KAP3_MOUSE
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 03-AUG-2022, entry version 190.
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, 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 [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; 29.
DR CORUM; P31324; -.
DR DIP; DIP-31571N; -.
DR IntAct; P31324; 18.
DR MINT; P31324; -.
DR STRING; 10090.ENSMUSP00000039797; -.
DR iPTMnet; P31324; -.
DR PhosphoSitePlus; P31324; -.
DR SwissPalm; P31324; -.
DR EPD; P31324; -.
DR jPOST; P31324; -.
DR MaxQB; P31324; -.
DR PaxDb; P31324; -.
DR PeptideAtlas; P31324; -.
DR PRIDE; P31324; -.
DR ProteomicsDB; 301730; -.
DR Antibodypedia; 1082; 391 antibodies from 35 providers.
DR DNASU; 19088; -.
DR Ensembl; ENSMUST00000003079; ENSMUSP00000003079; ENSMUSG00000002997.
DR Ensembl; ENSMUST00000036497; ENSMUSP00000039797; ENSMUSG00000002997.
DR GeneID; 19088; -.
DR KEGG; mmu:19088; -.
DR UCSC; uc007nhx.2; mouse.
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; YDNWSPP; -.
DR OrthoDB; 1047290at2759; -.
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 71 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 245 other tissues.
DR ExpressionAtlas; P31324; baseline and differential.
DR Genevisible; P31324; MM.
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: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; IMP:SynGO.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
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; IMP:SynGO.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; ISO:MGI.
DR GO; GO:0045859; P:regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0097332; P:response to antipsychotic drug; IEA:Ensembl.
DR GO; GO:0097338; P:response to clozapine; IEA:Ensembl.
DR CDD; cd00038; CAP_ED; 2.
DR DisProt; DP01944; -.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 1.
DR PIRSF; PIRSF000548; PK_regulatory; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
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
