DMPK_MOUSE
ID DMPK_MOUSE Reviewed; 631 AA.
AC P54265;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Myotonin-protein kinase;
DE Short=MT-PK;
DE EC=2.7.11.1;
DE AltName: Full=DM-kinase;
DE Short=DMK;
DE AltName: Full=DMPK;
DE AltName: Full=Myotonic dystrophy protein kinase;
DE Short=MDPK;
GN Name=Dmpk; Synonyms=Dm15, Mdpk;
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 [GENOMIC DNA].
RX PubMed=8499920; DOI=10.1093/hmg/2.3.299;
RA Mahadevan M.S., Amemiya C., Jansen G., Sabourin L., Baird S., Neville C.E.,
RA Wormskamp N., Segers B., Batzer M., Lamerdin J., de Jong P.J., Wieringa B.,
RA Korneluk R.G.;
RT "Structure and genomic sequence of the myotonic dystrophy (DM kinase)
RT gene.";
RL Hum. Mol. Genet. 2:299-304(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=8401505; DOI=10.1093/hmg/2.8.1221;
RA Jansen G., Bartolomei M., Kalscheuer V., Merkx G., Wormskamp N.,
RA Mariman E., Smeets D., Ropers H.-H., Wieringa B.;
RT "No imprinting involved in the expression of DM-kinase mRNAs in mouse and
RT human tissues.";
RL Hum. Mol. Genet. 2:1221-1227(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 117-631 (ISOFORMS 2; 4; 5 AND 8).
RC TISSUE=Brain;
RX PubMed=1302022; DOI=10.1038/ng0792-261;
RA Jansen G., Mahadevan M.S., Amemiya C., Wormskamp N., Segers B.,
RA Hendriks W., O'Hoy K., Baird S., Sabourin L., Lennon G., Jap P.L., Iles D.,
RA Coerwinkel M., Hofker M., Carrano A.V., de Jong P.J., Korneluk R.G.,
RA Wieringa B.;
RT "Characterization of the myotonic dystrophy region predicts multiple
RT protein isoform-encoding mRNAs.";
RL Nat. Genet. 1:261-266(1992).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=8673132; DOI=10.1038/ng0796-325;
RA Reddy S., Smith D.B., Rich M.M., Leferovich J.M., Reilly P., Davis B.M.,
RA Tran K., Rayburn H., Bronson R., Cros D., Balice-Gordon R.J., Housman D.;
RT "Mice lacking the myotonic dystrophy protein kinase develop a late onset
RT progressive myopathy.";
RL Nat. Genet. 13:325-335(1996).
RN [5]
RP FUNCTION IN CELLULAR CALCIUM HOMEOSTASIS.
RX PubMed=9294109; DOI=10.1172/jci119664;
RA Benders A.A., Groenen P.J., Oerlemans F.T., Veerkamp J.H., Wieringa B.;
RT "Myotonic dystrophy protein kinase is involved in the modulation of the
RT Ca2+ homeostasis in skeletal muscle cells.";
RL J. Clin. Invest. 100:1440-1447(1997).
RN [6]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 3; 5; 6; 8 AND 9).
RX PubMed=10699184; DOI=10.1093/hmg/9.4.605;
RA Groenen P.J.T.A., Wansink D.G., Coerwinkel M., van den Broek W., Jansen G.,
RA Wieringa B.;
RT "Constitutive and regulated modes of splicing produce six major myotonic
RT dystrophy protein kinase (DMPK) isoforms with distinct properties.";
RL Hum. Mol. Genet. 9:605-616(2000).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=10936001; DOI=10.1023/a:1009842114968;
RA Berul C.I., Maguire C.T., Gehrmann J., Reddy S.;
RT "Progressive atrioventricular conduction block in a mouse myotonic
RT dystrophy model.";
RL J. Interv. Card. Electrophysiol. 4:351-358(2000).
RN [8]
RP FUNCTION IN SYNAPTIC PLASTICITY.
RX PubMed=12612014; DOI=10.1152/jn.00504.2002;
RA Schulz P.E., McIntosh A.D., Kasten M.R., Wieringa B., Epstein H.F.;
RT "A role for myotonic dystrophy protein kinase in synaptic plasticity.";
RL J. Neurophysiol. 89:1177-1186(2003).
RN [9]
RP FUNCTION IN CALCIUM UPTAKE BY CARDIAC SARCOPLASMIC RETICULUM, FUNCTION IN
RP PHOSPHORYLATION OF PLN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15598648; DOI=10.1074/jbc.m412845200;
RA Kaliman P., Catalucci D., Lam J.T., Kondo R., Gutierrez J.C., Reddy S.,
RA Palacin M., Zorzano A., Chien K.R., Ruiz-Lozano P.;
RT "Myotonic dystrophy protein kinase phosphorylates phospholamban and
RT regulates calcium uptake in cardiomyocyte sarcoplasmic reticulum.";
RL J. Biol. Chem. 280:8016-8021(2005).
RN [10]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP AUTOPHOSPHORYLATION.
RX PubMed=15684391; DOI=10.1128/mcb.25.4.1402-1414.2005;
RA van Herpen R.E., Oude Ophuis R.J., Wijers M., Bennink M.B.,
RA van de Loo F.A., Fransen J., Wieringa B., Wansink D.G.;
RT "Divergent mitochondrial and endoplasmic reticulum association of DMPK
RT splice isoforms depends on unique sequence arrangements in tail anchors.";
RL Mol. Cell. Biol. 25:1402-1414(2005).
RN [11]
RP FUNCTION IN MYOGENESIS, AND SUBCELLULAR LOCATION.
RX PubMed=18729234; DOI=10.1002/dvdy.21653;
RA Harmon E.B., Harmon M.L., Larsen T.D., Paulson A.F., Perryman M.B.;
RT "Myotonic dystrophy protein kinase is expressed in embryonic myocytes and
RT is required for myotube formation.";
RL Dev. Dyn. 237:2353-2366(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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 [13]
RP FUNCTION IN NUCLEAR ENVELOPE STABILITY, AND SUBCELLULAR LOCATION.
RX PubMed=21949239; DOI=10.1074/jbc.m111.241455;
RA Harmon E.B., Harmon M.L., Larsen T.D., Yang J., Glasford J.W.,
RA Perryman M.B.;
RT "Myotonic dystrophy protein kinase is critical for nuclear envelope
RT integrity.";
RL J. Biol. Chem. 286:40296-40306(2011).
CC -!- FUNCTION: Non-receptor serine/threonine protein kinase which is
CC necessary for the maintenance of skeletal muscle structure and
CC function. May play a role in myocyte differentiation and survival by
CC regulating the integrity of the nuclear envelope and the expression of
CC muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the
CC myosin phosphatase activity to regulate myosin phosphorylation. Also
CC critical to the modulation of cardiac contractility and to the
CC maintenance of proper cardiac conduction activity probably through the
CC regulation of cellular calcium homeostasis. Phosphorylates PLN, a
CC regulator of calcium pumps and may regulate sarcoplasmic reticulum
CC calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is
CC able to induce chloride currents. May also play a role in synaptic
CC plasticity. {ECO:0000269|PubMed:12612014, ECO:0000269|PubMed:15598648,
CC ECO:0000269|PubMed:18729234, ECO:0000269|PubMed:21949239,
CC ECO:0000269|PubMed:9294109}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Coiled-coil-mediated oligomerization enhances the
CC catalytic activity. Proteolytic processing of the C-terminus may
CC release the protein from membranes and constitute a mean to regulate
CC the enzyme. May be regulated by HSPB2, RAC1, RAF1 and G-protein second
CC messengers (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; homodimerization stimulates the kinase activity.
CC Interacts with HSPB2; may enhance DMPK kinase activity. Interacts with
CC PLN; phosphorylates PLN. May interact with RAC1; may regulate DMPK
CC kinase activity. Interacts with LMNA; may regulate nuclear envelope
CC stability (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane. Cell membrane.
CC Note=Localizes to sarcoplasmic reticulum membranes of cardiomyocytes.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane;
CC Single-pass type IV membrane protein; Cytoplasmic side. Nucleus outer
CC membrane; Single-pass type IV membrane protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Mitochondrion outer membrane;
CC Single-pass type IV membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytosol.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=DMPK A;
CC IsoId=P54265-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54265-2; Sequence=VSP_004819;
CC Name=3; Synonyms=DMPK B;
CC IsoId=P54265-3; Sequence=VSP_004820;
CC Name=4;
CC IsoId=P54265-4; Sequence=VSP_004820, VSP_004821, VSP_004822;
CC Name=5; Synonyms=DMPK E;
CC IsoId=P54265-5; Sequence=VSP_004823, VSP_004824;
CC Name=6; Synonyms=DMPK F;
CC IsoId=P54265-6; Sequence=VSP_004820, VSP_004823, VSP_004824;
CC Name=7;
CC IsoId=P54265-7; Sequence=VSP_004825, VSP_004826;
CC Name=8; Synonyms=DMPK C;
CC IsoId=P54265-8; Sequence=VSP_004827;
CC Name=9; Synonyms=DMPK D;
CC IsoId=P54265-9; Sequence=VSP_004820, VSP_004827;
CC Name=10;
CC IsoId=P54265-10; Sequence=VSP_004828, VSP_004829;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, with a
CC predominance in brain, skeletal muscle, heart, and other tissues
CC containing smooth muscle. In the heart, expression is restricted to the
CC cardiomyocytes in the ventricle and atrium.
CC {ECO:0000269|PubMed:15598648}.
CC -!- DEVELOPMENTAL STAGE: Primarily detected in striated muscle structures
CC of the 14.5 day embryo, including all major muscles in the skeletal
CC structures, cardiac muscle, diaphragm, and the smooth muscle of the
CC lung and gut. {ECO:0000269|PubMed:15598648}.
CC -!- DOMAIN: The coiled coil domain is required for homodimerization and
CC regulates the enzymatic activity. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Autophosphorylates. Phosphorylation by RAF1 may
CC result in activation of DMPK (By similarity). {ECO:0000250}.
CC -!- PTM: Proteolytic processing of the C-terminus may remove the
CC transmembrane domain and release the kinase from membranes stimulating
CC its activity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are fertile and no negative selection
CC against the absence of the protein is apparent. Newborn do not display
CC hypotonia, respiratory distress or gross anatomical abnormalities.
CC However, a progressive muscle weakness a hall mark of myopathies is
CC observed. Muscles from mature mice show variation in fiber size,
CC increase fiber degeneration and fibrosis. They also display age-related
CC progression in atrioventricular conduction defects that are reminiscent
CC of congenital myotonic dystrophy. {ECO:0000269|PubMed:10936001,
CC ECO:0000269|PubMed:8673132}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z21503; CAA79715.1; -; Genomic_DNA.
DR EMBL; Z21504; CAA79715.1; JOINED; Genomic_DNA.
DR EMBL; Z21505; CAA79715.1; JOINED; Genomic_DNA.
DR EMBL; Z21506; CAA79715.1; JOINED; Genomic_DNA.
DR EMBL; Z38015; CAA86113.1; -; Genomic_DNA.
DR EMBL; S60313; AAC60667.1; -; mRNA.
DR EMBL; S60314; AAC60666.1; -; mRNA.
DR EMBL; S60315; AAC60665.1; -; mRNA.
DR EMBL; S60316; AAC60664.1; -; mRNA.
DR CCDS; CCDS39794.1; -. [P54265-1]
DR CCDS; CCDS52054.1; -. [P54265-5]
DR CCDS; CCDS90170.1; -. [P54265-9]
DR PIR; I78393; I78393.
DR PIR; I78394; I78394.
DR PIR; I78395; I78395.
DR PIR; I78396; I78396.
DR PIR; S71829; S71829.
DR RefSeq; NP_001177420.1; NM_001190491.1. [P54265-5]
DR RefSeq; NP_115794.1; NM_032418.2. [P54265-1]
DR RefSeq; XP_006539581.1; XM_006539518.3.
DR RefSeq; XP_006539582.1; XM_006539519.3. [P54265-3]
DR RefSeq; XP_011248735.1; XM_011250433.2.
DR AlphaFoldDB; P54265; -.
DR SMR; P54265; -.
DR STRING; 10090.ENSMUSP00000032568; -.
DR iPTMnet; P54265; -.
DR PhosphoSitePlus; P54265; -.
DR MaxQB; P54265; -.
DR PaxDb; P54265; -.
DR PeptideAtlas; P54265; -.
DR PRIDE; P54265; -.
DR ProteomicsDB; 279443; -. [P54265-1]
DR ProteomicsDB; 279444; -. [P54265-2]
DR ProteomicsDB; 279445; -. [P54265-3]
DR ProteomicsDB; 279446; -. [P54265-4]
DR ProteomicsDB; 279447; -. [P54265-5]
DR ProteomicsDB; 279448; -. [P54265-6]
DR ProteomicsDB; 279449; -. [P54265-7]
DR ProteomicsDB; 279450; -. [P54265-8]
DR ProteomicsDB; 279451; -. [P54265-9]
DR ProteomicsDB; 279452; -. [P54265-10]
DR Antibodypedia; 2044; 301 antibodies from 30 providers.
DR DNASU; 13400; -.
DR Ensembl; ENSMUST00000032568; ENSMUSP00000032568; ENSMUSG00000030409. [P54265-1]
DR Ensembl; ENSMUST00000108473; ENSMUSP00000104113; ENSMUSG00000030409. [P54265-5]
DR Ensembl; ENSMUST00000238982; ENSMUSP00000158930; ENSMUSG00000030409. [P54265-9]
DR GeneID; 13400; -.
DR KEGG; mmu:13400; -.
DR UCSC; uc009fkn.2; mouse. [P54265-1]
DR UCSC; uc009fkp.2; mouse. [P54265-5]
DR UCSC; uc009fkq.2; mouse. [P54265-8]
DR CTD; 1760; -.
DR MGI; MGI:94906; Dmpk.
DR VEuPathDB; HostDB:ENSMUSG00000030409; -.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT00940000162019; -.
DR HOGENOM; CLU_000288_140_4_1; -.
DR InParanoid; P54265; -.
DR OMA; EYFEFPP; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; P54265; -.
DR TreeFam; TF105337; -.
DR BRENDA; 2.7.11.1; 3474.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR BioGRID-ORCS; 13400; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Dmpk; mouse.
DR PRO; PR:P54265; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P54265; protein.
DR Bgee; ENSMUSG00000030409; Expressed in myocardium of ventricle and 203 other tissues.
DR ExpressionAtlas; P54265; baseline and differential.
DR Genevisible; P54265; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017020; F:myosin phosphatase regulator activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0010657; P:muscle cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0014853; P:regulation of excitatory postsynaptic membrane potential involved in skeletal muscle contraction; IMP:MGI.
DR GO; GO:0008016; P:regulation of heart contraction; IDA:UniProtKB.
DR GO; GO:0010830; P:regulation of myotube differentiation; IMP:UniProtKB.
DR GO; GO:0014722; P:regulation of skeletal muscle contraction by calcium ion signaling; IMP:UniProtKB.
DR GO; GO:0002028; P:regulation of sodium ion transport; IMP:MGI.
DR GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:UniProtKB.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF08826; DMPK_coil; 1.
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; Cell membrane; Coiled coil; Cytoplasm;
KW Endoplasmic reticulum; Kinase; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Sarcoplasmic reticulum;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..631
FT /note="Myotonin-protein kinase"
FT /id="PRO_0000085925"
FT TOPO_DOM 1..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 614..631
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 71..339
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 340..415
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT COILED 464..532
FT /evidence="ECO:0000255"
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 77..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 216
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 228
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 234
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT VAR_SEQ 328..356
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1302022"
FT /id="VSP_004819"
FT VAR_SEQ 378..382
FT /note="Missing (in isoform 3, isoform 4, isoform 6 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:1302022"
FT /id="VSP_004820"
FT VAR_SEQ 412..416
FT /note="DNQVP -> LKRPT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1302022"
FT /id="VSP_004821"
FT VAR_SEQ 417..631
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1302022"
FT /id="VSP_004822"
FT VAR_SEQ 536..557
FT /note="AITGVPSPRATDPPSHLDGPPA -> GESLTCFQPRGHWVEMGGMLGV (in
FT isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_004825"
FT VAR_SEQ 536..537
FT /note="AI -> DP (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:1302022"
FT /id="VSP_004823"
FT VAR_SEQ 538..631
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:1302022"
FT /id="VSP_004824"
FT VAR_SEQ 552..631
FT /note="LDGPPAVAVGQCPLVGPGPMHRRHLLLPARIPRPGLSEARCLLLFAAALAAA
FT ATLGCTGLVAYTGGLTPVWCFPGATFAP -> MAPRPWLWASARWWGQAPCTAVTCCSL
FT PGSLGLAYPRRVACSCSPLLWLLPPHWAALGWWPIPAVSPQSGVSREPPSPPEP (in
FT isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:1302022"
FT /id="VSP_004827"
FT VAR_SEQ 552..562
FT /note="LDGPPAVAVGQ -> ASRQILPKGTP (in isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_004828"
FT VAR_SEQ 558..631
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_004826"
FT VAR_SEQ 563..631
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_004829"
SQ SEQUENCE 631 AA; 69602 MW; 5EE800A37EA81DF4 CRC64;
MSAEVRLRQL QQLVLDPGFL GLEPLLDLLL GVHQELGASH LAQDKYVADF LQWVEPIAAR
LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR GEVSCFREER
DVLVKGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE MARFYLAEIV
MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL QPDGMVRSLV AVGTPDYLSP
EILQAVGGGP GAGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYAKI VHYREHLSLP
LADTVVPEEA QDLIRGLLCP AEIRLGRGGA GDFQKHPFFF GLDWEGLRDS VPPFTPDFEG
ATDTCNFDVV EDRLTAMVSG GGETLSDMQE DMPLGVRLPF VGYSYCCMAF RDNQVPDPTP
MELEALQLPV SDLQGLDLQP PVSPPDQVAE EADLVAVPAP VAEAETTVTL QQLQEALEEE
VLTRQSLSRE LEAIRTANQN FSSQLQEAEV RNRDLEAHVR QLQERMEMLQ APGAAAITGV
PSPRATDPPS HLDGPPAVAV GQCPLVGPGP MHRRHLLLPA RIPRPGLSEA RCLLLFAAAL
AAAATLGCTG LVAYTGGLTP VWCFPGATFA P
