CMYA5_MOUSE
ID CMYA5_MOUSE Reviewed; 3739 AA.
AC Q70KF4; Q70X91; Q9CV01; Q9CV02; Q9ER93; Q9ER96;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cardiomyopathy-associated protein 5;
DE AltName: Full=Heart and skeletal muscle-specific and sprouty domain-containing;
DE AltName: Full=Myospryn {ECO:0000303|PubMed:14688250, ECO:0000303|PubMed:16407236};
DE AltName: Full=Stretch-response protein 553;
DE AltName: Full=Stretch-responsive fibronectin protein type 3;
DE AltName: Full=TRIM-like protein;
GN Name=Cmya5; Synonyms=Sr553, Srfsd, Tims;
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], INTERACTION WITH DTNBP1, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RX PubMed=14688250; DOI=10.1074/jbc.m312664200;
RA Benson M.A., Tinsley C.L., Blake D.J.;
RT "Myospryn is a novel binding partner for dysbindin in muscle.";
RL J. Biol. Chem. 279:10450-10458(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/10; TISSUE=Muscle;
RA McKoy G., Kemp T., Velineni R., Shaw A.L., Coulton G.R.;
RT "Characterisation of a novel stretch-sensitive gene encoding a Bbox/FN-
RT 3/SPRY domain containing protein.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3534-3739, AND INDUCTION BY MECHANICAL
RP STRETCH.
RC STRAIN=C57BL/10; TISSUE=Skeletal muscle;
RA Kemp T.J., Sadusky T.J., Coulton G.R.;
RT "Identification and characterisation of novel skeletal muscle genes
RT exhibiting increased expression in response to passive stretch.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH ACTN2, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16407236; DOI=10.1074/jbc.m510499200;
RA Durham J.T., Brand O.M., Arnold M., Reynolds J.G., Muthukumar L.,
RA Weiler H., Richardson J.A., Naya F.J.;
RT "Myospryn is a direct transcriptional target for MEF2A that encodes a
RT striated muscle, alpha-actinin-interacting, costamere-localized protein.";
RL J. Biol. Chem. 281:6841-6849(2006).
RN [6]
RP FUNCTION, INTERACTION WITH PRKAR2A, MUTAGENESIS OF LEU-3197; LEU-3309 AND
RP CYS-3437, SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY PKA.
RX PubMed=17499862; DOI=10.1016/j.bbamcr.2007.04.004;
RA Reynolds J.G., McCalmon S.A., Tomczyk T., Naya F.J.;
RT "Identification and mapping of protein kinase A binding sites in the
RT costameric protein myospryn.";
RL Biochim. Biophys. Acta 1773:891-902(2007).
RN [7]
RP INTERACTION WITH DES, AND SUBCELLULAR LOCATION.
RX PubMed=17872945; DOI=10.1074/jbc.m704733200;
RA Kouloumenta A., Mavroidis M., Capetanaki Y.;
RT "Proper perinuclear localization of the TRIM-like protein myospryn requires
RT its binding partner desmin.";
RL J. Biol. Chem. 282:35211-35221(2007).
RN [8]
RP FUNCTION, INTERACTION WITH DMD, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18252718; DOI=10.1074/jbc.c700221200;
RA Reynolds J.G., McCalmon S.A., Donaghey J.A., Naya F.J.;
RT "Deregulated protein kinase A signaling and myospryn expression in muscular
RT dystrophy.";
RL J. Biol. Chem. 283:8070-8074(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-850; SER-2192;
RP SER-2411; SER-2495 AND SER-2905, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Lung;
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 [10]
RP SUBCELLULAR LOCATION.
RX PubMed=20634290; DOI=10.1074/jbc.m110.108720;
RA Sarparanta J., Blandin G., Charton K., Vihola A., Marchand S., Milic A.,
RA Hackman P., Ehler E., Richard I., Udd B.;
RT "Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to
RT tibial and limb-girdle muscular dystrophies.";
RL J. Biol. Chem. 285:30304-30315(2010).
RN [11]
RP FUNCTION, AND INTERACTION WITH PPP3CA.
RX PubMed=21427212; DOI=10.1096/fj.10-169219;
RA Kielbasa O.M., Reynolds J.G., Wu C.L., Snyder C.M., Cho M.Y., Weiler H.,
RA Kandarian S., Naya F.J.;
RT "Myospryn is a calcineurin-interacting protein that negatively modulates
RT slow-fiber-type transformation and skeletal muscle regeneration.";
RL FASEB J. 25:2276-2286(2011).
RN [12]
RP SUBUNIT, INTERACTION WITH FSD2, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=28740084; DOI=10.1038/s41598-017-06395-6;
RA Benson M.A., Tinsley C.L., Waite A.J., Carlisle F.A., Sweet S.M.M.,
RA Ehler E., George C.H., Lai F.A., Martin-Rendon E., Blake D.J.;
RT "Ryanodine receptors are part of the myospryn complex in cardiac muscle.";
RL Sci. Rep. 7:6312-6312(2017).
CC -!- FUNCTION: May serve as an anchoring protein that mediates the
CC subcellular compartmentation of protein kinase A (PKA) via binding to
CC PRKAR2A. May attenuate calcineurin ability to induce slow-fiber gene
CC program in muscle and may negatively modulate skeletal muscle
CC regeneration. Plays a role in the assembly of ryanodine receptor (RYR2)
CC clusters in striated muscle. {ECO:0000269|PubMed:17499862,
CC ECO:0000269|PubMed:18252718, ECO:0000269|PubMed:21427212,
CC ECO:0000269|PubMed:28740084}.
CC -!- SUBUNIT: Interacts with PRKAR2A. Interacts with ACTN2, DES and
CC DTNBP1/dysbindin. Interacts with DMD/dystrophin. Interacts with the
CC calcineurin catalytic subunit PPP3CA. Interacts with TTN (By
CC similarity). Interacts with CAPN3; this interaction, which results in
CC CMYA5 proteolysis, may protect CAPN3 from autolysis (By similarity).
CC Interacts with FSD2 (PubMed:28740084). In cardiac muscles, identified
CC in a complex composed of FSD2, CMYA5 and RYR2 (PubMed:28740084).
CC {ECO:0000250, ECO:0000269|PubMed:28740084}.
CC -!- INTERACTION:
CC Q70KF4; Q91WZ8: Dtnbp1; NbExp=5; IntAct=EBI-782290, EBI-643186;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A286XF80}.
CC Cytoplasm. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm, myofibril, sarcomere, M
CC line. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:A0A286XF80}.
CC Note=Found predominantly at the periphery of the nucleus but also
CC throughout the cell. Localized in lysosomes. In skeletal muscles,
CC localizes along myofiber periphery, at costameres. Predominantly flanks
CC Z-disks (By similarity). Occasionally present at the M-band level. In
CC the mdx mouse model for Duchenne muscular dystrophy, exhibits a
CC discontinuous localization at the myofiber periphery with extensive
CC regions devoid of CMYA5. This highly irregular pattern is associated
CC with an increased cytoplasmic localization, particularly in discrete
CC foci within myofibers. Colocalized with RYR2 in the sarcoplasmic
CC reticulum (By similarity). {ECO:0000250|UniProtKB:A0A286XF80}.
CC -!- TISSUE SPECIFICITY: Expressed in skin as well as in cardiac muscle.
CC Expressed in skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:14688250, ECO:0000269|PubMed:16407236,
CC ECO:0000269|PubMed:18252718, ECO:0000269|PubMed:28740084}.
CC -!- DEVELOPMENTAL STAGE: At 10.5 dpc, strong expression is observed in the
CC atria and ventricles of the heart. The signal is localized
CC predominantly to the trabecular zone but not the compact zone of the
CC ventricles. Weaker expression is detected in the developing somites at
CC this time point. At 12.5 dpc the intense hybridization signal is
CC maintained in the heart with stronger expression in the atria compared
CC with the ventricles. At 15.5 dpc, continues to be expressed in the
CC heart with lower levels in the atria compared with the ventricles. In
CC contrast, skeletal muscle displays high levels of transcripts. A
CC sagittal section of an isolated heart from an 17.5 dpc mouse embryo
CC shows abundant expression in myocardial cells with a more robust signal
CC in the trabecular region. Expression in the cardiac valves is
CC completely absent at this time point. {ECO:0000269|PubMed:16407236}.
CC -!- INDUCTION: Up-regulated in response to mechanical stretch of skeletal
CC muscle (hypertrophy mechanically-induced). May be up-regulated by the
CC PKA-CREB signaling pathway. {ECO:0000269|PubMed:18252718,
CC ECO:0000269|Ref.4}.
CC -!- DOMAIN: Amphipathic helix regions act as an anchoring domain for PKA,
CC and appear to be responsible of the interaction between myospryn and
CC PRKAR2A.
CC -!- PTM: Phosphorylated by PKA. {ECO:0000269|PubMed:17499862}.
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DR EMBL; AJ575748; CAE02649.1; -; mRNA.
DR EMBL; AJ511265; CAD53474.1; -; mRNA.
DR EMBL; AK010194; BAB26761.1; -; mRNA.
DR EMBL; AK010195; BAB26762.1; -; mRNA.
DR EMBL; AJ245954; CAC08494.1; -; mRNA.
DR EMBL; AJ250188; CAC08495.1; -; mRNA.
DR SMR; Q70KF4; -.
DR IntAct; Q70KF4; 2.
DR STRING; 10090.ENSMUSP00000050408; -.
DR iPTMnet; Q70KF4; -.
DR PhosphoSitePlus; Q70KF4; -.
DR MaxQB; Q70KF4; -.
DR PaxDb; Q70KF4; -.
DR PRIDE; Q70KF4; -.
DR ProteomicsDB; 283644; -.
DR MGI; MGI:1923719; Cmya5.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q70KF4; -.
DR PhylomeDB; Q70KF4; -.
DR ChiTaRS; Cmya5; mouse.
DR PRO; PR:Q70KF4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q70KF4; protein.
DR GO; GO:0043034; C:costamere; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IGI:MGI.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:MGI.
DR GO; GO:0014733; P:regulation of skeletal muscle adaptation; IGI:MGI.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50853; FN3; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Sarcoplasmic reticulum.
FT CHAIN 1..3739
FT /note="Cardiomyopathy-associated protein 5"
FT /id="PRO_0000328723"
FT REPEAT 482..493
FT /note="1"
FT REPEAT 494..505
FT /note="2"
FT REPEAT 506..519
FT /note="3; approximate"
FT REPEAT 520..531
FT /note="4"
FT REPEAT 532..545
FT /note="5; approximate"
FT REPEAT 546..559
FT /note="6; approximate"
FT REPEAT 560..571
FT /note="7"
FT REPEAT 572..583
FT /note="8"
FT REPEAT 584..595
FT /note="9"
FT REPEAT 596..607
FT /note="10"
FT REPEAT 608..621
FT /note="11; approximate"
FT REPEAT 622..633
FT /note="12; approximate"
FT REPEAT 634..647
FT /note="14; approximate"
FT REPEAT 648..659
FT /note="15"
FT REPEAT 660..673
FT /note="16; approximate"
FT REPEAT 674..685
FT /note="17"
FT REPEAT 686..696
FT /note="18"
FT REPEAT 697..708
FT /note="19"
FT REPEAT 709..720
FT /note="20"
FT DOMAIN 3374..3475
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3476..3568
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3550..3735
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 1..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..720
FT /note="20 X 12 AA approximate tandem repeats of R-[DE]-
FT [EK]-[EG]-H-[AV]-P-E-[PS]-[IM]-V-[HLR]"
FT REGION 835..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1650..1969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1986..2016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2065..2246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2273..2318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2377..2498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2513..2532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2579..2616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2667..2725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2731..3041
FT /note="Required for RYR2 clustering"
FT /evidence="ECO:0000269|PubMed:28740084"
FT REGION 2742..2773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2791..2835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2881..2959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3027..3047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3111..3174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3187..3214
FT /note="Amphipathic helix H1"
FT REGION 3215..3342
FT /note="B-box coiled-coil; BBC"
FT REGION 3301..3318
FT /note="Amphipathic helix H2"
FT REGION 3421..3437
FT /note="Amphipathic helix H3"
FT COILED 380..406
FT /evidence="ECO:0000255"
FT COILED 2640..2664
FT /evidence="ECO:0000255"
FT COILED 3244..3323
FT /evidence="ECO:0000255"
FT COMPBIAS 22..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..149
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1728..1742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1808..1824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1899..1917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2070..2085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2129..2146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2155..2169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2208..2246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2377..2422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2430..2449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2667..2711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2758..2772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2896..2959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3128..3142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3149..3174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2905
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 3197
FT /note="L->P: Complete loss of PRKAR2A-binding."
FT /evidence="ECO:0000269|PubMed:17499862"
FT MUTAGEN 3309
FT /note="L->P: Complete loss of PRKAR2A-binding."
FT /evidence="ECO:0000269|PubMed:17499862"
FT MUTAGEN 3437
FT /note="C->P: Important loss of PRKAR2A-binding."
FT /evidence="ECO:0000269|PubMed:17499862"
FT CONFLICT 81
FT /note="S -> R (in Ref. 3; BAB26762)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="L -> F (in Ref. 1; CAE02649)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="A -> T (in Ref. 1; CAE02649)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="N -> Y (in Ref. 1; CAE02649)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="I -> T (in Ref. 1; CAE02649)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="H -> Y (in Ref. 1; CAE02649)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="H -> Q (in Ref. 1; CAE02649)"
FT /evidence="ECO:0000305"
FT CONFLICT 515..516
FT /note="Missing (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="S -> P (in Ref. 1; CAE02649)"
FT /evidence="ECO:0000305"
FT CONFLICT 540..545
FT /note="PVPIVH -> SIVQ (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="A -> V (in Ref. 1; CAE02649)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="E -> G (in Ref. 1; CAE02649)"
FT /evidence="ECO:0000305"
FT CONFLICT 567..603
FT /note="EPIVHRDKGHALEPIVHREEEHAPEPIVHRDEGHAPE -> GPV (in
FT Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="P -> L (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 621..622
FT /note="RK -> HR (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 635..639
FT /note="EEEQV -> DEGHA (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 643..644
FT /note="Missing (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="A -> V (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 661..665
FT /note="EEEQV -> DEGHA (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 669..670
FT /note="Missing (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="A -> V (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 683..705
FT /note="MVLREEHAPEPIVRREEEHAPEP -> ES (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="H -> L (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="Missing (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="I -> T (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="N -> S (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1094
FT /note="S -> SP (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1163
FT /note="E -> D (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1203
FT /note="T -> R (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1227
FT /note="L -> P (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1254
FT /note="P -> L (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1284..1286
FT /note="RQA -> QQE (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1505
FT /note="V -> A (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1513
FT /note="T -> M (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1516
FT /note="T -> M (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1564
FT /note="I -> V (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1580
FT /note="A -> T (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1635
FT /note="L -> V (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1647
FT /note="F -> L (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1832
FT /note="I -> T (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1872
FT /note="S -> P (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 2145
FT /note="P -> S (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 2453
FT /note="P -> S (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 2477
FT /note="A -> V (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 2511
FT /note="A -> T (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 2533
FT /note="D -> Y (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 2569
FT /note="A -> T (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 2698
FT /note="K -> E (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 2879
FT /note="C -> G (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 2929
FT /note="S -> T (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 3315..3317
FT /note="EAE -> GAK (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 3477
FT /note="P -> A (in Ref. 2; CAD53474)"
FT /evidence="ECO:0000305"
FT CONFLICT 3496
FT /note="R -> G (in Ref. 3; BAB26761)"
FT /evidence="ECO:0000305"
FT CONFLICT 3530
FT /note="H -> L (in Ref. 2; CAD53474 and 3; BAB26761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3739 AA; 413040 MW; CE3C5CB93E2A6487 CRC64;
MESGDSGLAA QGFLGWGADE EVAQELETEE ESEGEGEETA AESEEEPDAR LSDEDEEGKT
KQECIVSDPS FSMVAVQRED SGITWETNSS RSSTPWASGE SQTSGICSLE GSALTSPPGS
VSFIMDEVKR TRKRTQKSKR GSPSLRRKGS KKRNSLESQD VLTNQEDGPS ISESPVLNIE
NEKSSIGTYD KTRRKKTASN TPPITGAIYK EHKPLVLKPV YIGTVQYKIK MFNSVKEELI
PLQFYGTLPK GYVIKEIHYR RGKDSSISLE PDLSNGGSNI VPQRKLAQSP EEDKVRELAP
PWRGALSKGS RTSLFSHEEQ KKTYADSNLN VPSSTEHAFP SSARNDTADQ EENLSLPQMM
PQQPADESKT HRMEPPSIPA TMVLERAKEE LEQNAQGKES SEDDASVLTG SADDVQQEGL
VSVNHSMPWE AEKESLETGP PRPAPAIQEK FEPDMEGLEP ISTEKTEQAS EYVTSSEPIV
HREEEHAPEP IVHREEEHAP EPIVHREEEH APEPESIVHR EEEHAPESIV HREEEHAPEP
VPIVHREEEH APEPESIVHR EEEHAPEPIV HRDKGHALEP IVHREEEHAP EPIVHRDEGH
APEPIVHREE EHVPEPESIV RKGEEHAPEP IVHREEEQVP EPESIVHREE EHAPEPIVHR
EEEQVPEPES IVHREEEHAP EPMVLREEHA PEPIVRREEE HAPEPIVHRE EEHAPEPMVH
RKAQQLERGV ETSTPITDIT EPEDSSLEEE IIELDYPESP LASKETSPSP LSPEVEHRKE
PILPTQMTFT PERITLSEEE REENESVSTD SAFVSEYSVL QDLNHTPEKL EVEAVSVSDV
KSSNEPAVFS EDDEERESYS PAMTSVSEQS LSPSTTEKTS AIQSPLFSTV SPVLSGDEAS
ENVCHSPESE SAAEYSVPAH AQELLLKTGD HKLPLKSQRV SEPIIQAEDE KEDIGLLPPA
ALSQAVLSED ESLGSGSFAS DSKLPFKPSV SQNATRESPQ KTIDDMPQFK PRGLSDPATL
LEEEKEAIGV GLSSSNEVSA VECALPPQTT ELLSESHAPP PWAISSEQVV QSEEGSRDQQ
RGSFSSTPEL GHTSLLLKGA SSPTGLSEQG QEEDNIGPLS PDSAFASEFS FSPYPTQELE
KRELGRDSPL CLTSPSEQTV LSEEDTEEAD LFSPDSASQV SIPPYRIAET EQNKVEPDEL
LPTRSAPDYP YFSEADEEEA GSSVVTLVPE HSEPSQEREE SSPCRPVFED LSLPPSADKT
GQAETMSDVP TISTSVSEYL ILARQAKTQA SLEPEAEDLV PPPTSGWEKR DAKSSLPAVT
IAASSSALSS VVKEETTSVL PTSQPSVSPE STCVLKPEQE PTAPLTLTSA DEQMALPRVG
REKAVLDSQE ATAHKSQDQT PEPRLPNVPG SGMKYSVLSD LGDEPKADVK LNLAPTVTSE
LEQRMLSKNE PEVAKPHSPP EETSISGPKV LSAVKTEVKQ ESKITRELPA ASSGRERGAE
HSPPVPPALP ALTEETGKDT EASSSATTVP VTKLDSNSTK LGRDEVLTDP SLASPVEHPG
LKGIGKSELG SGLPLPSMSA SEVLRPEPKL PVNSGVEVER EDNEPPPLQV SPTSKPTVPN
DKHEEITRSP DSENLVSDDL APTLLAFRHE MNRQAEETSS PVPGSFLSGE QELIKLPPEP
EKHKQLSEVP TAGSELIDSR DRDRSLGIEP VKPIGTEPGP SILEKGPAEL QRRGKEQEEN
RKLPVPASAP LETASFDLPI EQKEPKRTLH EGQAVEVPDE SSSSADKPEL GVKQLAEKKE
NLEQPKPFVT TERASVTGSK VKESLISPKD NIWMLEKPDG LVNQHEDRKP GTGQLESSES
TDLMSEKLGA ASLDTDHTSE TRNQETSKAP VSGEKLSQEP RRVQSKAVDD SEEGRKLASG
NVEVLTQSKS VPAVKAKATP QPPETPEVTQ KPSEKSLVTE QGLPAEKGKK GISSFKSWMS
SLLFGSSIPD SKVSDNEDLE TRPGPSVEKA VPAIEPKGTV PAEVNIAEKP AVHSLPEVTV
KLAEEPKGVS VKSSISQDLK EKLTFLSNED VLKQPKSNSE NYGQKELPGF SEGMGESLAT
SVGDKHPGIH PCSPMGEKVG MEEAQNMAPL HITESQRRQK PEVSPPSMWN ISARKEEPSS
DHKETWLSSS DVVDRMPQKP KSAQSAFTRM NSEEPASMIL PVESKGSLSD LGEDRLRQEM
PKPTSLEHCE EEVERPTEEK DGWETRSFSL AGKRGLAEKQ EIMAPLELRE NEAVGELQRM
PESRPFKLEE SKAAERLEQR ISPTEKLMEK PSKTLALDRR EKEVQEWVFS EGEKQEYPPA
AMPVPGASAV SLDKAQPHLL AKPTPVVEKP EHIVTEVYPE IRERKAAETQ PHPQEEGKTL
VEKTKVSRVE SPHGEETDGH SLTQEGNLEL EKSGESRVDL KEERRRFVMP ELPLGASVAA
EDGSVQPRPL SKDAARASDM TDETKHLGTP PTQPSAVEPQ TLVLGTSVEH AVKKQETWSD
RPTVHTFQTS KDDTEEMLKQ SVLISKHHLE AVEDVHRNEP PSSAASNYAQ FMLSASEISA
DGVPPMGGTA QEPEGTSVKD EEFSVTSKPA GLSEDQKSAF SIISEGCEIL NIHAPAFIPS
VDQEESEQMQ DKLQYLEEKA SFKSISVHDE KKAAASHKTQ KSKLEVPDRK ITSLKENKTK
ETHKTKEEIA TDSGMGDFTP IQPTVSGEED YFEKYTLIDY NLSPGSGKQK STVEESSEEA
TKTLTSFPES SAEQALDHEY NLVKLDESFY GPEKDDSKLS HAEMQKSLAI QKPDDRNAPK
GISRDVDSRS PGMPLFDVEE GVLSKRQIFP TTPKAVNPEL LEEPPALSFF YKDLYEGACG
EKNEGETASE GDSVDSETSF PRRHSDTDDG PGMYFEKYIL KDDILHDESV TQEDQGQGLE
EKPVGEEDSQ QLRVAEREIR RKPETSFWEK NLEEQHKVVG REGEPTGHME TLDEAAMQQK
APITEQVRAV TQKMSYAVPF QDTRCVLESE PSSQGNEAGN ASPDVNLNVP VQVSFPEEES
AAGATYAPEV LQERLVPSVS REERLHNTPV QDEYDFVGSL NQEAASQAIL PEEPGSESSP
KEVLSQGSES FEHIREQELT SEGEPRMSAS QEVWDRTEDQ SARESVTAKT QKEPKKTQAE
SYCYTCKSLV SEMDKALDIH KDHEVSALDT AISAVKVQLG EFLENLQEKS LRIEAFVSEI
ESFFNTIEEK CSKNEKRLEM QNEEMMKRVL AQYDEKAQSF EEVKKKKMEF LHDQMVHFLQ
SMDTAKDTLE TIVREAEELD ETVFLASFEE INERLLSAME STASLENMPA AFSLFEHYDD
SSARSDQMLK QVAVPQPPRL EPQEPSSATS TTIAVYWSVN KEDVVDSFQV YCVEEPQDDQ
EINELVEEYR LTVKESCCIF EDLEPDRCYQ VWVMAVNFTG CSLPSERAIF RTAPSTPVIH
VEDCTVCWNT ATVRWRPANP EATETYTLEY CRQHSPEGEG LRSFSGIKGH QLKVNLPPND
NYFFYVRATN ASGTSEQSEA ALISTRGTRF LLLRETAHPA LQISANGTVI SFSERRRLTE
IPSVLGEELP ACGQHYWETT VADSPAYRLG ICTSSAVRAG ALGQGETSWY MHCSEPQRYT
FFYSGIVSEV HATERPARVG ILLDYTNQRL LFINAESGQL LFIVRHRFNE GVHPAFALEK
PGRCTLHLGL EPPDSVRHK
