:ENSMUSG00000007564; -.
DR eggNOG; KOG0211; Eukaryota.
DR GeneTree; ENSGT00950000183066; -.
DR HOGENOM; CLU_015533_2_1_1; -.
DR InParanoid; Q76MZ3; -.
DR OMA; WAQNTVI; -.
DR OrthoDB; 447572at2759; -.
DR PhylomeDB; Q76MZ3; -.
DR TreeFam; TF105552; -.
DR Reactome; R-MMU-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-MMU-1295596; Spry regulation of FGF signaling.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-180024; DARPP-32 events.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-MMU-198753; ERK/MAPK targets.
DR Reactome; R-MMU-202670; ERKs are inactivated.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
DR Reactome; R-MMU-432142; Platelet sensitization by LDL.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 51792; 27 hits in 81 CRISPR screens.
DR ChiTaRS; Ppp2r1a; mouse.
DR EvolutionaryTrace; Q76MZ3; -.
DR PRO; PR:Q76MZ3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q76MZ3; protein.
DR Bgee; ENSMUSG00000007564; Expressed in vestibular membrane of cochlear duct and 271 other tissues.
DR ExpressionAtlas; Q76MZ3; baseline and differential.
DR Genevisible; Q76MZ3; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:1990405; F:protein antigen binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:MGI.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IMP:MGI.
DR GO; GO:0051232; P:meiotic spindle elongation; IMP:MGI.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IMP:MGI.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IDA:MGI.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:InterPro.
DR GO; GO:1903538; P:regulation of meiotic cell cycle process involved in oocyte maturation; IMP:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR031090; PP2A_A_meta.
DR PANTHER; PTHR10648:SF2; PTHR10648:SF2; 1.
DR Pfam; PF02985; HEAT; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 11.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cell projection; Centromere;
KW Chromosome; Chromosome partition; Cytoplasm; Membrane; Nucleus;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P30153"
FT CHAIN 2..589
FT /note="Serine/threonine-protein phosphatase 2A 65 kDa
FT regulatory subunit A alpha isoform"
FT /id="PRO_0000071401"
FT REPEAT 8..46
FT /note="HEAT 1"
FT REPEAT 47..84
FT /note="HEAT 2"
FT REPEAT 85..123
FT /note="HEAT 3"
FT REPEAT 124..161
FT /note="HEAT 4"
FT REPEAT 162..200
FT /note="HEAT 5"
FT REPEAT 201..239
FT /note="HEAT 6"
FT REPEAT 240..278
FT /note="HEAT 7"
FT REPEAT 279..321
FT /note="HEAT 8"
FT REPEAT 322..360
FT /note="HEAT 9"
FT REPEAT 361..399
FT /note="HEAT 10"
FT REPEAT 400..438
FT /note="HEAT 11"
FT REPEAT 439..477
FT /note="HEAT 12"
FT REPEAT 478..516
FT /note="HEAT 13"
FT REPEAT 517..555
FT /note="HEAT 14"
FT REPEAT 556..589
FT /note="HEAT 15"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P30153"
FT MOD_RES 280
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:3FGA"
FT TURN 77..81
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2IAE"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:3FGA"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 160..174
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 189..193
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 198..213
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 276..291
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:3FGA"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 318..324
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 353..373
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:2IAE"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 397..403
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 417..424
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 427..434
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 436..442
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 444..451
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 456..473
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 475..481
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 483..488
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 495..520
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 522..528
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 534..547
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 553..558
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 560..568
FT /evidence="ECO:0007829|PDB:3FGA"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:2IAE"
FT HELIX 573..585
FT /evidence="ECO:0007829|PDB:3FGA"
SQ SEQUENCE 589 AA; 65323 MW; 5175409E4D50A366 CRC64;
MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY
DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE ETVVRDKAVE SLRAISHEHS
PSDLEAHFVP LVKRLAGGDW FTSRTSACGL FSVCYPRVSS AVKAELRQYF RNLCSDDTPM
VRRAAASKLG EFAKVLELDN VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL
EALVMPTLRQ AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA
AASHKVKEFC ENLSADCREN VIMTQILPCI KELVSDANQH VKSALASVIM GLSPILGKDN
TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL SQSLLPAIVE LAEDAKWRVR
LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW LVDHVYAIRE AATSNLKKLV EKFGKEWAHA
TIIPKVLAMS GDPNYLHRMT TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV
AKSLQKIGPI LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA
