KCC2D_RAT
ID KCC2D_RAT Reviewed; 533 AA.
AC P15791; P97915; P97916; Q3B7L0; Q63904; Q63905; Q63906; Q63907; Q63908;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit delta;
DE Short=CaM kinase II subunit delta;
DE Short=CaMK-II subunit delta;
DE EC=2.7.11.17;
GN Name=Camk2d;
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 DELTA 1).
RX PubMed=2553697; DOI=10.1016/s0021-9258(19)84658-6;
RA Tobimatsu T., Fujisawa H.;
RT "Tissue-specific expression of four types of rat calmodulin-dependent
RT protein kinase II mRNAs.";
RL J. Biol. Chem. 264:17907-17912(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA 2).
RC TISSUE=Prostate;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 314-533 (ISOFORMS DELTA 2; DELTA 3 AND DELTA
RP 4).
RC STRAIN=Sprague-Dawley; TISSUE=Aorta, and Skeletal muscle;
RX PubMed=8390994; DOI=10.1016/s0021-9258(19)85259-6;
RA Schworer C.M., Rothblum L.I., Thekkumkara T.J., Singer H.A.;
RT "Identification of novel isoforms of the delta subunit of Ca2+/calmodulin-
RT dependent protein kinase II. Differential expression in rat brain and
RT aorta.";
RL J. Biol. Chem. 268:14443-14449(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 307-533 (ISOFORMS DELTA 1; DELTA 2;
RP DELTA 4; DELTA 5; DELTA 6 AND DELTA 7).
RX PubMed=8224201; DOI=10.1016/0014-5793(93)80678-n;
RA Mayer P., Moehlig M., Schatz H., Pfeiffer A.;
RT "New isoforms of multifunctional calcium/calmodulin-dependent protein
RT kinase II.";
RL FEBS Lett. 333:315-318(1993).
RN [5]
RP FUNCTION IN PHOSPHORYLATION OF PLN/PLB.
RX PubMed=10825152; DOI=10.1074/jbc.c000253200;
RA Hagemann D., Kuschel M., Kuramochi T., Zhu W., Cheng H., Xiao R.P.;
RT "Frequency-encoding Thr17 phospholamban phosphorylation is independent of
RT Ser16 phosphorylation in cardiac myocytes.";
RL J. Biol. Chem. 275:22532-22536(2000).
RN [6]
RP INDUCTION BY COCAINE.
RX PubMed=16891908; DOI=10.1097/01.fjc.0000211796.45281.46;
RA Henning R.J., Cuevas J.;
RT "Cocaine activates calcium/calmodulin kinase II and causes cardiomyocyte
RT hypertrophy.";
RL J. Cardiovasc. Pharmacol. 48:802-813(2006).
RN [7]
RP INTERACTION WITH RRAD.
RX PubMed=18056528; DOI=10.1161/circulationaha.107.707257;
RA Chang L., Zhang J., Tseng Y.-H., Xie C.-Q., Ilany J., Bruning J.C., Sun Z.,
RA Zhu X., Cui T., Youker K.A., Yang Q., Day S.M., Kahn C.R., Chen Y.E.;
RT "Rad GTPase deficiency leads to cardiac hypertrophy.";
RL Circulation 116:2976-2983(2007).
RN [8]
RP FUNCTION IN PHOSPHORYLATION OF HDAC4 AND RYR2.
RX PubMed=17923476; DOI=10.1074/jbc.m707083200;
RA Zhang T., Kohlhaas M., Backs J., Mishra S., Phillips W., Dybkova N.,
RA Chang S., Ling H., Bers D.M., Maier L.S., Olson E.N., Brown J.H.;
RT "CaMKIIdelta isoforms differentially affect calcium handling but similarly
RT regulate HDAC/MEF2 transcriptional responses.";
RL J. Biol. Chem. 282:35078-35087(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND THR-371, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase involved in the
CC regulation of Ca(2+) homeostatis and excitation-contraction coupling
CC (ECC) in heart by targeting ion channels, transporters and accessory
CC proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release
CC from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and
CC K(+) channel transport. Targets also transcription factors and
CC signaling molecules to regulate heart function. In its activated form,
CC is involved in the pathogenesis of dilated cardiomyopathy and heart
CC failure. Contributes to cardiac decompensation and heart failure by
CC regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+)
CC channel on 'Ser-2808'. In the nucleus, phosphorylates the MEF2
CC repressor HDAC4, promoting its nuclear export and binding to 14-3-3
CC protein, and expression of MEF2 and genes involved in the hypertrophic
CC program. Is essential for left ventricular remodeling responses to
CC myocardial infarction. In pathological myocardial remodeling acts
CC downstream of the beta adrenergic receptor signaling cascade to
CC regulate key proteins involved in ECC. Regulates Ca(2+) influx to
CC myocytes by binding and phosphorylating the L-type Ca(2+) channel
CC subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and
CC regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+
CC channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart
CC failure. Phosphorylates phospholamban (PLN/PLB), an endogenous
CC inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR
CC Ca(2+) uptake that may be important in frequency-dependent acceleration
CC of relaxation (FDAR) and maintenance of contractile function during
CC acidosis. May participate in the modulation of skeletal muscle function
CC in response to exercise, by regulating SR Ca(2+) transport through
CC phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling
CC factor (By similarity). {ECO:0000250, ECO:0000269|PubMed:10825152,
CC ECO:0000269|PubMed:17923476}.
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=2.7.11.17;
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=2.7.11.17;
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC calmodulin results in conformational change that relieves intrasteric
CC autoinhibition and allows autophosphorylation of Thr-287 which turns
CC the kinase in a constitutively active form and confers to the kinase a
CC Ca(2+)-independent activity.
CC -!- SUBUNIT: CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta
CC (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms
CC assemble into homo- or heteromultimeric holoenzymes composed of 12
CC subunits with two hexameric rings stacked one on top of the other.
CC Interacts with RRAD and CACNB2. {ECO:0000269|PubMed:18056528}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Sarcoplasmic reticulum membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform Delta 1]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=Delta 1;
CC IsoId=P15791-1; Sequence=Displayed;
CC Name=Delta 2;
CC IsoId=P15791-2; Sequence=VSP_004784;
CC Name=Delta 3;
CC IsoId=P15791-3; Sequence=VSP_004785, VSP_004786, VSP_004787;
CC Name=Delta 4;
CC IsoId=P15791-4; Sequence=VSP_004788;
CC Name=Delta 5;
CC IsoId=P15791-5; Sequence=VSP_004784, VSP_012043;
CC Name=Delta 6;
CC IsoId=P15791-6; Sequence=VSP_012043;
CC Name=Delta 7;
CC IsoId=P15791-7; Sequence=VSP_004788, VSP_012043;
CC -!- TISSUE SPECIFICITY: Isoform Delta 1 is the predominant form in the
CC brain, isoform Delta 2 and isoform Delta 3 predominate in the aorta and
CC isoform Delta 4 in skeletal muscle.
CC -!- INDUCTION: By cocaine in cardiomyocytes. {ECO:0000269|PubMed:16891908}.
CC -!- DOMAIN: The CAMK2 protein kinases contain a unique C-terminal subunit
CC association domain responsible for oligomerization.
CC -!- PTM: Autophosphorylation of Thr-287 following activation by
CC Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an
CC activated state (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; J05072; AAA40866.1; -; mRNA.
DR EMBL; BC107562; AAI07563.1; -; mRNA.
DR EMBL; L13406; AAA41479.1; -; mRNA.
DR EMBL; L13407; AAA41480.1; -; mRNA.
DR EMBL; L13408; AAA41481.1; -; mRNA.
DR EMBL; X77192; CAA54412.1; -; Genomic_DNA.
DR EMBL; X77193; CAA54413.1; -; Genomic_DNA.
DR EMBL; X77194; CAA54414.1; -; Genomic_DNA.
DR EMBL; X77195; CAA54415.1; -; Genomic_DNA.
DR EMBL; X75774; CAA53395.1; -; Genomic_DNA.
DR PIR; A34366; A34366.
DR RefSeq; NP_036651.1; NM_012519.2. [P15791-1]
DR RefSeq; XP_017446093.1; XM_017590604.1. [P15791-1]
DR RefSeq; XP_017446094.1; XM_017590605.1. [P15791-1]
DR RefSeq; XP_017446095.1; XM_017590606.1. [P15791-1]
DR RefSeq; XP_017446099.1; XM_017590610.1. [P15791-4]
DR RefSeq; XP_017446100.1; XM_017590611.1. [P15791-4]
DR RefSeq; XP_017446102.1; XM_017590613.1. [P15791-6]
DR RefSeq; XP_017446106.1; XM_017590617.1. [P15791-2]
DR AlphaFoldDB; P15791; -.
DR SMR; P15791; -.
DR BioGRID; 246431; 7.
DR IntAct; P15791; 5.
DR MINT; P15791; -.
DR STRING; 10116.ENSRNOP00000016026; -.
DR BindingDB; P15791; -.
DR ChEMBL; CHEMBL4296090; -.
DR iPTMnet; P15791; -.
DR PhosphoSitePlus; P15791; -.
DR jPOST; P15791; -.
DR PaxDb; P15791; -.
DR PRIDE; P15791; -.
DR Ensembl; ENSRNOT00000015564; ENSRNOP00000015559; ENSRNOG00000011589. [P15791-5]
DR Ensembl; ENSRNOT00000016026; ENSRNOP00000016026; ENSRNOG00000011589. [P15791-1]
DR Ensembl; ENSRNOT00000103949; ENSRNOP00000095840; ENSRNOG00000011589. [P15791-6]
DR GeneID; 24246; -.
DR KEGG; rno:24246; -.
DR CTD; 817; -.
DR RGD; 2263; Camk2d.
DR eggNOG; KOG0033; Eukaryota.
DR GeneTree; ENSGT00940000159769; -.
DR HOGENOM; CLU_000288_71_0_1; -.
DR InParanoid; P15791; -.
DR OMA; CIPNGRE; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; P15791; -.
DR BRENDA; 2.7.11.17; 5301.
DR Reactome; R-RNO-3371571; HSF1-dependent transactivation.
DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR Reactome; R-RNO-5673000; RAF activation.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-877300; Interferon gamma signaling.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR PRO; PR:P15791; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011589; Expressed in cerebellum and 19 other tissues.
DR Genevisible; P15791; RN.
DR GO; GO:0043194; C:axon initial segment; ISO:RGD.
DR GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030315; C:T-tubule; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; IMP:CACAO.
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:0019871; F:sodium channel inhibitor activity; ISO:RGD.
DR GO; GO:0031432; F:titin binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IDA:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0086003; P:cardiac muscle cell contraction; IDA:BHF-UCL.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IMP:RGD.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:RGD.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:1902306; P:negative regulation of sodium ion transmembrane transport; ISO:RGD.
DR GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:RGD.
DR GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IMP:RGD.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IDA:BHF-UCL.
DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; IDA:BHF-UCL.
DR GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; IC:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IC:BHF-UCL.
DR GO; GO:0010649; P:regulation of cell communication by electrical coupling; IDA:BHF-UCL.
DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IC:BHF-UCL.
DR GO; GO:0060341; P:regulation of cellular localization; ISS:UniProtKB.
DR GO; GO:0003254; P:regulation of membrane depolarization; ISO:RGD.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IGI:ARUK-UCL.
DR GO; GO:1901897; P:regulation of relaxation of cardiac muscle; IDA:BHF-UCL.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISO:RGD.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IDA:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IMP:RGD.
DR InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF08332; CaMKII_AD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF56112; SSF56112; 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 Acetylation; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Cell membrane; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Sarcoplasmic reticulum;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13557"
FT CHAIN 2..533
FT /note="Calcium/calmodulin-dependent protein kinase type II
FT subunit delta"
FT /id="PRO_0000086100"
FT DOMAIN 14..272
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 283..292
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT REGION 291..301
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 337..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13557"
FT MOD_RES 287
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13557"
FT MOD_RES 306
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 307
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13557"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PHZ2"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13557"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13557"
FT MOD_RES 365
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13557"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 370
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PHZ2"
FT MOD_RES 371
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13557"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PHZ2"
FT VAR_SEQ 329..362
FT /note="Missing (in isoform Delta 2 and isoform Delta 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8390994"
FT /id="VSP_004784"
FT VAR_SEQ 329..335
FT /note="INNKANV -> KRKSSSV (in isoform Delta 3)"
FT /evidence="ECO:0000303|PubMed:8390994"
FT /id="VSP_004785"
FT VAR_SEQ 337..359
FT /note="Missing (in isoform Delta 3)"
FT /evidence="ECO:0000303|PubMed:8390994"
FT /id="VSP_004786"
FT VAR_SEQ 349..362
FT /note="Missing (in isoform Delta 4 and isoform Delta 7)"
FT /evidence="ECO:0000303|PubMed:8390994"
FT /id="VSP_004788"
FT VAR_SEQ 360..362
FT /note="GNK -> QMM (in isoform Delta 3)"
FT /evidence="ECO:0000303|PubMed:8390994"
FT /id="VSP_004787"
FT VAR_SEQ 512..533
FT /note="KPPCIPNGKENFSGGTSLWQNI -> N (in isoform Delta 5,
FT isoform Delta 6 and isoform Delta 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_012043"
SQ SEQUENCE 533 AA; 60081 MW; E41BCB2B5A00E7CA CRC64;
MASTTTCTRF TDEYQLFEEL GKGAFSVVRR CMKIPTGQEY AAKIINTKKL SARDHQKLER
EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI
LESVNHCHLN GIVHRDLKPE NLLLASKSKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY
LSPEVLRKDP YGKPVDMWAC GVILYILLVG YPPFWDEDQH RLYQQIKAGA YDFPSPEWDT
VTPEAKDLIN KMLTINPAKR ITASEALKHP WICQRSTVAS MMHRQETVDC LKKFNARRKL
KGAILTTMLA TRNFSAAKSL LKKPDGVKIN NKANVVTSPK ENIPTPALEP QTTVIHNPDG
NKESTESSNT TIEDEDVKAR KQEIIKVTEQ LIEAINNGDF EAYTKICDPG LTAFEPEALG
NLVEGMDFHR FYFENALPKI NKPIHTIILN PHVHLVGDDA ACIAYIRLTQ YMDGNGMPKT
MQSEETRVWH RRDGKWQNIH FHRSGSPTVP IKPPCIPNGK ENFSGGTSLW QNI
