CDK17_CAEEL
ID CDK17_CAEEL Reviewed; 667 AA.
AC Q8I7M8; G5EDS3;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cyclin-dependent kinase 17 {ECO:0000305};
DE EC=2.7.11.22 {ECO:0000269|PubMed:20510931};
DE AltName: Full=Cell division protein kinase 17 {ECO:0000305};
DE AltName: Full=PCTAIRE-motif protein kinase {ECO:0000305|PubMed:20510931};
GN Name=pct-1 {ECO:0000312|WormBase:C07G1.3c};
GN ORFNames=C07G1.3 {ECO:0000312|WormBase:C07G1.3c};
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|EMBL:AAD37120.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAD37120.1};
RX PubMed=10207147; DOI=10.1242/dev.126.10.2227;
RA Boxem M., Srinivasan D.G., van den Heuvel S.;
RT "The Caenorhabditis elegans gene ncc-1 encodes a cdc2-related kinase
RT required for M phase in meiotic and mitotic cell divisions, but not for S
RT phase.";
RL Development 126:2227-2239(1999).
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH CYY-1, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF ASP-467.
RX PubMed=20510931; DOI=10.1016/j.cell.2010.04.011;
RA Ou C.Y., Poon V.Y., Maeder C.I., Watanabe S., Lehrman E.K., Fu A.K.,
RA Park M., Fu W.Y., Jorgensen E.M., Ip N.Y., Shen K.;
RT "Two cyclin-dependent kinase pathways are essential for polarized
RT trafficking of presynaptic components.";
RL Cell 141:846-858(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase, which, in association with
CC cyy-1, regulates the trafficking of synaptic vesicles in the DA9 motor
CC neuron and probably also in the DD motor neurons and in RIA
CC interneurons. {ECO:0000269|PubMed:20510931}.
CC -!- FUNCTION: [Isoform c]: Sufficient for synaptic vesicle trafficking in
CC the DA9 motor neuron. {ECO:0000269|PubMed:20510931}.
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:0000269|PubMed:20510931};
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:0000269|PubMed:20510931};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20510931};
CC Note=Binds 2 Mg(2+) ions. {ECO:0000250|UniProtKB:P24941};
CC -!- SUBUNIT: Interacts with cyy-1; the interaction is required to activate
CC pct-1. {ECO:0000269|PubMed:20510931}.
CC -!- INTERACTION:
CC Q8I7M8; P34624: cyy-1; NbExp=2; IntAct=EBI-2918577, EBI-2696495;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20510931}. Cell
CC projection, dendrite {ECO:0000269|PubMed:20510931}. Cell projection,
CC axon {ECO:0000269|PubMed:20510931}. Note=Evenly distributed in the
CC dendrite, the axon and the cell body of the DA motor neuron.
CC {ECO:0000269|PubMed:20510931}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=c {ECO:0000312|WormBase:C07G1.3a};
CC IsoId=Q8I7M8-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C07G1.3c};
CC IsoId=Q8I7M8-2; Sequence=VSP_057763;
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; AF129110; AAD37120.1; -; mRNA.
DR EMBL; FO080125; CCD61393.1; -; Genomic_DNA.
DR EMBL; FO080125; CCD61395.1; -; Genomic_DNA.
DR PIR; T15445; T15445.
DR RefSeq; NP_001021312.1; NM_001026141.3. [Q8I7M8-1]
DR RefSeq; NP_501372.1; NM_068971.5. [Q8I7M8-2]
DR AlphaFoldDB; Q8I7M8; -.
DR SMR; Q8I7M8; -.
DR ComplexPortal; CPX-4962; CyclinY-CDK17 complex.
DR IntAct; Q8I7M8; 2.
DR STRING; 6239.C07G1.3b; -.
DR EPD; Q8I7M8; -.
DR PaxDb; Q8I7M8; -.
DR EnsemblMetazoa; C07G1.3a.1; C07G1.3a.1; WBGene00003961. [Q8I7M8-2]
DR EnsemblMetazoa; C07G1.3a.2; C07G1.3a.2; WBGene00003961. [Q8I7M8-2]
DR EnsemblMetazoa; C07G1.3c.1; C07G1.3c.1; WBGene00003961. [Q8I7M8-1]
DR GeneID; 177615; -.
DR KEGG; cel:CELE_C07G1.3; -.
DR UCSC; C07G1.3a.1; c. elegans. [Q8I7M8-1]
DR CTD; 177615; -.
DR WormBase; C07G1.3a; CE06779; WBGene00003961; pct-1. [Q8I7M8-2]
DR WormBase; C07G1.3c; CE32571; WBGene00003961; pct-1. [Q8I7M8-1]
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000156963; -.
DR HOGENOM; CLU_000288_154_1_1; -.
DR OMA; DDVGWER; -.
DR OrthoDB; 1010560at2759; -.
DR PRO; PR:Q8I7M8; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003961; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008089; P:anterograde axonal transport; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0048489; P:synaptic vesicle transport; IC:ComplexPortal.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 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; Cell projection; Cytoplasm; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..667
FT /note="Cyclin-dependent kinase 17"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433390"
FT DOMAIN 328..609
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..667
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 449
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 334..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT VAR_SEQ 1..225
FT /note="MTAYSPADSNAEARLLSGGSDPISDTENLLDLAYEVGTSSSDNTRYDRESEN
FT DEEEIGVGWEDTTSSSLNKRMCKSATFHDFCDDSEYSRRPVTTLHEEDFDEEEEDEFED
FT ASDRRNLDEDDVEYEDEDDEDDIVVEEEEITPEDIEHSPTGVTTQTTPPSNNTSKSKKK
FT KKRKSDEEDGLRKMKKSSTFASFLNMFVSRRRSGRDSGERLMSRSTCMLRPSISL ->
FT MKKLKRRLSAAFRPGSNNNVSITSSGGSYYDSDCEGRNNIVIGYGMMSAPLHGRTWTLS
FT ESMSHLSDKNGAILEECAVVDPTALLRVSRGGTAGRRYDTNVNYINGMHVPPPRTHSLY
FT YPRGYNSRRNSYYGSNA (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057763"
FT MUTAGEN 467
FT /note="D->N: In wy575; abnormal localization of several
FT synaptic vesicle components and active zone proteins in the
FT cell body and in the dendrite of DA9 motor neuron. No other
FT phenotype except a slightly smaller progeny size."
FT /evidence="ECO:0000269|PubMed:20510931"
SQ SEQUENCE 667 AA; 76153 MW; 8570731607218A3F CRC64;
MTAYSPADSN AEARLLSGGS DPISDTENLL DLAYEVGTSS SDNTRYDRES ENDEEEIGVG
WEDTTSSSLN KRMCKSATFH DFCDDSEYSR RPVTTLHEED FDEEEEDEFE DASDRRNLDE
DDVEYEDEDD EDDIVVEEEE ITPEDIEHSP TGVTTQTTPP SNNTSKSKKK KKRKSDEEDG
LRKMKKSSTF ASFLNMFVSR RRSGRDSGER LMSRSTCMLR PSISLSVVQE SMILGSDGES
VEVSPCTSDQ TPTGVPPRYI VNVKMRQKTA RKWSEEEIQK RLSLPADLRL PVAVVDKLNR
TPTLDQPLTR KNRRASLSEI GFGKLETYEK LDKLGEGTYA TVFRGRSILT NKFVALKEIR
LEQEEGAPCT AIREVSLLRN LRHANVVTLH DIIHTDRLLT LVFEYVDRDL KQYMDSCNNA
MQMNNIRLFL YQLLRGLAYC HQRRVLHRDL KPQNLLITAK GELKLADFGL ARAKSVPTKT
YSNEVVTLWY RPPDVLLGST DYSTHIDMWG VGCILFEMIA GRALFPGGTP TEQLGLIFRT
LGSPRPDRHP TICEKPTFYP YANRHYNPDP LCRQIPRIDA HGFELLMKFL QYEGKDRVSA
AEAVKHPFLR TIAVKCCHLR DEQSVLEADG IHIERELLAS DHHHSSRRHH RGTLVKDKYR
MHSSHHT
