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Database: UniProt
Entry: A0A1S3WIF9_ERIEU
LinkDB: A0A1S3WIF9_ERIEU
Original site: A0A1S3WIF9_ERIEU 
ID   A0A1S3WIF9_ERIEU        Unreviewed;      2055 AA.
AC   A0A1S3WIF9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
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|RefSeq:XP_016046125.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016046125.1};
RN   [1] {ECO:0000313|RefSeq:XP_016046125.1}
RP   IDENTIFICATION.
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|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   RefSeq; XP_016046125.1; XM_016190639.1.
DR   GeneID; 103118398; -.
DR   CTD; 11113; -.
DR   OrthoDB; 3490126at2759; -.
DR   Proteomes; UP000079721; Unplaced.
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: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; 1.10.287.1490; -; 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   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; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
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..361
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          362..432
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          1391..1440
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1472..1592
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1620..1910
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          1319..1339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1351..1380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1933..2040
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          459..589
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          626..750
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          776..1241
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1979..2027
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   2055 AA;  234599 MW;  A3DF0A56BC0DB159 CRC64;
     MLKFKYGTRN PQDVGAAEPI TSRASRLNLF FQGKPPFMTQ QQVSPLSREG VLDALFVLFE
     ECSQPAMMKM KHVNNFVRKY SDTIAELQGL QPSAKDFEVR SLVGCGHFAE VQVVREKATG
     DIYAMKVMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKSNL YLVMEYQPGG
     DLLSLLNRYE DQLDENMIQF YLAELILAVH SIHQMGYVHR DIKPENILID RTGHLKLVDF
     GSAAKLNSNK MVTAKLPIGT PDYMAPEVLT VMNGDGKGAA YGPDCDWWSV GVITYEMIYG
     RTPFTEGTSA RTFNNIMNFQ RFLKFPDDPK VSSTLLDLIQ SLLCGQKERL KFEGLCCHPF
     FSKIDWNNIR NTPPPFVPTL KSDDDTSNFD EPEKNLWVSS SACQLSPSGF SGEELPFVGF
     SYSKALGILG RSESVVSGLD SPAKTSSMEK KLLIKSKELQ DSQDKCHKME QEMTRLHRRV
     SEVEAVLSQK EVELKASETQ RSLLEQDLAT YITECSSLKR SLEQARMEVS QEDDKALQLL
     HDIREQSRKL QEIKEQEYQA QVEEMRLMMN QLEEDLVSAR RRSDLYESEL RESRLAAEEF
     KRKATECQHK LVKAAKDPGK PEVGEYSKLE KINAEQQIKI QELQEKLEKA VKASTEAAEL
     LQNIRQAKER AERELEKLQN REDSSEGIKK KLVEAEERRH SLENKVKRLE TMERRENRLK
     DDIQTKSQQI QQMADKILEL EEKHREAQVS AQHLEVHLKQ KEQHYEEKIK VLDSQIKKDL
     ADKESLENLM QRHEEEAHEK GKILSEQKAM INAMDSKIRS LEQRIVELSE ANKLAANSSL
     FTQRNMKAQE EMISELRQQK FYLETQAGKL EAQNRKLEEQ LEKISHQDHS DKSRLLELET
     RLREVSLEHE EQKLELKRQL TELQLSLQER ESQLTALQSA RAALEGQLRQ AKTELEETTA
     EAEEEIQALT AHRDEIQRKF DALRNSCTVI TDLEEQLNQL TEDNAELNNQ NFYLSKQLDE
     ASGANDEIVQ LRSEVDHLRR EITEREMQLT SQKQTMEALK TTCTMLEEQV MDLEALNDEL
     LEKERQWEAW RSVLGDEKSQ FECRVRELQR MLDTEKQSRA RADQRITESR QVVELAVKEH
     KAEILALQQA LKEQKLKAES LSDKLNDLEK KHAMLEMNAR SLQQKLETER ELKQRLLEEQ
     AKLQQQMDLQ KSHIFRLTQG LQEALDRADL LKTERSDLEY QLENIQVLYS HEKVKMEGTI
     SQQTKLIDFL QAKMDQPAKK KKVPLQYNEL KAALEKEKAR CAELEEALQK TRIELRSARE
     EAAHRKATEH PHPSTPATAR QQIAMSAIVR SPEHQPSAMS LLAPPSGRRK ESSTPEEFSR
     RLKERMHHNI PHRFNVGLNM RATKCAVCLD TVHFGRQASK CLECQVMCHP KCSTCLPATC
     GLPAEYATHF TEAFCRDKMN SPGLQTKEPS SGLHLEGWMK VPRNNKRGQQ GWDRKYIVLE
     GSKVLIYDSE AREAGQRPVE EFELCLPDGD VSIHGAVGAS ELANTAKADV PYILKMESHP
     HTTCWPGRSL YLLAPSFPDK QRWVTALESV VAGGRVSREK AEADAKLLGN SLLKLEGDDR
     LDMNCTLPFS DQVVLVGTEE GLYALNVLKN SLTHVPGIGA VFQIYIIKDL EKLLMIAGEE
     RALCLVDVKK VKQSLAQSHL PAQPDISPNV FEAVKGCHLF AAGKIESGLC ICAATPSKVV
     ILRYNENLSK YCIRKEIETS EPCSCIHFTN YSVLIGTNKF YEIDMKQYTL EEFLDKNDHS
     LAPAVFASSS NSFLVSIVQV NGAGQREEYL LCFHEFGVFV DSYGRRSRTD DLKWSRLPLA
     FAYREPYLFV THFNSLEVIE IQARSSLGTP ARAYLEIPNP RYLGPAISSG AIYLASSYQD
     KLRIICCKGN LVKESGTDHH RGPSTSRSPN KRGPPTYNEH ITKRVASSPA PPEGPSHPRE
     PSTPHRYREG RTELRRDKSP GRPLEREKSP GRVLSTRRER SPGRLFEDSS RGRLPAGAVR
     TPLSQVNKVW DQSSV
//
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