ID A0A2D0QD00_ICTPU Unreviewed; 2092 AA.
AC A0A2D0QD00;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Citron Rho-interacting kinase {ECO:0000256|PIRNR:PIRNR038145};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038145};
GN Name=cita {ECO:0000313|RefSeq:XP_017316174.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017316174.1};
RN [1] {ECO:0000313|RefSeq:XP_017316174.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017316174.1};
RG RefSeq;
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 RefSeq; XP_017316174.1; XM_017460685.3.
DR STRING; 7998.ENSIPUP00000016870; -.
DR GeneID; 108260404; -.
DR KEGG; ipu:108260404; -.
DR CTD; 100329792; -.
DR OrthoDB; 3490126at2759; -.
DR Proteomes; UP000221080; Chromosome 28.
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:0048513; P:animal organ development; IEA:UniProt.
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; 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|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 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 98..362
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 363..434
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1420..1469
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1501..1621
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1649..1939
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 382..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1963..2092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 447..840
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 865..1208
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1315..1356
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 385..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1963..1984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2012..2068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2074..2092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2092 AA; 238801 MW; E1972463B6B270B4 CRC64;
MLKFKYGGHG SVKDLASVEP ITSRCSRLNQ LLQGKSSAYG LAGGSELKRE TLLDALLLLY
QECSSPELMK IKHVARFVHK FSDVVAELQQ LQPSKKDFEV RGVVGRGRFA EVQVVKERAT
GDVFAMKMMD KDCLRTQDNV AFYEEERAIL ALSTSPWIPQ LQHAFQDQDN VYLVMEYLPG
GDLMALLNRY EDQFDESMAQ FYLAELVQAI HTVHQMGYVH RDVKPENVLI DRTGHIKLAD
FGSASKLTTN KSVGSSKLPV GTQDFLAPEV LSALSGGSQC SYGPECDWWS LGVIAYEMIY
MKSPFTEGTS AKTINNIMNF QRYLKFPEDP KASSQFVDLV QSLLCMARER LGYEGLRSHP
FFSSVDWGGL RHAVPPFVPS LRAEDDTSNF EEPERAPRRA HAAQREPPCP GFQGQDLPFL
GWFFSRALTA LAKSESVAAG LNSPAKSNSM EKKLQLKSKE LQDTQDKCHK MEQEISRFQR
KMTDLESVLQ QKDVELKASE TQRSILEQDL ATYITECSSL KRSLEQARVE VSQEDDKALQ
LLHDIREQSN KLQEIKEQEY HAQLEEMQVT IRQLEEDLSA ARRRSDLYEA ELRDSRQTSE
ELKRKAADYQ QRIQKAKEQG KTEAEELLTK LEKTNAEQQL KIQELQDKLS KAVKASTEAT
ELLQNIRQAK ERLERDLERL RSKTDPSDTL RRRLRETEEG RKTLENQVKR LEIVERRENK
LKDDIQTKSQ QIQQMAEKIL ELEDNLRETQ ATAQRMEAHL VQKERLYEDK IKVLEAQMKA
DLADKDVLEA KRAQHEEEVR EKGKLLSEQK ATINAMENKM KSLEQRIAEL SEANKLAANS
SIYTQKNMKA QEEMISELRQ QKFYLESQAG KLEAQNAKLE EHLEKMSQQE QCKKSRLIEL
ETRLREMGLE HEEQKLELKR QVTELTLSLQ ERESQISSLQ AARHALESQL QQAKTELEET
TAEAEEEITA LRAHRDEIQR KFDALRDSCS VITDLEEQLT QLTQENAELN RQNFYLSKQL
DEVTDESEER LQLSQDVERL RREVADREMH LNNQKQNIET LKTTCSMLEE QVVELETLND
ELLEKERQWE NWRSALEDEK EQAERRTRDL QRLLDNEKQN RLRADQRSTE SRQAVELAVR
EHKAEILALQ QALKEQRLKA ESLSDTLNDL EKKHAMLEMN ARSLQQKLET ERELKQRLME
EQGKLQQQMD LQKTHIFRLT QGLQEALDQT DLLKTERTDL EYQLENIQAV YSHEKVKMEG
TISQQTKLID FLQAKMDQPI KKKKGIFGRR REDMVAAGNG AAGMAQGQPA VPMQYSDMKA
ALDKERARCT ELEEALQKMR IELRSLREEA AHFKTQEHVA PSTPASARHQ LLMSAIVKSP
ERQPNPSSLL NPASSARRKE TSTPEEYGRR VKERMHHNIP HRFTVGLNMR AAKCAVCLDT
VHFGRQAATC LECHTLCHPK CSPCLPATCG LPPEYATHFS EALCRDKANS PALQVKEASG
HVRLEGWMKQ PRNGKRGQQG WESKYVVLDG TKVSIYESEP REDSVKPQEE FELCLPDGDV
TVHGAVGASE LINTAKSDIP YVLKLESHPH TTCWPGQSLY FMAPSFPDKQ RWVAVLESVV
AGSRSSREKS ESDAKLLGNS LLKLEGDDRL DINCTLPLTD QIVMVGSEEG LYALNVIKNS
LTHVPGLTSV FQIQILKELD KLLMITGEER ALCLVEIKRV KQSLSQSHLP AQPELCPYIF
EAVKGCHLFA SGKIENGMCI CAAMPNKITI LRYNESLSKF CIRKEIETSE PCSCIHFTGY
SIIIGTNKFY EIEMKQYVLE EFLDKNDVTL ASAVFAASSH SFPISIIQVS CAPQKDEYLL
CFHEFGVFVD AYGRRSRSDD IKWSRLPLSF AYREPYLFVT YFNSLDVIEV QSHSALGPHT
YAHLDIPSPR YLGPAISSGA VYLASSYQNK LRVICCKGNL VQESSSSEPQ RSGSTRSPNK
RGPPSYNEHI SKRLAAGPVP QDSMQQVATP RRYREARTEF RRDASPSGPL EREKSPGRLV
DRGMDTRLER SPARVMELRR ERSPGRAFER LHTGSSRTPI NGVNKVWDQS SV
//
