ID   KAP3_MOUSE              Reviewed;         416 AA.
AC   P31324; B1B199; Q3UTZ1; Q80ZM4; Q8BRZ7;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 199.
DE   RecName: Full=cAMP-dependent protein kinase type II-beta regulatory subunit;
GN   Name=Prkar2b;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RX   PubMed=2069562; DOI=10.1016/0006-291x(91)91802-j;
RA   Singh I.S., Luo Z., Eng A., Erlichman J.;
RT   "Molecular cloning and characterization of the promoter region of the mouse
RT   regulatory subunit RII beta of type II cAMP-dependent protein kinase.";
RL   Biochem. Biophys. Res. Commun. 178:221-226(1991).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-112, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH PRKACA, AND SUBUNIT.
RX   PubMed=22323819; DOI=10.1126/science.1213979;
RA   Zhang P., Smith-Nguyen E.V., Keshwani M.M., Deal M.S., Kornev A.P.,
RA   Taylor S.S.;
RT   "Structure and allostery of the PKA RIIbeta tetrameric holoenzyme.";
RL   Science 335:712-716(2012).
CC   -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
CC       involved in cAMP signaling in cells. Type II regulatory chains mediate
CC       membrane association by binding to anchoring proteins, including the
CC       MAP2 kinase.
CC   -!- SUBUNIT: The inactive form of the enzyme is composed of two regulatory
CC       chains and two catalytic chains. Activation by cAMP produces two active
CC       catalytic monomers and a regulatory dimer that binds four cAMP
CC       molecules. Interacts with PRKACA and PRKACB. Interacts with the
CC       phosphorylated form of PJA2. Forms a complex composed of PRKAR2B, GSK3B
CC       and GSKIP through GSKIP interaction; facilitates PKA-induced
CC       phosphorylation and regulates GSK3B activity.
CC       {ECO:0000250|UniProtKB:P31323}.
CC   -!- INTERACTION:
CC       P31324; Q5S006: Lrrk2; NbExp=3; IntAct=EBI-455340, EBI-2693710;
CC       P31324; P05132: Prkaca; NbExp=15; IntAct=EBI-455340, EBI-400564;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and at the
CC       cell membrane. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Four types of regulatory chains are found: I-alpha,
CC       I-beta, II-alpha, and II-beta. Their expression varies among tissues
CC       and is in some cases constitutive and in others inducible.
CC   -!- PTM: Phosphorylated by the activated catalytic chain.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000305}.
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DR   EMBL; AK041013; BAC30779.1; -; mRNA.
DR   EMBL; AK138963; BAE23838.1; -; mRNA.
DR   EMBL; CT010463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC048710; AAH48710.1; -; mRNA.
DR   EMBL; M68861; AAA40057.1; -; Genomic_DNA.
DR   CCDS; CCDS25869.1; -.
DR   PIR; PQ0161; PQ0161.
DR   RefSeq; NP_035288.2; NM_011158.3.
DR   RefSeq; XP_006515077.1; XM_006515014.3.
DR   PDB; 3TNP; X-ray; 2.30 A; B/E=1-416.
DR   PDB; 3TNQ; X-ray; 3.10 A; A=1-416.
DR   PDB; 4WBB; X-ray; 2.80 A; A=1-416.
DR   PDB; 4X6Q; X-ray; 2.52 A; B=1-416.
DR   PDBsum; 3TNP; -.
DR   PDBsum; 3TNQ; -.
DR   PDBsum; 4WBB; -.
DR   PDBsum; 4X6Q; -.
DR   AlphaFoldDB; P31324; -.
DR   SMR; P31324; -.
DR   BioGRID; 202369; 30.
DR   CORUM; P31324; -.
DR   DIP; DIP-31571N; -.
DR   IntAct; P31324; 18.
DR   MINT; P31324; -.
DR   STRING; 10090.ENSMUSP00000039797; -.
DR   GlyGen; P31324; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P31324; -.
DR   PhosphoSitePlus; P31324; -.
DR   SwissPalm; P31324; -.
DR   EPD; P31324; -.
DR   jPOST; P31324; -.
DR   MaxQB; P31324; -.
DR   PaxDb; 10090-ENSMUSP00000039797; -.
DR   PeptideAtlas; P31324; -.
DR   ProteomicsDB; 301730; -.
DR   Pumba; P31324; -.
DR   Antibodypedia; 1082; 423 antibodies from 35 providers.
DR   DNASU; 19088; -.
DR   Ensembl; ENSMUST00000003079.12; ENSMUSP00000003079.6; ENSMUSG00000002997.16.
DR   Ensembl; ENSMUST00000036497.16; ENSMUSP00000039797.10; ENSMUSG00000002997.16.
DR   GeneID; 19088; -.
DR   KEGG; mmu:19088; -.
DR   UCSC; uc007nhx.2; mouse.
DR   AGR; MGI:97760; -.
DR   CTD; 5577; -.
DR   MGI; MGI:97760; Prkar2b.
DR   VEuPathDB; HostDB:ENSMUSG00000002997; -.
DR   eggNOG; KOG1113; Eukaryota.
DR   GeneTree; ENSGT00940000158160; -.
DR   HOGENOM; CLU_018310_2_0_1; -.
DR   InParanoid; P31324; -.
DR   OMA; GEQGDTF; -.
DR   OrthoDB; 55978at2759; -.
DR   PhylomeDB; P31324; -.
DR   TreeFam; TF314920; -.
DR   Reactome; R-MMU-163615; PKA activation.
DR   Reactome; R-MMU-164378; PKA activation in glucagon signalling.
DR   Reactome; R-MMU-180024; DARPP-32 events.
DR   Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
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-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-MMU-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR   Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR   Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR   Reactome; R-MMU-9634597; GPER1 signaling.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 19088; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Prkar2b; mouse.
DR   PRO; PR:P31324; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; P31324; Protein.
DR   Bgee; ENSMUSG00000002997; Expressed in brown adipose tissue and 248 other cell types or tissues.
DR   ExpressionAtlas; P31324; baseline and differential.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:MGI.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0097546; C:ciliary base; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0043198; C:dendritic shaft; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0043197; C:dendritic spine; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:0030552; F:cAMP binding; ISO:MGI.
DR   GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; ISO:MGI.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IDA:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   GO; GO:0097332; P:response to antipsychotic drug; IEA:Ensembl.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd12104; DD_RIIbeta_PKA; 1.
DR   DisProt; DP01944; -.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR   PANTHER; PTHR11635:SF169; CAMP-DEPENDENT PROTEIN KINASE TYPE II-BETA REGULATORY SUBUNIT; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   Genevisible; P31324; MM.
PE   1: Evidence at protein level;
KW   3D-structure; cAMP; cAMP-binding; Cell membrane; Cytoplasm; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..416
FT                   /note="cAMP-dependent protein kinase type II-beta
FT                   regulatory subunit"
FT                   /id="PRO_0000205391"
FT   REGION          1..151
FT                   /note="Dimerization and phosphorylation"
FT   BINDING         152..273
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         221
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..416
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         350
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         359
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P31323"
FT   MOD_RES         112
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:21183079"
FT   CONFLICT        69
FT                   /note="I -> T (in Ref. 3; AAH48710)"
FT                   /evidence="ECO:0000305"
FT   HELIX           137..147
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   HELIX           158..167
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          169..173
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          178..180
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          188..194
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          196..202
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          207..215
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   HELIX           221..224
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          231..246
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   HELIX           247..261
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          262..268
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   HELIX           269..271
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   HELIX           273..275
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   HELIX           280..289
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          291..295
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          300..302
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          310..322
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          338..342
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          347..349
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   HELIX           350..353
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   STRAND          360..375
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   HELIX           376..383
FT                   /evidence="ECO:0007829|PDB:3TNP"
FT   HELIX           386..390
FT                   /evidence="ECO:0007829|PDB:3TNP"
SQ   SEQUENCE   416 AA;  46167 MW;  24196C3037789827 CRC64;
     MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGAAR FGHEGRTWGD
     AGAAAGGGIP SKGVNFAEEP MRSDSENGEE EEAAEAGAFN APVINRFTRR ASVCAEAYNP
     DEEEDDAESR IIHPKTDDQR NRLQEACKDI LLFKNLDPEQ MSQVLDAMFE KLVKEGEHVI
     DQGDDGDNFY VIDRGTFDIY VKCDGVGRCV GNYDNRGSFG ELALMYNTPR AATITATSPG
     ALWGLDRVTF RRIIVKNNAK KRKMYESFIE SLPFLKSLEV SERLKVVDVI GTKVYNDGEQ
     IIAQGDLADS FFIVESGEVK ITMKRKGKSE VEENGAVEIA RCFRGQYFGE LALVTNKPRA
     ASAHAIGTVK CLAMDVQAFE RLLGPCMEIM KRNIATYEEQ LVALFGTNMD IVEPTA
//