ID H2UTA1_TAKRU Unreviewed; 2001 AA.
AC H2UTA1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 82.
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:ENSTRUP00000040174.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000040174.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000040174.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000040174.3}
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|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 STRING; 31033.ENSTRUP00000072735; -.
DR Ensembl; ENSTRUT00000040316.3; ENSTRUP00000040174.3; ENSTRUG00000015721.3.
DR eggNOG; KOG0612; Eukaryota.
DR eggNOG; KOG0976; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR TreeFam; TF101140; -.
DR Proteomes; UP000005226; Chromosome 19.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0048468; P:cell development; IEA:UniProt.
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; 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; 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 PIRSF; PIRSF038145; Citron_Rho-interacting_kinase; 2.
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|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 Reference proteome {ECO:0000313|Proteomes:UP000005226};
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 99..359
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 360..432
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1354..1403
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1435..1555
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1583..1873
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 383..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1931..2001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 452..610
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 653..684
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 719..788
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 813..1156
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1258..1292
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1316..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1939..1970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2001 AA; 228776 MW; BABB4D900AC3A6CF CRC64;
MLKFKYVSQG NLKPSLSPLD PITIRSSRLN QVFQGRVSLC GQQGGCTVGR EEFLEALLIL
YKECTSPALM KIQNVANFVN KFSEAIAELQ VLQPCVDDFD VRAVVGRGHF AEVQVVREKA
TGDVCALKVM KKAFLRSQEN VVFHEEERSI LALNSSPWIP QLLYAFQDKE HVYLAMEYLP
GGDLMSLLNR YEDQFDESMA QFYLSELVEA IHTVHQLGYV HRDVKPENVL IDRTGHIKLA
DFGSAARLTV AFHTIPVGTQ DFLSPEVLTA MNGGPNCTYG IECDWWSLGV IAYEMVYSRS
PFSEGTAAKT INNILNYQHF LKFPEEPRAS KQFVDLLQRL LCGAKERLGF QGLRCHSFFS
SVDWNNLRQV LPPFVPALHA EDDTSNFEEP EQAAPRPGSA AHQGAQPVGF QGQDLPFLGW
FFSRPLTTLA KAESAPAGIN SPAKTNSMEK KLHLKSRELQ ETQDKCHKME QEISRFQRKM
TDLESVLHQK DVELKASETQ RSILEQDLAT YITECSSLKR SLEEARVEVS REDDKAMQLL
HDIREQSNKL QEIKEQEYHA QLEEMQVTIR QLEEDLSAAR RRSDLYEAEL RDSRQTSEEL
KRKAVEYQQR IQKVPFIPFT ECHCLKYIEA KLTKTNSEQQ VKILELQDKL SKAVKASTEA
TELLQNVRQA KDRLERDLER LRGKTDSSDT LKRRLRETEV TEQKEFNTNE YNISWLCFIK
ILEGQMKADL AEKESLEAKR AQQEEESREN SKLISEQKAT INAMDSKMKN LEQRIAELSE
ANKLAANSSI YTQKNMKAQE EMISELRQQK FYLESQAGKL EAQNAKLEEH LEKMSQQEQT
KRTRLLELES RLREMGLEHE EEKLEIKRQV SELTLSLQER ESQISSLQAA RLALESQLQQ
AKTELEETTA EAEEEITALR NQRDEIQRKF DALRDSCSVI TDLEEQLTQL SQENAELNRQ
NFYLSKQLDE ASDEREDQMQ LSHEVDRLRR EVADREMHLN NQKQNIETLK TTCSMLEEQV
VELESLNDEL LEKERQWEAW RGALEDEKSQ AERRTRDLQR LLDNEKQNRL RADQRSSESR
QAVELAVKEH KAEILALQQA LKEQRLKAES LSDTLNDLEK KHAMLEMNAR SLQQKLETER
ELKQRLMEEQ GKLQQQMDLQ KSHIFRLTQG LQDALDQTDM LKTERTDLEY QLENIQAVYS
HEKVKMEGTI SQQTKLIDFL QAKMDQPTKK KKVSERSLNT PQPQPAVPMQ YCDMKLALEK
ERSRCVELEE ALQKMRIELR SLREEAAHFK AQEHLPPSTP AQARHQILMS AIVKSPEHQP
NPSSLLNPST RSKETSTPEE FSRRVKERMH HNIPHRFTVG LNMRAAKCVV CLDTVHFGRQ
AATCLECHTL CHPKCSPCLP ATCGLPTEYA THFSEALCRE KANSPALQVK EASGHVRLEG
WMKQPRNNKR GQQGWETKYV VLDGTKVSIY DSEPREDYIN PEEEFELCLP DGEVTVHGAV
GSSELINTAK SDIPYVLKLE SHPHTSCWPG QSLYFMAPSF PDKQRWVAVL ESVVGSHRGS
REKVDSDAKL LGNSLLKLEG DDRLDINCTM PLTDQIVLVG SEEGLYALNV IKNSLTHIPG
LTSVFQIQIL KELDKLLMIT GEDRALCLVE IKKVKQSLSQ SHLPTPPDLN PFVFETVKGC
HLFSSGKIDN GTCICAAMAN KITILRHNES LNKFCIRKEI ETSEPCSCIH FTGYSIVIGT
NKFYEIETKQ YVLEEFLDKN DVTLASAVFA ASSHSFPISI IQVTTAPQND EYLLCFHEFG
VFVDAYGRRS RTDDIKWSRL PLSFAYREPY LFVTYFNSLD VIEILGHSSL GPHSYAHLDI
PNPRYLGPAI SSGAIYLASS YQNKLRVICC KGNLVQSQEG PLSLPRFLPN SPNKRGPPSY
NEHISKRLAA NPLVHGDPGT PHRYREARTE FRRDKSPSRP LEREKSPGRM LESRMVGSPG
RAMADPRLER SPGRVWDQSS V
//
