VWKA_DICDI
ID VWKA_DICDI Reviewed; 625 AA.
AC Q6B9X6; Q55FF0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Alpha-protein kinase vwkA;
DE EC=2.7.11.1;
DE AltName: Full=von Willebrand factor A alpha-kinase;
DE Short=vWF kinase;
GN Name=vwkA; ORFNames=DDB_G0268144;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, INTERACTION WITH
RP CALMODULIN, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, DEVELOPMENTAL STAGE,
RP AND FUNCTION.
RC STRAIN=AX2;
RX PubMed=15728726; DOI=10.1091/mbc.e04-07-0639;
RA Betapudi V., Mason C., Licate L., Egelhoff T.T.;
RT "Identification and characterization of a novel alpha-kinase with a von
RT Willebrand factor A-like motif localized to the contractile vacuole and
RT Golgi complex in Dictyostelium discoideum.";
RL Mol. Biol. Cell 16:2248-2262(2005).
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, AND CHARACTERIZATION.
RX PubMed=18381083; DOI=10.1016/j.bbapap.2008.03.001;
RA Crawley S.W., Cote G.P.;
RT "Determinants for substrate phosphorylation by Dictyostelium myosin II
RT heavy chain kinases A and B and eukaryotic elongation factor-2 kinase.";
RL Biochim. Biophys. Acta 1784:908-915(2008).
RN [4]
RP INTERACTION WITH CALMODULIN.
RX PubMed=17897809; DOI=10.1016/j.cellsig.2007.08.017;
RA Catalano A., O'Day D.H.;
RT "Calmodulin-binding proteins in the model organism Dictyostelium: a
RT complete & critical review.";
RL Cell. Signal. 20:277-291(2008).
CC -!- FUNCTION: Displays a modest preference for threonine over serine
CC residues. Does not phosphorylate myosin II, however can phosphorylate
CC MBP, in vitro. May be involved in the regulation of myosin II function
CC during cytokinesis. Overexpression leads to impaired cell proliferation
CC in suspension culture and fails to develop beyond the mound stage. Both
CC overexpression and absence of the gene can result in defects in
CC cytokinesis and alterations in myosin II abundance and assembly.
CC {ECO:0000269|PubMed:15728726, ECO:0000269|PubMed:18381083}.
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 -!- ACTIVITY REGULATION: Autophosphorylation activity enhanced by
CC calcium/calmodulin.
CC -!- SUBUNIT: Interacts with calmodulin; in the presence of calcium.
CC {ECO:0000269|PubMed:15728726, ECO:0000269|PubMed:17897809}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15728726}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:15728726}.
CC Contractile vacuole membrane {ECO:0000269|PubMed:15728726}.
CC Note=Enriched adjacent to large spherical structures such as
CC contractile vacuoles and Golgi-like structures (perinuclear).
CC -!- DEVELOPMENTAL STAGE: Expressed continuously throughout development. Low
CC expression (at protein level). {ECO:0000269|PubMed:15728726}.
CC -!- PTM: Autophosphorylated, in vitro.
CC -!- DISRUPTION PHENOTYPE: Impaired development, multinucleation, fruiting
CC body formation that is delayed by 36-48 hours during the development in
CC addition to stalks and spores that are thin and smaller.
CC {ECO:0000269|PubMed:15728726}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000305}.
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DR EMBL; AY672633; AAT76981.1; -; Genomic_DNA.
DR EMBL; AAFI02000003; EAL73525.1; -; Genomic_DNA.
DR RefSeq; XP_647583.1; XM_642491.1.
DR AlphaFoldDB; Q6B9X6; -.
DR SMR; Q6B9X6; -.
DR STRING; 44689.DDB0216405; -.
DR PaxDb; Q6B9X6; -.
DR EnsemblProtists; EAL73525; EAL73525; DDB_G0268144.
DR GeneID; 8616395; -.
DR KEGG; ddi:DDB_G0268144; -.
DR dictyBase; DDB_G0268144; vwkA.
DR eggNOG; ENOG502QVA3; Eukaryota.
DR HOGENOM; CLU_026740_0_0_1; -.
DR InParanoid; Q6B9X6; -.
DR OMA; NPYVVKS; -.
DR PhylomeDB; Q6B9X6; -.
DR PRO; PR:Q6B9X6; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0031164; C:contractile vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0005516; F:calmodulin binding; IDA:dictyBase.
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; IDA:dictyBase.
DR GO; GO:0070177; P:contractile vacuole discharge; IMP:dictyBase.
DR GO; GO:0033298; P:contractile vacuole organization; IMP:dictyBase.
DR GO; GO:0006971; P:hypotonic response; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0031038; P:myosin II filament organization; IMP:dictyBase.
DR GO; GO:0018209; P:peptidyl-serine modification; IDA:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR004166; MHCK_EF2_kinase.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF02816; Alpha_kinase; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Vacuole.
FT CHAIN 1..625
FT /note="Alpha-protein kinase vwkA"
FT /id="PRO_0000363923"
FT DOMAIN 122..322
FT /note="VWFA"
FT DOMAIN 386..600
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..114
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 570..576
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 625 AA; 70158 MW; 4A2DE8CC64119F36 CRC64;
MESKYVLSTE KESKTKPSGR VNVSDMDSIS NSLSKTSLGT RKVPTSLKTD ASRSGLSSGG
SKTHISDESA LRMVYGSTPR DEKTTTTKDS ITLAKEKEKK IEKRNEEIKL TFKAIRASEC
VDLLFIVDCT GSMDPYIEQI KSDIVKLQEA LKLKHSFLDI EFGFIRYTDF DVASNRCSTF
QFSRSTVEFV RFVSEIRAGG GADGPEDVFG GMDLIKSMKW RPNSTRVVIH IADAPCHGTE
YHSMADSYPG GDPNGIKLDD LLTDIISLNI NYYFGHINLK ETGQMIDFFD KKTKEISRNK
KSINSFDSKE TSKMNERIFI SIEESISVSR SVLTEQYLGH NIDGSTGKQR SEREFEINTN
MDIDFGELPY IQMLQTKFKM PSDIVTCLSS SYEMKLNEIT ISIKIAPNPF SHGACRLAYL
GIDEHGKKVV LKQSKYIGGR ENSKKRYFES MECQTVAAKF ALEFNKQLSL TSSEHQITFT
VAKVLQMKHS EKPMYFGIET FINGEYQKYN SNCGWLKDDA MSEILQTFSH WTYQESKNKA
IVVDIQGVKT SKGYLLTDPA IHSTDTLRFG SCNLGKPGII KFFQSHKCNQ HCKKLGLTIP
SFTSSSSTSS SSRSTSSSSS ISYSY
