CD112_CAEEL
ID CD112_CAEEL Reviewed; 668 AA.
AC Q23357;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Cyclin-dependent kinase 11.2 {ECO:0000305};
DE EC=2.7.11.22 {ECO:0000250|UniProtKB:P24941};
GN Name=cdk-11.2 {ECO:0000303|PubMed:29886128, ECO:0000312|WormBase:ZC504.3};
GN ORFNames=ZC504.3 {ECO:0000312|WormBase:ZC504.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=29886128; DOI=10.1016/j.ydbio.2018.06.006;
RA Williams C.W., Iyer J., Liu Y., O'Connell K.F.;
RT "CDK-11-Cyclin L is required for gametogenesis and fertility in C.
RT elegans.";
RL Dev. Biol. 441:52-66(2018).
CC -!- FUNCTION: Probable cyclin-dependent kinase whose activity is most
CC likely regulated by the cyclin cyl-1/Cylin-L (PubMed:29886128). Acts
CC partially redundantly with cdk-11.1 to ensure embryonic viability
CC (PubMed:29886128). In contrast to cdk-11.1, not essential for male and
CC female fertility (PubMed:29886128). {ECO:0000269|PubMed:29886128}.
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=2.7.11.22;
CC Evidence={ECO:0000250|UniProtKB:P24941};
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=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P24941};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29886128}. Cytoplasm
CC {ECO:0000269|PubMed:29886128}. Note=Evenly distributed between the
CC cytoplasm and nucleus in embryos, but becomes more enriched in the
CC nucleus from the 4- and 6-cell stage as embryos develop
CC (PubMed:29886128). In the germline, localizes to the nucleus and
CC cytoplasm in the mitotic region, but is enriched in the cytoplasm
CC (PubMed:29886128). Nuclear localization increases as cells enter late
CC pachytene, and then the distribution between the cytoplasm and nucleus
CC becomes more even as oocytes mature (PubMed:29886128).
CC {ECO:0000269|PubMed:29886128}.
CC -!- TISSUE SPECIFICITY: Expressed in somatic cells and at varying levels
CC throughout the germline (at protein level) (PubMed:29886128). Highly
CC expressed in the germ line of hermaphrodites (at protein level)
CC (PubMed:29886128). {ECO:0000269|PubMed:29886128}.
CC -!- DEVELOPMENTAL STAGE: Expression in embryos increases as development
CC proceeds (at protein level). {ECO:0000269|PubMed:29886128}.
CC -!- DISRUPTION PHENOTYPE: Viable, with no visible phenotype
CC (PubMed:29886128). Knockout combined with RNAi-mediated knockdown of
CC cdk-11.1 at the L1 stage of larval development results in sterility
CC (PubMed:29886128). Knockout combined with RNAi-mediated knockdown of
CC cdk-11.1 at the L4 larval stage results in fertile adults that produce
CC few viable embryos (PubMed:29886128). {ECO:0000269|PubMed:29886128}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; BX284606; CAA90342.2; -; Genomic_DNA.
DR PIR; T27620; T27620.
DR RefSeq; NP_509746.2; NM_077345.4.
DR AlphaFoldDB; Q23357; -.
DR SMR; Q23357; -.
DR STRING; 6239.ZC504.3; -.
DR EPD; Q23357; -.
DR PaxDb; Q23357; -.
DR PeptideAtlas; Q23357; -.
DR EnsemblMetazoa; ZC504.3.1; ZC504.3.1; WBGene00013917.
DR GeneID; 181247; -.
DR KEGG; cel:CELE_ZC504.3; -.
DR UCSC; ZC504.3; c. elegans.
DR CTD; 181247; -.
DR WormBase; ZC504.3; CE40176; WBGene00013917; cdk-11.2.
DR eggNOG; KOG0663; Eukaryota.
DR GeneTree; ENSGT00970000196694; -.
DR HOGENOM; CLU_000288_91_3_1; -.
DR InParanoid; Q23357; -.
DR OMA; HERTKMN; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; Q23357; -.
DR PRO; PR:Q23357; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00013917; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; 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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..668
FT /note="Cyclin-dependent kinase 11.2"
FT /id="PRO_0000447606"
FT DOMAIN 304..600
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 432
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 310..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 668 AA; 77936 MW; 3DA7FD8E854FFAED CRC64;
MSNYSTNGSR KIRISNSDDD SRETRFSIQP RNSHKTKEER YRDKEKERDH ERHHDRERRD
DRYRKVDSRD HRDRNRRSPA GSRTYCRDEP DRRRNNHSDR NRRDRSSERD RDNRSSKSKT
KSPDSLRSKS SRKSQTPNHL PDDGKLFDRI LDPNYKKKEK TVMEVEDVEM SPVEMLDEEE
VSTFTFDDAC GPVRPSNEPE EKDYKSEGDP ESRPATPKTP LTPDYLENTI VSLNETLSDD
EDKGPDDKYG KTPDKEQWES MTENEQKLHR DAMKKRREQR HREAVSKLPV YYPGLRGCQH
ISEYVILNVI AEGTYGEVFR GKNTRTDEVV ALKRFKMEKE KEGFPITALR EINMLLKAGA
HENIVNVKEI LVGSTKTEVY MAMEYVEHDV KSLIDKMRSR NQRFKTGQQK TLMSQLLSGI
EHMHKLWILH RDLKTSNLLI SHSGILKIAD FGLAREYGEA RDIEKRMKLT PIVVTLWYRS
PELLLEPKTY STPVDMWSIG CIMAEFIMMK PMFQGDSEPN QVHQIFQMMG TPTEQIWPDI
KELKVWNMVE FPPVKPGQLR RIFKGEKLVN ETGFDLLNGM LCLNPANRLT ASEALQHDWF
SEHPKAVPPE DLPVYPAKSE LNAAPPENRR KNRLEALLAD EEPERAALLR QFNVKAEQLK
PSGFQLRG
