MHCKC_DICDI
ID MHCKC_DICDI Reviewed; 780 AA.
AC Q8MY12; O76739; Q54FQ7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Myosin heavy chain kinase C;
DE Short=MHCK-C;
DE EC=2.7.11.7 {ECO:0000305|PubMed:11278493, ECO:0000305|PubMed:12475956};
GN Name=mhkC; Synonyms=mhckC; ORFNames=DDB_G0290687;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL
RP STAGE, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=12475956; DOI=10.1091/mbc.e02-04-0228;
RA Nagasaki A., Itoh G., Yumura S., Uyeda T.P.Q.;
RT "Novel myosin heavy chain kinase involved in disassembly of myosin II
RT filaments and efficient cleavage in mitotic dictyostelium cells.";
RL Mol. Biol. Cell 13:4333-4342(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-751.
RC STRAIN=AX4;
RA Iranfar N., Loomis W.F.;
RT "Dictyostelium discoideum developmental gene mhkC.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11278493; DOI=10.1074/jbc.m009366200;
RA Luo X., Crawley S.W., Steimle P.A., Egelhoff T.T., Cote G.P.;
RT "Specific phosphorylation of threonine by the Dictyostelium myosin II heavy
RT chain kinase family.";
RL J. Biol. Chem. 276:17836-17843(2001).
RN [5]
RP FUNCTION, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP MHCA.
RX PubMed=12139770; DOI=10.1186/1471-2121-3-19;
RA Liang W., Licate L.S., Warrick H.M., Spudich J.A., Egelhoff T.T.;
RT "Differential localization in cells of myosin II heavy chain kinases during
RT cytokinesis and polarized migration.";
RL BMC Cell Biol. 3:19-19(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15987738; DOI=10.1091/mbc.e05-03-0219;
RA Yumura S., Yoshida M., Betapudi V., Licate L.S., Iwadate Y., Nagasaki A.,
RA Uyeda T.Q.P., Egelhoff T.T.;
RT "Multiple myosin II heavy chain kinases: roles in filament assembly control
RT and proper cytokinesis in Dictyostelium.";
RL Mol. Biol. Cell 16:4256-4266(2005).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=17371831; DOI=10.1083/jcb.200607072;
RA Jeon T.J., Lee D.-J., Merlot S., Weeks G., Firtel R.A.;
RT "Rap1 controls cell adhesion and cell motility through the regulation of
RT myosin II.";
RL J. Cell Biol. 176:1021-1033(2007).
RN [8]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA Skelton J., Ivens A., Bozzaro S.;
RT "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT bacteria in Dictyostelium.";
RL BMC Genomics 9:291-291(2008).
CC -!- FUNCTION: Phosphorylates threonine at 'Thr-1823', 'Thr-1833' and 'Thr-
CC 2029' in the C-terminal tail region of myosin II heavy chain (mhcA) (By
CC similarity). This phosphorylation is critical in actin-activated ATPase
CC activity of the myosin and regulating the assembly and disassembly of
CC myosin II filament. In vitro, catalytic domain phosphorylates mhcA,
CC myelin basic protein, myosin regulatory light chain, casein and
CC caldesmon. Drives the disassembly of myosin II filaments for efficient
CC cytokinesis and recycling of myosin II that occurs during late
CC cytokinesis. Can be activated in vitro by autophosphorylation.
CC {ECO:0000250, ECO:0000269|PubMed:11278493, ECO:0000269|PubMed:12139770,
CC ECO:0000269|PubMed:12475956, ECO:0000269|PubMed:15987738}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[myosin heavy-chain] = ADP + H(+) + O-
CC phospho-L-threonyl-[myosin heavy-chain]; Xref=Rhea:RHEA:11424,
CC Rhea:RHEA-COMP:13718, Rhea:RHEA-COMP:13719, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.7;
CC Evidence={ECO:0000305|PubMed:11278493, ECO:0000305|PubMed:12475956};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11425;
CC Evidence={ECO:0000305|PubMed:11278493, ECO:0000305|PubMed:12475956};
CC -!- SUBUNIT: Interacts with myosin II heavy chain (mhcA).
CC {ECO:0000269|PubMed:12139770}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Membrane. Cleavage
CC furrow. Note=Localizes to the cortex of interphase cells, cleavage
CC furrow of mitotic cells (at the late stage of cytokinesis), and
CC posterior side of both migrating cells and daughter cells beginning to
CC separate at the very late stage of cytokinesis. Localization is myosin
CC II-dependent. Occasionally displays transient enrichment in
CC pseudopodial extensions as well. {ECO:0000269|PubMed:12475956}.
CC -!- DEVELOPMENTAL STAGE: Expressed continuously throughout development.
CC {ECO:0000269|PubMed:12475956}.
CC -!- INDUCTION: Down-regulated by growth on bacteria.
CC {ECO:0000269|PubMed:18559084}.
CC -!- PTM: Autophosphorylated in vitro.
CC -!- DISRUPTION PHENOTYPE: Null cells exhibit excessive aggregation of
CC myosin II filaments in the cleavage furrows and in the posteriors of
CC the daughter cells once cleavage is complete. The cleavage process is
CC slowed down for cells where the gene is disrupted. Myosin II
CC overassembly increases incrementally in the mutants, with the mhkA,
CC mhkB, mhkC triple mutant showing severe myosin II overassembly and
CC myosin II phosphorylation is highly reduced. Overexpression results in
CC multinucleation of cells. {ECO:0000269|PubMed:12475956,
CC ECO:0000269|PubMed:15987738, ECO:0000269|PubMed:17371831}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000305}.
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DR EMBL; AB079663; BAC07316.1; -; mRNA.
DR EMBL; AAFI02000166; EAL62094.1; -; Genomic_DNA.
DR EMBL; AF079447; AAC31918.1; -; Genomic_DNA.
DR RefSeq; XP_635600.1; XM_630508.1.
DR AlphaFoldDB; Q8MY12; -.
DR SMR; Q8MY12; -.
DR STRING; 44689.DDB0216199; -.
DR PaxDb; Q8MY12; -.
DR EnsemblProtists; EAL62094; EAL62094; DDB_G0290687.
DR GeneID; 8627781; -.
DR KEGG; ddi:DDB_G0290687; -.
DR dictyBase; DDB_G0290687; mhkC.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_378764_0_0_1; -.
DR InParanoid; Q8MY12; -.
DR OMA; CERAIKW; -.
DR PhylomeDB; Q8MY12; -.
DR BRENDA; 2.7.11.7; 1939.
DR PRO; PR:Q8MY12; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:dictyBase.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0016905; F:myosin heavy chain kinase activity; IMP:dictyBase.
DR GO; GO:0045159; F:myosin II binding; ISS:dictyBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0031037; P:myosin II filament disassembly; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR GO; GO:1903013; P:response to differentiation-inducing factor 1; HDA:dictyBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR004166; MHCK_EF2_kinase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00811; Alpha_kinase; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; WD repeat.
FT CHAIN 1..780
FT /note="Myosin heavy chain kinase C"
FT /id="PRO_0000361271"
FT DOMAIN 40..243
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REPEAT 507..546
FT /note="WD 1"
FT REPEAT 549..589
FT /note="WD 2"
FT REPEAT 591..628
FT /note="WD 3"
FT REPEAT 631..668
FT /note="WD 4"
FT REPEAT 671..708
FT /note="WD 5"
FT REPEAT 748..780
FT /note="WD 6"
FT REGION 310..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 86180 MW; 65EBFF0FE027CF31 CRC64;
MEEKKTGAAA ALALLNQKFP VADVIAGTKC ERAIKWELTI GDDLKPKWTH SIVCVSIEKT
PFAKGSCRTA HKLKDWSQPD QGLVGKFSTN KKTTRDSYFT DVLMQTFCAK WAEKFNEAKP
PKPITFLPSY VYELIDHPPP YPVCGGEPFI EGDYKKHNNN SGYVSSDARN TPQSFSHFSY
ELSNHELLIV DIQGVNDFYT DPQIHTKSGE GFGEGNLGET GFHKFLQTHK CNPVCDFLKL
KPINQSKKAL LRGTLPVVQL MDFHDAIGLN GNGSGPKNNY DMNYFRNGGG AQQPISLDDE
EKMLQEQLER IRAQQQQKSK PSPPLVKQPS GNNLHKQQSP SSPTSKPVPQ IVKTPSQSNV
VNKSPVSPPK ENSNVKLEQD NINNNNSSIS SNNDNSNNNN NNNDNINNSS NSSSVNSNSS
SVSSSSSSSS SSSSSSTTNA APISIQVSRN SPPPQQPIQP SSAAASASST SSSNVPTPES
TSTSSMEQTP DRSEFEKWDL TSIKNIDTVR GLQSECITGD SLRLYSGSND GQIGVWDAVE
LKHVTNIKAH GKSIRAVIKR PGFDQNILTA GADSLVKEWD INTQQTIKEI KESNEVNTIF
IQDNLLYTGC NDKTVKVWDM RSYECVKTLS GHTRAIKSVC AMGNLLFSGS NDQQIYVWNL
ATGTILTNFQ GHEGWVKTLY AHNNMLYSGS HDETIRIWDL KTTRCVNTIK CKDRVETLHV
TNQGIFAGSG DWLQVFSHDK YENLASLNTR SSILCLWRNQ NQLFTGSLAS NLKVWSWDKM
