ID I3MC26_ICTTR Unreviewed; 2054 AA.
AC I3MC26;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Citron Rho-interacting kinase {ECO:0000256|PIRNR:PIRNR038145};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038145};
GN Name=CIT {ECO:0000313|Ensembl:ENSSTOP00000007769.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000007769.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000007769.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays a role in cytokinesis. Displays serine/threonine
CC protein kinase activity. {ECO:0000256|PIRNR:PIRNR038145}.
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:0000256|ARBA:ARBA00001433,
CC ECO:0000256|PIRNR:PIRNR038145};
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:0000256|ARBA:ARBA00000775,
CC ECO:0000256|PIRNR:PIRNR038145};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR038145}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|PIRNR:PIRNR038145}.
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DR EMBL; AGTP01090500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005336878.1; XM_005336821.1.
DR STRING; 43179.ENSSTOP00000007769; -.
DR Ensembl; ENSSTOT00000008668.3; ENSSTOP00000007769.3; ENSSTOG00000008634.3.
DR GeneID; 101957378; -.
DR CTD; 11113; -.
DR eggNOG; KOG0976; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_2_1; -.
DR InParanoid; I3MC26; -.
DR OrthoDB; 3490126at2759; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IEA:Ensembl.
DR CDD; cd20814; CRIK; 1.
DR CDD; cd05601; STKc_CRIK; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR017405; Citron_Rho-interacting_kinase.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR037708; CRIK_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988:SF71; CITRON RHO-INTERACTING KINASE; 1.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF038145; Citron_Rho-interacting_kinase; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038145};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR038145};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR038145};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038145};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038145};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR038145};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038145};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 97..360
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 361..431
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1389..1438
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1470..1590
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1618..1908
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1317..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1933..2038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..1239
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1940..1954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1978..2026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2054 AA; 235114 MW; 54EE6B02CA3DCAA5 CRC64;
MLKFKYGSRN TQDAGAVEPI ASRASRLNLF FQGKPPFMTQ QQMSPLSREG ILDALFVLFE
ECSQPALMKI KHVSNFVRKY SDIIAELQEL QPSAKDFEVR SLVGCGHFAE VQVVRERATG
DIYAMKIMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNNL YLVMEYQPGG
DLLSLLNRYE DQLDENMIQF YLAELILAVH SVHQMGYVHR DIKPENVLID RTGHIKLVDF
GSAAKMNSNQ MVNSKLPIGT PDYMAPEVLT IMNGDGKGVY GPDCDWWSVG VIAYEMVYGR
TPFTEGTSAR TFNNIMNFQR FLKFPDDPKV SSGFLDLIQS LLCGQRERLK FEGLCCHPFF
SKIDWNDIRN SPPPFVPTLK SDDDTSNFDE PEKNSWVSSS LCQLSPSGFS GEELPFVGFS
YSKALGILGR SESVVSGLDS PAKTSSMEKK LLIKSKELQD SQDKCHKMEQ EMTRLHRRVS
EVEAVLSQKE VELKASETQR SLLEQDLATY ITECSSLKRS LEQARMEVSQ EDDKALQLLH
DIREQSRKLQ EIKEQEYQAQ VEEMRLMMNQ LEEDLVSARR RSDLYESELR ESRLAAEEFK
RKATECQHKL MKAKDQGKPE AGEYSKLEKI NAEQQLKIRE LQEKLEKAVK ASTEATELLQ
NIRQAKERAE RELEKLQNRE DSSEGIRKKL VEAEERRHSL ENKVKRLETM ERRENRLKDD
IQTKSQQIQQ MADKILELEE KHREAQVSAQ HLEVHLKQKE QHYEEKIKVL DNQIKKDLAD
KESLENLMQR HEEEAHEKGK ILSEQKAMIN AMDSKIRSLE QRIVELSEAN KLAANSSLFT
QRNMKAQEEM ISELRQQKFY LETQAGKLEA QNRKLEEQLE KISHQDHSDK SRLLELETRL
RGVSLEHEEQ KLELKRQLTE LQLSLQERES QLTALQAARA ALESQLRQAK TELEETTAEA
EEEIQALTAH RDEIQRKFDA LRNSCTVITD LEEQLNQLTE DNAELNNQNF YLSKQLDEAS
GANDEIVQLR SEVDHLRREI TEREMQLTSQ KQTMEALKTT CTMLEEQVMD LEALNDELLE
KERQWEAWRS VLGDEKSQFE CRVRELQRML DTEKQSRARA DQRITESRQV VELAVKEHKA
EILALQQALK EQKLKAESLS DKLNDLEKKH AMLEMNARSL QQKLETEREL KQRLLEEQAK
LQQQMDMQKN HIFRLTQGLQ EALDRADLLK TERSDLEYQL ENIQVLYSHE KVKMEGTISQ
QTKLIDFLQA KMDQPAKKKK VPLQYNELKL ALEKEKARCA ELEEALQKTR IELRSAREEA
AHRKATDHPH PSTPATARQQ IAMSAIVRSP EHQPSAMSLL APPSSRRKES STPEEYSRRL
KERMHHNIPH RFNVGLNMRA TKCAVCLDTV HFGRQASKCL ECQVMCHPKC STCLPATCGL
PAEYATHFTE AFCRDKMNSP GLQTKDPSSS LHLEGWMKVP RNNKRGQQGW DRKYIVLEGS
KVLIYDNEAR EAGQRPVEEF ELCLPDGDVS IHGAVGASEL ANTAKADVPY ILKMESHPHT
TCWPGRTLYL LAPSFPDKQR WVTALESVVA GGRVSREKAE ADAKLLGNSL LKLEGDDRLD
MNCTLPFSDQ VVLVGTEEGL YALNVLKNSL THVPGVGAVF QIYIIKDLEK LLMIAGEERA
LCLVDVKKVK QSLAQSHLPA QPDISPNIFE AVKGCHLFAA GKIENGLCIC AAMPNKVVIL
RYNENLSKYC IRKEIETSEP CSCIHFTNYS ILIGTNKFYE IDMKQYTLEE FLDKNDHSLA
PAVFASSSNS FPVSIVQVNG AGQREEYLLC FHEFGVFVDS YGRRSRTDDL KWSRLPLAFA
YREPYLFVTH FNSLEVIEIQ ARSSLGTPAR AYLEIPNPRY LGPAISSGAI YLASSYQDKL
RVICCKGNLV KESGTDHHRV PSTSRSSPNK RGPPTYNEHI TKRVASSPAP PEGPSHPREP
STPHRYREGR TELRRDKSPG RPLEREKSPG RMLSTRRERS PGRLFEDSSR GRLPVGAVRT
PLSQVNKVWD QSSV
//
