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Database: UniProt
Entry: A0A2K6AXH0_MACNE
LinkDB: A0A2K6AXH0_MACNE
Original site: A0A2K6AXH0_MACNE 
ID   A0A2K6AXH0_MACNE        Unreviewed;      2052 AA.
AC   A0A2K6AXH0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-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:ENSMNEP00000003828.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000003828.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000003828.1}
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; ENSMNET00000019495.1; ENSMNEP00000003828.1; ENSMNEG00000015804.1.
DR   GeneTree; ENSGT01030000234517; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000015804; Expressed in temporal lobe and 7 other cell types or tissues.
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:UP000233120};
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          1373..1422
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1454..1574
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1617..1907
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          1301..1362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1931..2037
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          458..1223
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1976..2024
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2052 AA;  234897 MW;  068E9AF095F8A914 CRC64;
     MLKFKYGTRN PLDAGAAEPI ASRASRLNLF FQGKPPFMTQ QQMSPLSREG ILDALFVLFE
     ECSQPALMKI KHVSNFVRKY SDTIAELQEL QPSTKDFEVR SLVGCGHFAE VQVVREKATG
     DIHAMKVMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNHL YLVMEYQPGG
     DLLSLLNRYE DQLDENLIQF YLAELILAVH SVHQMGYVHR DIKPENILID RTGHIKLVDF
     GSAAKMNSNK MVNARLPIGT PDYMAPEVLT VMNADGKGTY GLDCDWWSVG VIAYEMIYGR
     SPFAEGTSAR TFNNIMNFQR FLKFPDDPKV SSDFLDLIQS LLCGQKERLK FEGLCCHPFF
     SKIDWNNIRN SPPPFVPTLK SDDDTSNFDE PEKNSWVSSS PCQLSPSGFL GEELPFVGFS
     YSKALGILGR SESVVSGLDS PAKTSSMEKK LLIKSKELQD SQDKCHKMEQ EMTRLHRRVS
     EVEAVLSQKE VELKASETQR SLLEQDLATY ITECSSLKRS LEQARMEVSQ EDDKALQLLH
     DIREQSRKLQ EIKEQEYQAQ VEEMRLMMNQ LEEDLVSARR RSDLYESELR ESRLAAEEFK
     RKATECQHKL LKVINAEQQL KIQELQEKLE KAVKASTEAT ELLQNIRQAK ERAERELEKL
     QNREDSSEGI RKKLVEAEER RHSLENKVKR LETMERRENR LKDDIQTKSQ QIQQMADKIL
     ELEEKHREAQ VSAQHLEVHL KQKEQHYEEK IKVLDNQIKK DLADKETLEN MMQRHEEEAH
     EKGKILSEQK AMINAMDSKI 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 EYQLENIQVL YSHEKVKMEG TISQQTKLID FLQAKMDQPA
     KKKKVPLQYN 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 EKAEADAARV CVSYELLPAW VQKLLGNSLL KLEGDDRLDM
     NCTLPFSDQV VLVGTEEGLY ALNVLKNSLT HVPGIGAVFQ IYIIKDLEKL LMIAGEERAL
     CLVDVKKVKQ SLAQSHLPAQ PDISPNIFEA VKGCHLFGAG KIENGLCICA AMPSKVVILR
     YNENLSKYCI RKEIETSEPC SCIHFTNYSI LIGTNKFYEI DMKQYTLEEF LDKNDHSLAP
     AVFAASSNSF PVSIVQVNSA GQREEYLLCF HEFGVFVDSY GRRSRTDDLK WSRLPLAFAY
     REPYLFVTHF NSLEVIEIQA RSSAGTPARA YLDIPNPRYL GPAISSGAIY LASSYQDKLR
     VICCKGNLVK ESGTEHHRGP STSRSPNKRG PPTYNEHITK RVASSPAPPE GPSHPREPST
     PHRYREGRTE LRRDKSPGRP LEREKSPGRM LSTRRERSPG RLFEDSSRGR LPAGAVRTPL
     SQVNKVWDQS SV
//
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