VRK1_CAEEL
ID VRK1_CAEEL Reviewed; 610 AA.
AC Q19848;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Serine/threonine-protein kinase VRK1 {ECO:0000303|PubMed:17170708};
DE EC=2.7.11.1;
DE AltName: Full=Vaccinia-related kinase 1 {ECO:0000303|PubMed:17170708};
GN Name=vrk-1 {ECO:0000312|WormBase:F28B12.3}; ORFNames=F28B12.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17170708; DOI=10.1038/sj.emboj.7601470;
RA Gorjanacz M., Klerkx E.P., Galy V., Santarella R., Lopez-Iglesias C.,
RA Askjaer P., Mattaj I.W.;
RT "Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in
RT post-mitotic nuclear envelope assembly.";
RL EMBO J. 26:132-143(2007).
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000305};
RX PubMed=19679119; DOI=10.1016/j.ydbio.2009.08.007;
RA Klerkx E.P., Alarcon P., Waters K., Reinke V., Sternberg P.W., Askjaer P.;
RT "Protein kinase VRK-1 regulates cell invasion and EGL-17/FGF signaling in
RT Caenorhabditis elegans.";
RL Dev. Biol. 335:12-21(2009).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000305};
RX PubMed=20599896; DOI=10.1016/j.ydbio.2010.06.022;
RA Waters K., Yang A.Z., Reinke V.;
RT "Genome-wide analysis of germ cell proliferation in C.elegans identifies
RT VRK-1 as a key regulator of CEP-1/p53.";
RL Dev. Biol. 344:1011-1025(2010).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF PRO-69.
RX PubMed=22770216; DOI=10.1016/j.cell.2012.04.043;
RA Asencio C., Davidson I.F., Santarella-Mellwig R., Ly-Hartig T.B., Mall M.,
RA Wallenfang M.R., Mattaj I.W., Gorjanacz M.;
RT "Coordination of kinase and phosphatase activities by Lem4 enables nuclear
RT envelope reassembly during mitosis.";
RL Cell 150:122-135(2012).
CC -!- FUNCTION: Serine/threonine kinase that phosphorylates baf-1, thus
CC regulating the association of baf-1 with chromatin and nuclear membrane
CC proteins during nuclear envelope formation. May act through the egl-17
CC signaling pathway. Essential in hermaphrodites for formation of the
CC vulva, uterus, and uterine seam cells and for development and
CC maintenance of the somatic gonad and thus the germ line. Acts to
CC prevent cep-1 from triggering an inappropriate cell cycle arrest,
CC thereby promoting germ cell proliferation. Regulates anchor cell
CC polarity and the timing of anchor cell invasion through the basement
CC membranes separating vulval and somatic gonadal cells during the L3
CC larval stage. {ECO:0000269|PubMed:17170708,
CC ECO:0000269|PubMed:19679119, ECO:0000269|PubMed:20599896,
CC ECO:0000269|PubMed:22770216}.
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 Evidence={ECO:0000269|PubMed:17170708};
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; Evidence={ECO:0000269|PubMed:17170708};
CC -!- INTERACTION:
CC Q19848; Q03565: baf-1; NbExp=3; IntAct=EBI-2414048, EBI-2535603;
CC Q19848; H2KZB2: lem-4; NbExp=2; IntAct=EBI-2414048, EBI-6258914;
CC Q19848; Q86XL3: ANKLE2; Xeno; NbExp=2; IntAct=EBI-2414048, EBI-1773621;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17170708,
CC ECO:0000269|PubMed:20599896}. Note=Nuclear during interphase,
CC accumulates at the nuclear rim in prophase and localizes to chromatin
CC throughout metaphase, anaphase and telophase.
CC {ECO:0000269|PubMed:17170708, ECO:0000269|PubMed:20599896}.
CC -!- TISSUE SPECIFICITY: Present in germ cells at all stages of progression
CC from the mitotic zone to mature oocytes, but not in maturing spermatids
CC (at the protein level). Expressed in the ventral nerve cord and vulva
CC cells. {ECO:0000269|PubMed:19679119, ECO:0000269|PubMed:20599896}.
CC -!- PTM: Autophosphorylates in vitro. {ECO:0000269|PubMed:17170708}.
CC -!- DISRUPTION PHENOTYPE: Embryonically lethal. Homozygous animals produced
CC by heterozygous hermaphrodites overcome this through maternal
CC contribution. In these animals, defects in the formation of the vulva,
CC uterus, and uterine seam cells and in development and maintenance of
CC the somatic gonad and thus the germ line appear in the early L3 larval
CC stage. Adults are sterile. Cells display mitotic defects, including
CC impaired nuclear envelope formation and baf-1 delocalization.
CC {ECO:0000269|PubMed:17170708, ECO:0000269|PubMed:19679119,
CC ECO:0000269|PubMed:20599896}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. VRK subfamily. {ECO:0000255}.
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DR EMBL; FO080105; CCD61237.1; -; Genomic_DNA.
DR PIR; T16194; T16194.
DR RefSeq; NP_495185.1; NM_062784.4.
DR AlphaFoldDB; Q19848; -.
DR SMR; Q19848; -.
DR BioGRID; 39345; 5.
DR IntAct; Q19848; 4.
DR STRING; 6239.F28B12.3.1; -.
DR EPD; Q19848; -.
DR PaxDb; Q19848; -.
DR PeptideAtlas; Q19848; -.
DR PRIDE; Q19848; -.
DR EnsemblMetazoa; F28B12.3.1; F28B12.3.1; WBGene00017895.
DR EnsemblMetazoa; F28B12.3.2; F28B12.3.2; WBGene00017895.
DR GeneID; 174004; -.
DR KEGG; cel:CELE_F28B12.3; -.
DR UCSC; F28B12.3.1; c. elegans.
DR CTD; 174004; -.
DR WormBase; F28B12.3; CE02704; WBGene00017895; vrk-1.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000168643; -.
DR HOGENOM; CLU_019279_4_0_1; -.
DR InParanoid; Q19848; -.
DR OMA; PDYDKCR; -.
DR OrthoDB; 834667at2759; -.
DR PhylomeDB; Q19848; -.
DR Reactome; R-CEL-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-CEL-9013405; RHOD GTPase cycle.
DR SignaLink; Q19848; -.
DR PRO; PR:Q19848; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017895; Expressed in adult organism and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IMP:WormBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:WormBase.
DR GO; GO:0008406; P:gonad development; IMP:WormBase.
DR GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..610
FT /note="Serine/threonine-protein kinase VRK1"
FT /id="PRO_0000405308"
FT DOMAIN 32..384
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 317..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 38..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 69
FT /note="P->L: Acts as a suppressor of lem-4l(ax475) mutant."
FT /evidence="ECO:0000269|PubMed:22770216"
SQ SEQUENCE 610 AA; 67355 MW; 9C23F0BCBA948FB6 CRC64;
MPPKKAPAKK LHELAAEVRV GHKINDISKK TFIVGKQFAT GGFGRIHTCT EEGKSQQMVM
KIEPSTNGPL LTEVVVFNRI LKKELIESYK KKKKISWIGL PYLIANGYFT YESEKMRYMI
IPKYATSLEA VRETNGGTLA MKDSLTVASC ILDALEYLHE SDYAHADVKA ANILLEKQGV
YSTAVLVDFG LAHRTTNNVD KPDKKRAHNG TCIFTSTDAH RGNNPSFRGD IEILAYNLMM
WATGTLPWMA LESSPEKVFD AKQKFIAGLP GTLQNVLKNE SSAVVGCIAS MFDISMKTNY
TDKVDMGKLK KLVTDAIQKT SSDGKKTPTR QKKLAEEDKN AVTPKRSTRR LAVKEESDNK
DNDEVEVKPE KKATPRKRTT RKAVEVNNDS DDNEEQYENP KSKSSRTQTK SKRAKEEDVD
DEEEIIIPKS SRSRSKVQLS GEGSDVTTPS SAASTSRSRS IRLGLTSSTA SSNKVAKKIE
QKYKRLSMNK SSLVPVTISV ASDKSPTTST PSSSSGLRSK RKSSEDVGEG ITLKTQVLIT
PAIKKAKTKS GISSATKASP TELRRVPGVR NFPKGRRSMI IKETSAKYKE RLASRQTKPT
FDDSSCSSEV
