ID MYLK_CHICK Reviewed; 1906 AA.
AC P11799; P19038; Q549S2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 27-MAR-2024, entry version 214.
DE RecName: Full=Myosin light chain kinase, smooth muscle;
DE Short=MLCK;
DE EC=2.7.11.18;
DE AltName: Full=Telokin;
DE Contains:
DE RecName: Full=Myosin light chain kinase, smooth muscle, deglutamylated form;
GN Name=Mylk;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=7589469; DOI=10.1016/0014-5793(95)01048-j;
RA Watterson D.M., Collinge M., Lukas T.J., van Eldik L.J., Birukov K.G.,
RA Stepanova O.V., Shirinsky V.P.;
RT "Multiple gene products are produced from a novel protein kinase
RT transcription region.";
RL FEBS Lett. 373:217-220(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2315320; DOI=10.1073/pnas.87.6.2284;
RA Olson N.J., Pearson R.B., Needleman D.S., Hurwitz M.J., Kemp B.E.,
RA Means A.R.;
RT "Regulatory and structural motifs of chicken gizzard myosin light chain
RT kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2284-2288(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=9706877;
RX DOI=10.1002/(sici)1097-4644(19980901)70:3<402::aid-jcb13>3.3.co;2-4;
RA Birukov K.G., Schavocky J.P., Shirinsky V.P., Van Eldik L.J.,
RA Watterson D.M.;
RT "The organization of the genetic locus for chicken myosin light chain
RT kinase is complex: multiple proteins are encoded and exhibit differential
RT expression and localization.";
RL J. Cell. Biochem. 70:402-413(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 649-1906, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fibroblast;
RX PubMed=2202734; DOI=10.1083/jcb.111.3.1107;
RA Shoemaker M.O., Lau W., Shattuck R.L., Kwiatkowski A.P., Matrisian P.E.,
RA Guerra-Santos L., Wilson E., Lukas T.J., van Eldik L.J., Watterson D.M.;
RT "Use of DNA sequence and mutant analyses and antisense
RT oligodeoxynucleotides to examine the molecular basis of nonmuscle myosin
RT light chain kinase autoinhibition, calmodulin recognition, and activity.";
RL J. Cell Biol. 111:1107-1125(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1259-1906.
RC TISSUE=Gizzard;
RX PubMed=3030394; DOI=10.1021/bi00374a007;
RA Guerriero V. Jr., Russo M.A., Olson N.J., Putkey J.A., Means A.R.;
RT "Domain organization of chicken gizzard myosin light chain kinase deduced
RT from a cloned cDNA.";
RL Biochemistry 25:8372-8381(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1750-1906 (ISOFORM 3).
RC TISSUE=Gizzard;
RX PubMed=1444462; DOI=10.1016/0003-9861(92)90270-7;
RA Yoshikai S., Ikebe M.;
RT "Molecular cloning of the chicken gizzard telokin gene and cDNA.";
RL Arch. Biochem. Biophys. 299:242-247(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1750-1906 (ISOFORM 3).
RX PubMed=1373815; DOI=10.1128/mcb.12.5.2359-2371.1992;
RA Collinge M., Matrisian P.E., Zimmer W.E., Shattuck R.L., Lukas T.J.,
RA van Eldik L.J., Watterson D.M.;
RT "Structure and expression of a calcium-binding protein gene contained
RT within a calmodulin-regulated protein kinase gene.";
RL Mol. Cell. Biol. 12:2359-2371(1992).
RN [8]
RP PROTEIN SEQUENCE OF 1775-1789, ACETYLATION, DEGLUTAMYLATION,
RP PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=9283094; DOI=10.1021/bi970752e;
RA Rusconi F., Potier M.C., Le Caer J.P., Schmitter J.M., Rossier J.;
RT "Characterization of the chicken telokin heterogeneity by time-of-flight
RT mass spectrometry.";
RL Biochemistry 36:11021-11026(1997).
RN [9]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-1762 AND SER-1768, AND
RP MUTAGENESIS OF SER-1762 AND SER-1768.
RX PubMed=12176732; DOI=10.1152/ajpcell.00501.2001;
RA Komatsu S., Miyazaki K., Tuft R.A., Ikebe M.;
RT "Translocation of telokin by cGMP signaling in smooth muscle cells.";
RL Am. J. Physiol. 283:C752-C761(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1731-1749 IN COMPLEX WITH CALM1
RP AND CALCIUM.
RX PubMed=10194305; DOI=10.1021/bi9821263;
RA Mirzoeva S., Weigand S., Lukas T.J., Shuvalova L., Anderson W.F.,
RA Watterson D.M.;
RT "Analysis of the functional coupling between calmodulin's calcium binding
RT and peptide recognition properties.";
RL Biochemistry 38:3936-3947(1999).
RN [11]
RP ERRATUM OF PUBMED:10194305.
RX PubMed=10529260; DOI=10.1021/bi9950894;
RA Mirzoeva S., Weigand S., Lukas T.J., Shuvalova L., Anderson W.F.,
RA Watterson D.M.;
RL Biochemistry 38:14117-14118(1999).
CC -!- FUNCTION: Phosphorylates a specific serine in the N-terminus of a
CC myosin light chain, which leads to the formation of calmodulin/MLCK
CC signal transduction complexes which allow selective transduction of
CC calcium signals.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-
CC seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-
CC COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC ChEBI:CHEBI:456216; EC=2.7.11.18;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[myosin light chain] = ADP + H(+) + O-
CC phospho-L-threonyl-[myosin light chain]; Xref=Rhea:RHEA:53900,
CC Rhea:RHEA-COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.18;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Tyr-478. Isoforms
CC which lack this tyrosine residue are not regulated in this way. All
CC catalytically active isoforms require binding to calcium and calmodulin
CC for activation.
CC -!- SUBUNIT: All isoforms including Telokin bind calmodulin.
CC {ECO:0000269|PubMed:10194305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12176732}.
CC Membrane {ECO:0000269|PubMed:12176732}. Note=Telokin is cytosolic and
CC can translocate to the membrane upon stimulation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=3;
CC Name=1; Synonyms=MLCK-108, Smooth-muscle;
CC IsoId=P11799-1; Sequence=Displayed;
CC Name=2; Synonyms=MLCK-210, Non-muscle;
CC IsoId=P11799-2; Sequence=VSP_018851;
CC Name=3; Synonyms=Telokin;
CC IsoId=P11799-3; Sequence=VSP_018852;
CC -!- TISSUE SPECIFICITY: Isoform telokin is expressed in gizzard, heart,
CC lung, intestine, and skeletal muscle although the levels of the
CC expression in the latter were much less than that in the gizzard.
CC -!- PTM: The C-terminus is deglutamylated, leading to the formation of
CC Myosin light chain kinase, smooth muscle, deglutamylated form. The C-
CC terminus is variable, with one to five C-terminal glutamyl residues
CC being removed producing five forms differring in their number of C-
CC terminal glutamyl residues. {ECO:0000269|PubMed:9283094}.
CC -!- PTM: Acetylated. {ECO:0000269|PubMed:9283094}.
CC -!- PTM: Phosphorylation of telokin by PKG has no significant effect on its
CC myosin binding activity, but promotes translocation to the membrane.
CC {ECO:0000269|PubMed:12176732, ECO:0000269|PubMed:9283094}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; X52876; CAA37056.1; -; mRNA.
DR EMBL; X52876; CAA37057.1; -; mRNA.
DR EMBL; X52876; CAA37058.1; -; mRNA.
DR EMBL; M31048; AAA49069.1; -; mRNA.
DR EMBL; M14953; AAA69964.1; -; mRNA.
DR EMBL; AF045285; AAC29031.1; -; Genomic_DNA.
DR EMBL; AF045255; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045256; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045257; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045260; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045259; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045258; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045261; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045263; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045265; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045274; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045273; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045272; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045271; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045270; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045269; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045268; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045267; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045266; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045283; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045282; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045281; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045280; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045279; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045278; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045277; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045276; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045275; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045284; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045264; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; AF045262; AAC29031.1; JOINED; Genomic_DNA.
DR EMBL; M96655; AAA49083.1; -; mRNA.
DR EMBL; M88283; AAA48647.1; -; mRNA.
DR EMBL; M88284; AAB53768.1; -; Genomic_DNA.
DR PIR; S68235; S68235.
DR RefSeq; XP_015145280.1; XM_015289794.1.
DR PDB; 1CDL; X-ray; 2.00 A; E/F/G/H=1730-1749.
DR PDB; 1QS7; X-ray; 1.80 A; B/D=1731-1749.
DR PDB; 1QTX; X-ray; 1.65 A; B=1731-1749.
DR PDB; 1VRK; X-ray; 1.90 A; B=1731-1749.
DR PDB; 2O5G; X-ray; 1.08 A; B=1730-1748.
DR PDB; 3EK7; X-ray; 1.85 A; A=1730-1763.
DR PDB; 3EK8; X-ray; 2.80 A; A=1730-1763.
DR PDB; 3EKH; X-ray; 2.00 A; A=1730-1763.
DR PDB; 3EKJ; X-ray; 2.80 A; A=1730-1763.
DR PDB; 3EVR; X-ray; 2.00 A; A=1730-1763.
DR PDB; 3EVU; X-ray; 1.75 A; A=1731-1749.
DR PDB; 3EVV; X-ray; 2.60 A; A=1731-1749.
DR PDB; 3O77; X-ray; 2.35 A; A=1730-1749.
DR PDB; 3O78; X-ray; 2.60 A; A/B=1731-1749.
DR PDB; 4OY4; X-ray; 2.03 A; A=1715-1725, A=1731-1749.
DR PDBsum; 1CDL; -.
DR PDBsum; 1QS7; -.
DR PDBsum; 1QTX; -.
DR PDBsum; 1VRK; -.
DR PDBsum; 2O5G; -.
DR PDBsum; 3EK7; -.
DR PDBsum; 3EK8; -.
DR PDBsum; 3EKH; -.
DR PDBsum; 3EKJ; -.
DR PDBsum; 3EVR; -.
DR PDBsum; 3EVU; -.
DR PDBsum; 3EVV; -.
DR PDBsum; 3O77; -.
DR PDBsum; 3O78; -.
DR PDBsum; 4OY4; -.
DR AlphaFoldDB; P11799; -.
DR BMRB; P11799; -.
DR SMR; P11799; -.
DR BioGRID; 676694; 1.
DR IntAct; P11799; 3.
DR MINT; P11799; -.
DR STRING; 9031.ENSGALP00000061379; -.
DR BindingDB; P11799; -.
DR ChEMBL; CHEMBL3062; -.
DR DrugCentral; P11799; -.
DR iPTMnet; P11799; -.
DR PaxDb; 9031-ENSGALP00000037183; -.
DR VEuPathDB; HostDB:geneid_396445; -.
DR eggNOG; KOG0613; Eukaryota.
DR InParanoid; P11799; -.
DR PhylomeDB; P11799; -.
DR BRENDA; 2.7.11.18; 1306.
DR EvolutionaryTrace; P11799; -.
DR PRO; PR:P11799; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0032154; C:cleavage furrow; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004687; F:myosin light chain kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0014820; P:tonic smooth muscle contraction; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR CDD; cd05762; IgI_8_hMLCK_like; 1.
DR CDD; cd20973; IgI_telokin-like; 1.
DR CDD; cd14191; STKc_MLCK1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015725; MLCK1_kinase_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47633:SF7; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47633; IMMUNOGLOBULIN; 1.
DR Pfam; PF16620; 23ISL; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 9.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 9.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 9.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 9.
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 3D-structure; Acetylation; Alternative promoter usage; ATP-binding;
KW Calcium; Calmodulin-binding; Cytoplasm; Direct protein sequencing;
KW Immunoglobulin domain; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1906
FT /note="Myosin light chain kinase, smooth muscle"
FT /id="PRO_0000024361"
FT CHAIN 1..1901
FT /note="Myosin light chain kinase, smooth muscle,
FT deglutamylated form"
FT /id="PRO_0000424867"
FT DOMAIN 28..117
FT /note="Ig-like C2-type 1"
FT DOMAIN 156..244
FT /note="Ig-like C2-type 2"
FT DOMAIN 429..517
FT /note="Ig-like C2-type 3"
FT DOMAIN 521..613
FT /note="Ig-like C2-type 4"
FT DOMAIN 637..725
FT /note="Ig-like C2-type 5"
FT REPEAT 660..676
FT /note="IIA-1"
FT REPEAT 693..708
FT /note="IIB-1"
FT DOMAIN 735..830
FT /note="Ig-like C2-type 6"
FT REPEAT 758..774
FT /note="IIA-2"
FT REPEAT 791..807
FT /note="IIB-2"
FT REPEAT 970..987
FT /note="III-1"
FT REPEAT 999..1016
FT /note="III-2"
FT REPEAT 1061..1078
FT /note="III-3"
FT DOMAIN 1084..1172
FT /note="Ig-like C2-type 7"
FT REPEAT 1107..1123
FT /note="IIA-3"
FT REPEAT 1140..1156
FT /note="IIB-3"
FT REPEAT 1209..1226
FT /note="III-4"
FT DOMAIN 1225..1313
FT /note="Ig-like C2-type 8"
FT REPEAT 1281..1297
FT /note="IIB-4"
FT DOMAIN 1321..1414
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1453..1708
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1794..1885
FT /note="Ig-like C2-type 9"
FT REPEAT 1817..1833
FT /note="IIA-4"
FT REPEAT 1851..1866
FT /note="IIB-5"
FT REGION 127..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..1833
FT /note="4 X repeats, motif IIA"
FT REGION 693..1866
FT /note="5 X repeats, motif IIB"
FT REGION 831..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1226
FT /note="4 X repeats, motif III"
FT REGION 1180..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1364
FT /note="Motif IA"
FT REGION 1385..1402
FT /note="Motif IB"
FT REGION 1414..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1700..1763
FT /note="Calmodulin-binding"
FT REGION 1716..1728
FT /note="Calmodulin autoinhibition (AM13) region"
FT /evidence="ECO:0000255"
FT REGION 1730..1749
FT /note="Calmodulin recognition (RS20) region"
FT /evidence="ECO:0000255"
FT REGION 1885..1906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1053
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1892..1906
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1574
FT /note="Proton acceptor"
FT BINDING 1459..1467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1762
FT /note="Phosphoserine; by PKG"
FT /evidence="ECO:0000269|PubMed:12176732"
FT MOD_RES 1768
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000305|PubMed:12176732"
FT VAR_SEQ 1..1749
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1373815,
FT ECO:0000303|PubMed:1444462"
FT /id="VSP_018852"
FT VAR_SEQ 1..934
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7589469"
FT /id="VSP_018851"
FT MUTAGEN 1762
FT /note="S->A: Decreases membrane translocation."
FT /evidence="ECO:0000269|PubMed:12176732"
FT MUTAGEN 1768
FT /note="S->A: Decreases membrane translocation."
FT /evidence="ECO:0000269|PubMed:12176732"
FT CONFLICT 1439
FT /note="R -> Q (in Ref. 5; AAA49069/AAA69964)"
FT /evidence="ECO:0000305"
FT CONFLICT 1776
FT /note="E -> D (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 1719..1722
FT /evidence="ECO:0007829|PDB:4OY4"
FT HELIX 1731..1747
FT /evidence="ECO:0007829|PDB:2O5G"
FT STRAND 1753..1758
FT /evidence="ECO:0007829|PDB:3EVU"
FT HELIX 1759..1761
FT /evidence="ECO:0007829|PDB:3EVU"
SQ SEQUENCE 1906 AA; 210446 MW; AD7D8A3B69EE3363 CRC64;
MGDVKLVTST RVSKTSLTLS PSVPAEAPAF TLPPRNIRVQ LGATARFEGK VRGYPEPQIT
WYRNGHPLPE GDHYVVDHSI RGIFSLVIKG VQEGDSGKYT CEAANDGGVR QVTVELTVEG
NSLKKYSLPS SAKTPGGRLS VPPVEHRPSI WGESPPKFAT KPNRVVVREG QTGRFSCKIT
GRPQPQVTWT KGDIHLQQNE RFNMFEKTGI QYLEIQNVQL ADAGIYTCTV VNSAGKASVS
AELTVQGPDK TDTHAQPLCM PPKPTTLATK AIENSDFKQA TSNGIAKELK STSTELMVET
KDRLSAKKET FYTSREAKDG KQGQNQEANA VPLQESRGTK GPQVLQKTSS TITLQAVKAQ
PEPKAEPQTT FIRQAEDRKR TVQPLMTTTT QENPSLTGQV SPRSRETENR AGVRKSVKEE
KREPLGIPPQ FESRPQSLEA SEGQEIKFKS KVSGKPKPDV EWFKEGVPIK TGEGIQIYEE
DGTHCLWLKK ACLGDSGSYS CAAFNPRGQT STSWLLTVKR PKVEEVAPCF SSVLKGCTVS
EGQDFVLQCY VGGVPVPEIT WLLNEQPIQY AHSTFEAGVA KLTVQDALPE DDGIYTCLAE
NNAGRASCSA QVTVKEKKSS KKAEGTQAAK LNKTFAPIFL KGLTDLKVMD GSQVIMTVEV
SANPCPEIIW LHNGKEIQET EDFHFEKKGN EYSLYIQEVF PEDTGKYTCE AWNELGETQT
QATLTVQEPQ DGIQPWFISK PRSVTAAAGQ NVLISCAIAG DPFPTVHWFK DGQEITPGTG
CEILQNEDIF TLILRNVQSR HAGQYEIQLR NQVGECSCQV SLMLRESSAS RAEMLRDGRE
SASSGERRDG GNYGALTFGR TSGFKKSSSE TRAAEEEQED VRGVLKRRVE TREHTEESLR
QQEAEQLDFR DILGKKVSTK SFSEEDLKEI PAEQMDFRAN LQRQVKPKTL SEEERKVHAP
QQVDFRSVLA KKGTPKTPLP EKVPPPKPAV TDFRSVLGAK KKPPAENGSA STPAPNARAG
SEAQNATPNS EAPAPKPVVK KEEKNDRKCE HGCAVVDGGI IGKKAENKPA ASKPTPPPSK
GTAPSFTEKL QDAKVADGEK LVLQCRISSD PPASVSWTLD SKAIKSSKSI VISQEGTLCS
LTIEKVMPED GGEYKCIAEN AAGKAECACK VLVEDTSSTK AAKPAEKKTK KPKTTLPPVL
STESSEATVK KKPAPKTPPK AATPPQITQF PEDRKVRAGE SVELFAKVVG TAPITCTWMK
FRKQIQENEY IKIENAENSS KLTISSTKQE HCGCYTLVVE NKLGSRQAQV NLTVVDKPDP
PAGTPCASDI RSSSLTLSWY GSSYDGGSAV QSYTVEIWNS VDNKWTDLTT CRSTSFNVQD
LQADREYKFR VRAANVYGIS EPSQESEVVK VGEKQEEELK EEEAELSDDE GKETEVNYRT
VTINTEQKVS DVYNIEERLG SGKFGQVFRL VEKKTGKVWA GKFFKAYSAK EKENIRDEIS
IMNCLHHPKL VQCVDAFEEK ANIVMVLEMV SGGELFERII DEDFELTERE CIKYMRQISE
GVEYIHKQGI VHLDLKPENI MCVNKTGTSI KLIDFGLARR LESAGSLKVL FGTPEFVAPE
VINYEPIGYE TDMWSIGVIC YILVSGLSPF MGDNDNETLA NVTSATWDFD DEAFDEISDD
AKDFISNLLK KDMKSRLNCT QCLQHPWLQK DTKNMEAKKL SKDRMKKYMA RRKWQKTGHA
VRAIGRLSSM AMISGMSGRK ASGSSPTSPI NADKVENEDA FLEEVAEEKP HVKPYFTKTI
LDMEVVEGSA ARFDCKIEGY PDPEVMWYKD DQPVKESRHF QIDYDEEGNC SLTISEVCGD
DDAKYTCKAV NSLGEATCTA ELLVETMGKE GEGEGEGEED EEEEEE
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