CILK1_RAT
ID CILK1_RAT Reviewed; 629 AA.
AC Q62726;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Serine/threonine-protein kinase ICK;
DE EC=2.7.11.1 {ECO:0000269|PubMed:8570168};
DE AltName: Full=Intestinal cell kinase;
DE AltName: Full=MAK-related kinase;
DE Short=MRK;
GN Name=Cilk1; Synonyms=Ick;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:BAA05166.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND AUTOPHOSPHORYLATION.
RC TISSUE=Heart {ECO:0000312|EMBL:BAA05166.1};
RX PubMed=8570168;
RA Abe S., Yagi T., Ishiyama S., Hiroe M., Marumo F., Ikawa Y.;
RT "Molecular cloning of a novel serine/threonine kinase, MRK, possibly
RT involved in cardiac development.";
RL Oncogene 11:2187-2195(1995).
CC -!- FUNCTION: Required for ciliogenesis, particularly in neuronal and
CC retinal progenitor cells (By similarity). Phosphorylates KIF3A (By
CC similarity). Involved in the control of ciliary length (By similarity).
CC Regulates the ciliary localization of SHH pathway components as well as
CC the localization of IFT components at ciliary tips (By similarity). May
CC play a role in cardiac development (PubMed:8570168). Regulates
CC intraflagellar transport (IFT) speed and negatively regulates cilium
CC length in a cAMP and mTORC1 signaling-dependent manner and this
CC regulation requires its kinase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q9JKV2, ECO:0000303|PubMed:8570168}.
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:8570168};
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:8570168};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8570168};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8570168}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:Q9JKV2}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UPZ9}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q9JKV2}. Note=Also found at the ciliary
CC tip. {ECO:0000250|UniProtKB:Q9JKV2}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic heart from day 11. Highly
CC expressed in the uterus and at lower levels in brain, heart, lung,
CC kidney, skeletal muscle, ovary and liver in adult tissues.
CC {ECO:0000269|PubMed:8570168}.
CC -!- PTM: Autophosphorylated on serine and threonine residues
CC (PubMed:8570168). Phosphorylation at Thr-157 increases kinase activity
CC (By similarity). {ECO:0000250|UniProtKB:Q9JKV2,
CC ECO:0000250|UniProtKB:Q9NYX3, ECO:0000269|PubMed:8570168}.
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; D26178; BAA05166.1; -; mRNA.
DR RefSeq; NP_620241.1; NM_138886.1.
DR AlphaFoldDB; Q62726; -.
DR SMR; Q62726; -.
DR STRING; 10116.ENSRNOP00000012257; -.
DR iPTMnet; Q62726; -.
DR PhosphoSitePlus; Q62726; -.
DR jPOST; Q62726; -.
DR PaxDb; Q62726; -.
DR PRIDE; Q62726; -.
DR ABCD; Q62726; 1 sequenced antibody.
DR GeneID; 84411; -.
DR KEGG; rno:84411; -.
DR UCSC; RGD:71050; rat.
DR CTD; 22858; -.
DR RGD; 71050; Ick.
DR eggNOG; KOG0661; Eukaryota.
DR InParanoid; Q62726; -.
DR OrthoDB; 76933at2759; -.
DR PhylomeDB; Q62726; -.
DR PRO; PR:Q62726; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0097546; C:ciliary base; ISS:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0035720; P:intraciliary anterograde transport; ISS:UniProtKB.
DR GO; GO:0035721; P:intraciliary retrograde transport; ISS:UniProtKB.
DR GO; GO:0042073; P:intraciliary transport; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
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 ATP-binding; Cell projection; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Developmental protein; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..629
FT /note="Serine/threonine-protein kinase ICK"
FT /id="PRO_0000086009"
FT DOMAIN 4..284
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 292..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06493,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NYX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPZ9"
FT MOD_RES 159
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPZ9"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKV2"
SQ SEQUENCE 629 AA; 70569 MW; AA4143D73F891E8B CRC64;
MNRYTTIKQL GDGTYGSVLL GRSIESGELI AIKKMKRKFY SWEECMNLRE VKSLKKLNHA
NIVKLKEVIR ENDHLYFIFE YMKENLYQLI KERNKLFPES AIRNIMYQIL QGLAFIHKHG
FFHRDLKPEN LLCMGPELVK IADFGLAREI RSRPPYTDYV STRWYRAPEV LLRSTNYSSP
IDVWAVGCIM AEVYTLRPLF PGASEIDTIF KICQVLGTPK KTDWPEGYQL SSAMNFIWPQ
CIPNNLKTLI PNASSEAIQL LRDLLQWDPK KRPTASQALR YPYFQIGHPL GISTQDSGKP
QKDVQDKTGP PPYVKPAPPA QAPTKAHTLI SSRPNQASQP HQHFVYPYKG EASRTEQLSH
VQEGQPNPPF FPSLHNKNLP PKILAGLEQK SGDMKPKSRR RWGLISRSTK GSDDWADLAD
LDFSSSLTRI DVKNKKRQSD DPLCRFESVL DLKPSEPVGT GTSVSTQASS QRRDTPTLQS
TAKQHYLKHS RYLPGINIRN GVLPNPGKDF LPSSSWSSSG LSGKSSGTVS VVSKITSVGS
GSTSSTGLTG SYIPSFLKKE VGSVMQRVQL APLAAPSPGY SSLKAVRPHP GRPFFHTQPR
STPGLIPRPP AVQPVHGRID WSSKYPSRR
