CD111_CAEEL
ID CD111_CAEEL Reviewed; 719 AA.
AC Q09437; A0A2K5ATR0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cyclin-dependent kinase 11.1 {ECO:0000312|WormBase:B0495.2a};
DE EC=2.7.11.22 {ECO:0000250|UniProtKB:P24941};
GN Name=cdk-11.1 {ECO:0000303|PubMed:29886128, ECO:0000312|WormBase:B0495.2a};
GN ORFNames=B0495.2 {ECO:0000312|WormBase:B0495.2a};
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]
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).
CC Important for normal oocyte and sperm development; probably required
CC during multiple stages of gametogenesis (PubMed:29886128). Plays a role
CC in the activation of RAS-ERK signaling in the germ line
CC (PubMed:29886128). Also acts partially redundantly with cdk-11.2 to
CC ensure embryonic viability (PubMed:29886128).
CC {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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:B0495.2a};
CC IsoId=Q09437-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:B0495.2b};
CC IsoId=Q09437-2; Sequence=VSP_060204;
CC -!- TISSUE SPECIFICITY: Broadly expressed in somatic and germ line cells
CC (at protein level) (PubMed:29886128). Not expressed in sperm (at
CC protein level) (PubMed:29886128). {ECO:0000269|PubMed:29886128}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed during all stages of
CC embryogenesis, but expression is low during the first few cell cycles
CC (at protein level). {ECO:0000269|PubMed:29886128}.
CC -!- DISRUPTION PHENOTYPE: Viable, but exhibit low fecundity and have a
CC reduced brood size (PubMed:29886128). RNAi-mediated knockdown results
CC in fertile adults that produce viable progeny (PubMed:29886128). RNAi-
CC mediated knockdown in L1 stage cdk-11.2 bs101 mutants results in
CC sterility (PubMed:29886128). RNAi-mediated knockdown in L4 stage cdk-
CC 11.2 bs101 mutants results in fertile adults that produce few viable
CC 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; BX284602; CCD61471.1; -; Genomic_DNA.
DR EMBL; BX284602; SPC47283.1; -; Genomic_DNA.
DR PIR; C88216; C88216.
DR RefSeq; NP_495617.1; NM_063216.5. [Q09437-1]
DR AlphaFoldDB; Q09437; -.
DR SMR; Q09437; -.
DR BioGRID; 39578; 4.
DR IntAct; Q09437; 1.
DR STRING; 6239.B0495.2; -.
DR iPTMnet; Q09437; -.
DR EPD; Q09437; -.
DR PaxDb; Q09437; -.
DR PeptideAtlas; Q09437; -.
DR EnsemblMetazoa; B0495.2a.1; B0495.2a.1; WBGene00015203. [Q09437-1]
DR EnsemblMetazoa; B0495.2b.1; B0495.2b.1; WBGene00015203. [Q09437-2]
DR GeneID; 174244; -.
DR KEGG; cel:CELE_B0495.2; -.
DR UCSC; B0495.2; c. elegans. [Q09437-1]
DR CTD; 174244; -.
DR WormBase; B0495.2a; CE01761; WBGene00015203; cdk-11.1. [Q09437-1]
DR WormBase; B0495.2b; CE52485; WBGene00015203; cdk-11.1. [Q09437-2]
DR eggNOG; KOG0663; Eukaryota.
DR GeneTree; ENSGT00970000196694; -.
DR HOGENOM; CLU_000288_91_3_1; -.
DR InParanoid; Q09437; -.
DR OMA; MDKIYMA; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; Q09437; -.
DR PRO; PR:Q09437; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00015203; Expressed in germ line (C elegans) 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:0007276; P:gamete generation; IMP:UniProtKB.
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 CDD; cd07843; STKc_CDC2L1; 1.
DR InterPro; IPR045267; CDK11/PITSLRE_STKc.
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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..719
FT /note="Cyclin-dependent kinase 11.1"
FT /id="PRO_0000086834"
FT DOMAIN 356..647
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..144
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..293
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 484
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 362..370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 13..22
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060204"
SQ SEQUENCE 719 AA; 83567 MW; 2190532B1FECF15D CRC64;
MSDHLGSSHD EGELSDESHK KSQRASSSDE PNPAKSNKGL ESKMRESILS RLSKRKNSES
DDDTTEQRFS IQPKNAQKAK EDRYRDKERD KKREKDKRDD RRDVRGPDAR QKDRDFKGRQ
ERSGRDQKVH EHRHHHHHRK HETDGHRTNR SNRDRSSERD SEKHKRHIDR HKKSSTTSPD
NDKSPHKKSK HTDVPADAKL FDRILDPNYK KKDDDVLVIE DVEMSPIEIL EEKEEKEIVE
FTIDSPAGPK KYSKFESDPE SDHDDTKPKS PGKAEDDDDV IEVLDDALHS DDDADSDEDK
YLKTPEDREW EEMTETEQRL HKEAMKKRAS MKQKTLIAQL PVFYPGLMGC RNIDEYECVN
RVDEGTFGVV YRGKDKRTDE IVALKRLKME KEKEGFPITA LREINMLLKA GNHPNIVNVK
EILLGSNMDK IYMAMEFVEH DMKSLLDTMS RRNKRFSIGE QKTLLQQLLS GIEHMHKLWI
LHRDLKTSNL LMSHKGILKI ADFGLAREYG DPLKKFTSIV VTLWYRSPEL LLGTRLYSTP
VDMWSVGCIM AEFILLKPLF PGRGELEQIK KIFMEMGTPT ESIWPGVTEL DGWKALTFEK
YPYNQLRKRF LAGRLLNDTG FKLLNGLLTL DPKNRFSATQ ALDHEWFTEE PYPVPPEEFP
TFPAKSEQNK APPPAKQKQQ ENRISHVDPE TAKLLKQFEV RPEQVKPGGF SLKFDPTRF
