ID A0A2I3H1S3_NOMLE Unreviewed; 2048 AA.
AC A0A2I3H1S3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:ENSNLEP00000037470.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000037470.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000037470.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000037470.1}
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; ADFV01121712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01121713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01121714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01121715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01121716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01121717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01121718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01121719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01121720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01121721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 61853.ENSNLEP00000037470; -.
DR Ensembl; ENSNLET00000040571.1; ENSNLEP00000037470.1; ENSNLEG00000000249.3.
DR GeneTree; ENSGT01030000234517; -.
DR InParanoid; A0A2I3H1S3; -.
DR OMA; EGETHQK; -.
DR Proteomes; UP000001073; Chromosome 10.
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: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 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 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; 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:UP000001073};
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..355
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 356..426
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1383..1432
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1464..1584
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1612..1902
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1311..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1926..2033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 453..743
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 793..1230
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1934..1948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1972..2020
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 2048 AA; 234186 MW; 8C9E0AFDC7C61B32 CRC64;
MLKFKYGARN PLDAGAAEPI ASRASRLNLF FQGKPPFMTQ QQMSPLSREG ILDALFVLFE
ECSQPALMKI KHVSNFVRKY SDTIAELQEL QPSAKDFEVR SLVGCGHFAE VQVVREKATG
DIYAMKVMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNHL YLVMEYQPGG
DLLSLLNRYE DQLDENLIQF YLAELILAVH SIHLMGYVHR NILIDRTGHI KLVDFGSAAK
MNSNKMVNAK LPIGTPDYMA PEVLTVMNGD GKGTYGLDCD WWSVGVIAYE MIYGRSPFAE
GTSARTFNNI MNFQRFLKFP DDPKVSSDFL DLVQSLLCGQ KERLKFEGLC CHPFFSKIDW
NNIRNSPPPF VPTLKSDDDT SNFDEPEKNS WVSSSPCQLS PSGFSGEELP FVGFSYSKAL
GILGRSESVV SGLDSPAKTS SMEKKLLIKS KELQDSQDKC HKMEQEMTRL HRRVSEVEAV
LSQKEVELKA SETQRSLLEQ DLATYITECS SLKRSLEQAR MEVSQEDDKA LQLLHDIREQ
SRKLQEIKEQ EYQAQVEEMR LMMNQLEEDL VSARRRSDLY ESELRESRLA AEEFKRKATE
CQHKLLKAKD QGKPEVGEYA KLEKINAEQQ LKIQELQEKL EKAVKASTEA TELLQNIRQA
KERAERELEK LQNREDSSEG IRKKLVEAEE RRHSLENKVK RLETMERREN RLKDDIQTKS
QQIQQMADKI LELEEKHREA QVSAQHLEVH LKQKEQHYEE KIKVKTFYDL PWPCSYNTMY
KHKAVCTMSC QMINAMDSKI RSLEQRIVEL SEANKLAANS SLFTQRNMKA QEEMISELRQ
QKFYLETQAG KLEAQNRKLE EQLEKISHQD HSDKNRLLEL ETRLREVSLE HEEQKLELKR
QLTELQLSLQ ERESQLTALQ AARAALESQL RQAKTELEET TAEAEEEIQA LTAHRDEIQR
KFDALRNSCT VITDLEEQLN QLTEDNAELN NQNFYLSKQL DEASGANDEI VQLRSEVDHL
RREITEREMQ LTSQKQTMEA LKTTCTMLEE QVMDLEALND ELLEKERQWE AWRSVLGDEK
SQFECRVREL QRMLDTEKQS RARADQRITE SRQVVELAVK EHKAEILALQ QALKEQKLKA
ESLSDKLNDL EKKHAMLEMN ARSLQQKLET ERELKQRLLE EQAKLQQQMD LQKNHIFRLT
QGLQEALDRA DLLKTERSDL EYQLENIQVR TGRENLLKNG LHGWAQWLMP VIPAVWEAKG
LFSRRKEDPA LPTQVPLQYN ELKLALEKEK ARCAELEEAL QKTRIELRSA REEAAHRKAT
DHPHPSTPAT ARQQIAMSAI VRSPEHQPSA MSLLAPPSSR RKESSTPEEF SRRLKERMHH
NIPHRFNVGL NMRATKCAVC LDTVHFGRQA SKCLECQVMC HPKCSTCLPA TCGLPAEYAT
HFTEAFCRDK MNSPGLQTKE PSSSLHLEGW MKVPRNNKRG QQGWDRKYIV LEGSKVLIYD
NEAREAGQRP VEEFELCLPD GDVSIHGAVG ASELANTAKA DVPYILKMES HPHTTCWPGR
TLYLLAPSFP DKQRWVTALE SVVAGGRVSR EKAEADAKLL GNSLLKLEGD DRLDMNCTLP
FSDQVVLVGT EEGLYALNVL KNSLTHVPGI GAVFQIYIIK DLEKLLMIAG EERALCLVDV
KKVKQSLAQS HLPAQPDISP NIFEAVKGCH LFGAGKIENG LCICAAMPSK VVILRYNENL
SKYCIRKEIE TSEPCSCIHF TNYSILIGTN KFYEIDMKQY TLEEFLDKND HSLAPAVFAA
SSNSFPVSIV QVNSAGQREE YLLCFHEFGV FVDSYGRRSR TDDLKWSRLP LAFAYREPYL
FVTHFNSLEV IEIQARSSAG TPARAYLDIP NPRYLGPAIS SGAIYLASSY QDKLRVICCK
GNLVKESGTE HHRGPSTSRS SPNKRGPPTY NEHITKRVAS SPAPPEGPSH PREPSTPHRY
REGRTELRRD KSPGRPLERE KSPGRMLSTR RERSPGRLFE DSSRGRLPAG AVRTPLSQVN
KVWDQSSV
//
