ID A0A2K5JSD0_COLAP Unreviewed; 2037 AA.
AC A0A2K5JSD0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Citron Rho-interacting kinase {ECO:0000256|PIRNR:PIRNR038145};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038145};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000031752.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000031752.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSCANT00000054972.1; ENSCANP00000031752.1; ENSCANG00000039254.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20814; CRIK; 1.
DR CDD; cd05601; STKc_CRIK; 1.
DR Gene3D; 1.20.5.170; -; 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; 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; 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:UP000233080};
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 65..328
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 329..399
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1372..1421
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1453..1573
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1601..1891
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1300..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1915..2022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 426..1207
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1923..1937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..2009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2037 AA; 233046 MW; 99C5DB204206FBC7 CRC64;
GKPPFMTQQQ MSPLSREGIL DALFVLFEEC SQPALMKIKH VSNFVRKYSD TIAELQELQP
SAKDFEVRSL VGCGHFAEVQ VVREKATGDI HAMKVMKKKA LLAQEQVSFF EEERNILSQS
TSPWIPQLQY AFQDKNHLYL VMEYQPGGDL LSLLNRYEDQ LDENLIQFYL AELILAVHSV
HQMGYVHRDI KPENILIDRT GHIKLVDFGS AAKMNSNKMV NAKLPVGTPD YMAPEVLTVM
NADGKGTYGL DCDWWSVGVI AYEMIYGRSP FAEGTSARTF NNIMNFQRFL KFPDDPKVSS
DFLDLIQSLL CGQKERLKFE GLCCHPFFSK IDWNNIRNSP PPFVPTLKSD DDTSNFDEPE
KNSWVSSSPC QLSPSGFSGE ELPFVGFSYS KALGILGRSE SVVSGLDSPA KTSSMEKKLL
IKSKELQDSQ DKCHKMEQEM TRLHRRVSEV EAVLSQKEVE LKASETQRSL LEQDLATYIT
ECSSLKRSLE QARMEVSQED DKALQLLHDI REQSRKLQEI KEQEYQAQVE EMRLMMNQLE
EDLVSARRRS DLYESELRES RLAAEEFKRK ATECQHKLLK AKDQGKPEVG EYAKLEKINA
EQQLKIQELQ EKLEKAVKAS TEATELLQNI RQAKERAERE LEKLQNREDS SEGIRKKLVE
AEERRHSLEN KVKRLETMER RENRLKDDIQ TKSQQIQQMA DKILELEEKH REAQVSAQHL
EVHLKQKEQH YEEKIKVLDN QIKKDLADKE TLENMMQRHE EEAHEKGKIL SEQKAMINAM
DSKIRSLEQR IVELSEANKL AANSSLFTQR NMKAQEEMIS ELRQQKFYLE TQAGKLEAQN
RKLEEQLEKI SHQDHSDKNR LLELETRLRE VSLEHEEQKL ELKRQLTELQ LSLQERESQL
TALQAARAAL ESQLRQAKTE LEETTAEAEE EIQALTAHRD EIQRKFDALR NSCTVITDLE
EQLNQLTEDN AELNNQNFYL SKQLDEASGA NDEIVQLRSE VDHLRREITE REMQLTSQKQ
TMEALKTTCT MLEEQVMDLE ALNDELLEKE RQWEAWRSVL GDEKSQFECR VRELQRMLDT
EKQSRARADQ RITESRQVVE LAVKEHKAEI LALQQALKEQ KLKAESLSDK LNDLEKKHAM
LEMNARSLQQ KLETERELKQ RLLEEQAKLQ QQMDLQKNHI FRLTQGLQEA LDRADLLKTE
RSDLEYQLEN IQVLYSHEKV KMEGTISQQT KLIDFLQAKM DQPAKKKKGL FSRRKEDPAL
PTQVPLQYNE LKLALEKEKA RCAELEEALQ KTRIELRSAR EEAAHRKATD HPHPSTPATA
RQQIAMSAIV RSPEHQPSAM SLLAPPSSRR KESSTPEEFS RRLKERMHHN IPHRFNVGLN
MRATKCAVCL DTVHFGRQAS KCLECQVMCH PKCSTCLPAT CGLPAEYATH FTEAFCRDKM
NSPGLQTKEP SSSLHLEGWM KVPRNNKRGQ QGWDRKYIVL EGSKVLIYDN EAREAGQRPV
EEFELCLPDG DVSIHGAVGA SELANTAKAD VPYILKMESH PHTTCWPGRT LYLLAPSFPD
KQRWVTALES VVAGGRVSRE KAEADAKLLG NSLLKLEGDD RLDMNCTLPF SDQVVLVGTE
EGLYALNVLK NSLTHVPGIG AVFQIYIIKD LEKLLMIAGE ERALCLVDVK KVKQSLAQSH
LPAQPDISPN IFEAVKGCHL FGAGKIENGL CICAAMPSKV VILRYNENLS KYCIRKEIET
SEPCSCIHFT NYSILIGTNK FYEIDMKQYT LEEFLDKNDH SLAPAVFAAS SNSFPVSIVQ
VNSAGQREEY LLCFHEFGVF VDSYGRRSRT DDLKWSRLPL AFAYREPYLF VTHFNSLEVI
EIQARSSAGT PARAYLDIPN PRYLGPAISS GAIYLASSYQ DKLRVICCKG NLVKESGTEH
HRGPSTSRSS PNKRGPPTYN EHITKRVASS PAPPEGPSHP REPSTPHRYR EGRTELRRDK
SPGRPLEREK SPGRMLSTRR ERSPGRLFED SSRGRLPAGA VRTPLSQVNK VWDQSSV
//