SVKA_DICDI
ID SVKA_DICDI Reviewed; 478 AA.
AC O61122; Q54LT1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Serine/threonine-protein kinase svkA;
DE EC=2.7.11.1;
DE AltName: Full=Severin kinase A;
GN Name=svkA; ORFNames=DDB_G0286359;
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], PROTEIN SEQUENCE OF 21-26; 319-329; 341-351 AND
RP 386-403, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND AUTOPHOSPHORYLATION.
RC STRAIN=AX2;
RX PubMed=9582328; DOI=10.1074/jbc.273.21.12952;
RA Eichinger L., Baehler M., Dietz M., Eckerskorn C., Schleicher M.;
RT "Characterization and cloning of a Dictyostelium Ste20-like protein kinase
RT that phosphorylates the actin-binding protein severin.";
RL J. Biol. Chem. 273:12952-12959(1998).
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 FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18042625; DOI=10.1242/jcs.012179;
RA Rohlfs M., Arasada R., Batsios P., Janzen J., Schleicher M.;
RT "The Ste20-like kinase SvkA of Dictyostelium discoideum is essential for
RT late stages of cytokinesis.";
RL J. Cell Sci. 120:4345-4354(2007).
CC -!- FUNCTION: Involved in regulation of actin cytoskeleton organization
CC during cell motility; F-actin fragmenting and capping protein allowing
CC dynamic rearrangements of the actin cytoskeleton. Also part of a
CC regulatory pathway from the centrosome to the midzone, thus regulating
CC the completion of cell division. {ECO:0000269|PubMed:18042625,
CC ECO:0000269|PubMed:9582328}.
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;
CC Evidence={ECO:0000269|PubMed:9582328};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9582328};
CC -!- ACTIVITY REGULATION: Phosphorylation of severin is reduced with high
CC concentrations of calcium ions. {ECO:0000269|PubMed:9582328}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:9582328};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18042625}.
CC Nucleus {ECO:0000269|PubMed:18042625}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:18042625}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:18042625}. Cleavage furrow
CC {ECO:0000269|PubMed:18042625}. Note=Shows overall localization in the
CC cytosol and, to a lesser extent, in the nucleus. Enriched around the
CC centrosome. In dividing cells, forms a cloud around the spindle and
CC nuclei. Enriched in the cleavage furrow during late cytokinesis.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: Defects in cytokinesis, leading to multinucleated
CC cells caused by failure to sever the final connecting bridge between
CC the 2 daughter cells. Cells also display defects in development and
CC directed slug movement. {ECO:0000269|PubMed:18042625}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AF059534; AAC24522.1; -; mRNA.
DR EMBL; AAFI02000085; EAL64204.1; -; Genomic_DNA.
DR RefSeq; XP_637749.1; XM_632657.1.
DR AlphaFoldDB; O61122; -.
DR SMR; O61122; -.
DR BioGRID; 1250618; 1.
DR STRING; 44689.DDB0191176; -.
DR PaxDb; O61122; -.
DR EnsemblProtists; EAL64204; EAL64204; DDB_G0286359.
DR GeneID; 8625615; -.
DR KEGG; ddi:DDB_G0286359; -.
DR dictyBase; DDB_G0286359; svkA.
DR eggNOG; KOG0201; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; O61122; -.
DR OMA; KEFCALC; -.
DR PhylomeDB; O61122; -.
DR Reactome; R-DDI-75153; Apoptotic execution phase.
DR PRO; PR:O61122; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:dictyBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0035329; P:hippo signaling; IDA:dictyBase.
DR GO; GO:0006972; P:hyperosmotic response; IEP:dictyBase.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:UniProtKB.
DR GO; GO:1903438; P:positive regulation of mitotic cytokinetic process; IMP:dictyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
DR Gene3D; 1.10.12.70; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR046409; PDC10_dimerisation_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Kinase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..478
FT /note="Serine/threonine-protein kinase svkA"
FT /id="PRO_0000327907"
FT DOMAIN 12..262
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 306..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 478 AA; 52616 MW; B4935BE0812CDC32 CRC64;
MASKKGDPEE LYVRQEKIGK GSFGEVFKGI NKKTNETIAI KTIDLEDAED EIEDIQQEIN
VLSQCESPFV TKYFGSFLKG SKLWIIMEYL AGGSVLDLMK PGPFDEGYIA IILRELLKGL
EYLHSEGKIH RDIKAANVLL SASGDVKLAD FGVSGQLTDQ MTKRNTFVGT PFWMAPEVIK
QTGYDSKADI WSMGITALEM AKGEPPRADL HPMRALFLIP KDPPPTLEGN FSKGFKEFCA
LCLNKDPNQR PTAKDLLKHK FIKAAKKTSS LTDLIERRQK WLQLNGNNAD DENDDLDRDA
KSNEEDFGWE FPTIKQKSPV AVQEQQQTPQ KPTVVSTPIK EQQQQQQPTP VTTPQQPVTT
TTTTPTTETK VRSLSNSSQT TPVKTTVAAT TAPATTPASN APTSTTPNGA AVTQQQAPRA
SALTSVIYPV LSKLLKNTSD ENVINALAQL KMAFDNAEKA KPGITHSLIA QIIETLKR
