KAPCA_RAT
ID KAPCA_RAT Reviewed; 351 AA.
AC P27791; Q6UA68;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha;
DE Short=PKA C-alpha;
DE EC=2.7.11.11;
GN Name=Prkaca;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=1711374; DOI=10.1016/0167-4781(91)90018-h;
RA Wiemann S., Voss H., Kinzel V., Pyerin W.;
RT "Rat C alpha catalytic subunit of the cAMP-dependent protein kinase: cDNA
RT sequence and evidence that it is the only isoform expressed in myoblasts.";
RL Biochim. Biophys. Acta 1089:254-256(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-8 (ISOFORM 1), MYRISTOYLATION AT GLY-2, AND
RP DEAMIDATION AT ASN-3.
RX PubMed=9521123; DOI=10.1002/pro.5560070227;
RA Jedrzejewski P.T., Girod A., Tholey A., Koenig N., Thullner S., Kinzel V.,
RA Bossemeyer D.;
RT "A conserved deamidation site at Asn 2 in the catalytic subunit of
RT mammalian cAMP-dependent protein kinase detected by capillary LC-MS and
RT tandem mass spectrometry.";
RL Protein Sci. 7:457-469(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-313 (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Wistar;
RX PubMed=14514679; DOI=10.1074/jbc.m308365200;
RA Ullas K.S., Rao M.R.S.;
RT "Phosphorylation of rat spermatidal protein TP2 by sperm-specific protein
RT kinase A and modulation of its transport into the haploid nucleus.";
RL J. Biol. Chem. 278:52673-52680(2003).
RN [4]
RP FUNCTION IN RAPID EYE MOVEMENT SLEEP.
RX PubMed=20844122; DOI=10.1523/jneurosci.1563-10.2010;
RA Datta S., Desarnaud F.;
RT "Protein kinase A in the pedunculopontine tegmental nucleus of rat
RT contributes to regulation of rapid eye movement sleep.";
RL J. Neurosci. 30:12263-12273(2010).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP INTERACTION WITH RAB13.
RX PubMed=23419316; DOI=10.1530/jme-13-0011;
RA Su W., Liu X.;
RT "RAB13 regulates Sertoli cell permeability barrier dynamics through protein
RT kinase A.";
RL J. Mol. Endocrinol. 50:305-318(2013).
CC -!- FUNCTION: Phosphorylates a large number of substrates in the cytoplasm
CC and the nucleus (By similarity). Phosphorylates CDC25B, ABL1, NFKB1,
CC CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP (By similarity).
CC Regulates the abundance of compartmentalized pools of its regulatory
CC subunits through phosphorylation of PJA2 which binds and ubiquitinates
CC these subunits, leading to their subsequent proteolysis. RORA is
CC activated by phosphorylation. Required for glucose-mediated adipogenic
CC differentiation increase and osteogenic differentiation inhibition from
CC osteoblasts (By similarity). Involved in chondrogenesis by mediating
CC phosphorylation of SOX9 (By similarity). Involved in the regulation of
CC platelets in response to thrombin and collagen; maintains circulating
CC platelets in a resting state by phosphorylating proteins in numerous
CC platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and
CC NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt
CC these complexes and free active PRKACA stimulates platelets and leads
CC to platelet aggregation by phosphorylating VASP. RYR2 channel activity
CC is potentiated by phosphorylation in presence of luminal Ca(2+),
CC leading to reduced amplitude and increased frequency of store overload-
CC induced Ca(2+) release (SOICR) characterized by an increased rate of
CC Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves,
CC despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6
CC activation by phosphorylation stimulates proteasome. Negatively
CC regulates tight junctions (TJs) in ovarian cancer cells via CLDN3
CC phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA
CC binding. Involved in embryonic development by down-regulating the
CC Hedgehog (Hh) signaling pathway that determines embryo pattern
CC formation and morphogenesis (By similarity). Prevents meiosis
CC resumption in prophase-arrested oocytes via CDC25B inactivation by
CC phosphorylation (By similarity). May also regulate rapid eye movement
CC (REM) sleep in the pedunculopontine tegmental (PPT) (PubMed:20844122).
CC Phosphorylates APOBEC3G and AICDA. Phosphorylates HSF1; this
CC phosphorylation promotes HSF1 nuclear localization and transcriptional
CC activity upon heat shock (By similarity).
CC {ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P17612,
CC ECO:0000269|PubMed:20844122}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.11;
CC -!- ACTIVITY REGULATION: Allosterically activated by various compounds,
CC including ATP. Activated by cAMP; the nucleotide acts as a dynamic and
CC allosteric activator by coupling the two lobes of apo PKA, enhancing
CC the enzyme dynamics synchronously and priming it for catalysis.
CC -!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced by
CC the combination of homo- or heterodimers of the different regulatory
CC subunits associated with two catalytic subunits. cAMP causes the
CC dissociation of the inactive holoenzyme into a dimer of regulatory
CC subunits bound to four cAMP and two free monomeric catalytic subunits.
CC The cAMP-dependent protein kinase catalytic subunit binds PJA2. Both
CC isoforms 1 and 2 forms activate cAMP-sensitive PKAI and PKAII
CC holoenzymes by interacting with regulatory subunit (R) of PKA,
CC PRKAR1A/PKR1 and PRKAR2A/PKR2, respectively. Interacts with NFKB1,
CC NFKB2 and NFKBIA in platelets; these interactions are disrupted by
CC thrombin and collagen. Binds to ABL1 in spermatozoa and with CDC25B in
CC oocytes (By similarity). Interacts with APOBEC3G and AICDA (By
CC similarity). Interacts with RAB13; downstream effector of RAB13
CC involved in tight junction assembly. Found in a complex at least
CC composed of MROH2B, PRKACA isoform 2 and TCP11 (By similarity).
CC Interacts with MROH2B (By similarity). Interacts with HSF1 (By
CC similarity). Isoform 2 interacts with TCP11 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P05132,
CC ECO:0000250|UniProtKB:P17612, ECO:0000269|PubMed:23419316}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}.
CC Membrane {ECO:0000250|UniProtKB:P17612}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P17612}. Note=Translocates into the nucleus
CC (monomeric catalytic subunit). The inactive holoenzyme is found in the
CC cytoplasm. Distributed throughout the cytoplasm in meiotically
CC incompetent oocytes. Associated to mitochondrion as meiotic competence
CC is acquired. Aggregates around the germinal vesicles (GV) at the
CC immature GV stage oocytes (By similarity). Colocalizes with HSF1 in
CC nuclear stress bodies (nSBs) upon heat shock (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P17612}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:P05132}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:P05132}. Note=Expressed in the midpiece
CC region of the sperm flagellum. Expressed in the midpiece region of the
CC sperm flagellum. Colocalizes with MROH2B and TCP11 on the acrosome and
CC tail regions in round spermatids and spermatozoa regardless of the
CC capacitation status of the sperm. {ECO:0000250,
CC ECO:0000250|UniProtKB:P05132}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=C-alpha-1;
CC IsoId=P27791-1; Sequence=Displayed;
CC Name=2; Synonyms=Cs;
CC IsoId=P27791-2; Sequence=VSP_013277;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is round
CC spermatid specific. {ECO:0000269|PubMed:14514679,
CC ECO:0000269|PubMed:1711374}.
CC -!- DEVELOPMENTAL STAGE: In spermatids, isoform 1 is expressed until
CC spermatids become elutriated, whereafter isoform 2 is expressed.
CC {ECO:0000269|PubMed:14514679}.
CC -!- PTM: Asn-3 is deaminated to Asp in more than 25% of the proteins,
CC giving rise to 2 major isoelectric variants, called CB and CA
CC respectively (0.4 pH unit change). Deamidation proceeds via the so-
CC called beta-aspartyl shift mechanism and yields either 'D-Asp-2'
CC (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation
CC occurs after the addition of myristate. The Asn-3 form reaches a
CC significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form.
CC {ECO:0000269|PubMed:9521123}.
CC -!- PTM: Autophosphorylated. Phosphorylation is enhanced by vitamin K(2).
CC Phosphorylated on threonine and serine residues. Phosphorylation on
CC Thr-198 is required for full activity (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Tyr-331 by activated receptor tyrosine kinases
CC EGFR and PDGFR; this increases catalytic efficiency. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR EMBL; X57986; CAA41052.1; -; mRNA.
DR EMBL; AY375243; AAQ81631.1; -; mRNA.
DR PIR; S16240; OKRT2C.
DR AlphaFoldDB; P27791; -.
DR BMRB; P27791; -.
DR SMR; P27791; -.
DR CORUM; P27791; -.
DR DIP; DIP-37312N; -.
DR IntAct; P27791; 5.
DR MINT; P27791; -.
DR STRING; 10116.ENSRNOP00000044732; -.
DR BindingDB; P27791; -.
DR ChEMBL; CHEMBL3390; -.
DR GuidetoPHARMACOLOGY; 1476; -.
DR iPTMnet; P27791; -.
DR PhosphoSitePlus; P27791; -.
DR jPOST; P27791; -.
DR PaxDb; P27791; -.
DR PRIDE; P27791; -.
DR RGD; 3389; Prkaca.
DR eggNOG; KOG0616; Eukaryota.
DR InParanoid; P27791; -.
DR PhylomeDB; P27791; -.
DR BRENDA; 2.7.11.11; 5301.
DR Reactome; R-RNO-163615; PKA activation.
DR Reactome; R-RNO-164378; PKA activation in glucagon signalling.
DR Reactome; R-RNO-180024; DARPP-32 events.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-RNO-392517; Rap1 signalling.
DR Reactome; R-RNO-422356; Regulation of insulin secretion.
DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-RNO-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-RNO-5610787; Hedgehog 'off' state.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-8853659; RET signaling.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR Reactome; R-RNO-8963896; HDL assembly.
DR Reactome; R-RNO-9634597; GPER1 signaling.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P27791; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0097546; C:ciliary base; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0016607; C:nuclear speck; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0044853; C:plasma membrane raft; ISO:RGD.
DR GO; GO:0098793; C:presynapse; IMP:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:RGD.
DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR GO; GO:0030145; F:manganese ion binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0070417; P:cellular response to cold; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; ISO:RGD.
DR GO; GO:0042747; P:circadian sleep/wake cycle, REM sleep; IEP:RGD.
DR GO; GO:0001707; P:mesoderm formation; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; ISO:RGD.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IDA:RGD.
DR GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; ISO:RGD.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central.
DR GO; GO:1990044; P:protein localization to lipid droplet; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0043457; P:regulation of cellular respiration; IDA:RGD.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:RGD.
DR GO; GO:0070613; P:regulation of protein processing; ISO:RGD.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IDA:RGD.
DR GO; GO:0048240; P:sperm capacitation; ISO:RGD.
DR GO; GO:0048792; P:spontaneous exocytosis of neurotransmitter; IMP:UniProtKB.
DR CDD; cd14209; STKc_PKA; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR044109; STKc_PKA.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; cAMP; Cell membrane; Cell projection;
KW Cilium; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW Flagellum; Kinase; Lipoprotein; Membrane; Mitochondrion; Myristate;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9521123"
FT CHAIN 2..351
FT /note="cAMP-dependent protein kinase catalytic subunit
FT alpha"
FT /id="PRO_0000086055"
FT DOMAIN 44..298
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 299..351
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 50..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 122..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 169..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 3
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000269|PubMed:9521123"
FT MOD_RES 11
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P05132"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17612"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05132"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17612"
FT MOD_RES 198
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:P00517"
FT MOD_RES 331
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05132"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:9521123"
FT VAR_SEQ 1..15
FT /note="MGNAAAAKKGSEQES -> MASNSND (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14514679"
FT /id="VSP_013277"
SQ SEQUENCE 351 AA; 40620 MW; 4763ACD074AB2384 CRC64;
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WEDPSQNTAQ LDHFDRIKTL GTGSFGRVML
VKHKESGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV
MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY
IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT
TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFTE F
