ID M3WUL5_FELCA Unreviewed; 1361 AA.
AC M3WUL5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568};
GN Name=ROCK2 {ECO:0000313|Ensembl:ENSFCAP00000018052.4,
GN ECO:0000313|VGNC:VGNC:64715};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000018052.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000018052.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000018052.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000018052.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000018052.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000018052.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000018052.4};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton
CC and cell polarity. {ECO:0000256|PIRNR:PIRNR037568}.
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|PIRNR:PIRNR037568};
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|PIRNR:PIRNR037568};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR037568};
CC -!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-27632.
CC {ECO:0000256|PIRNR:PIRNR037568}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037568}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903,
CC ECO:0000256|PIRNR:PIRNR037568}.
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DR EMBL; AANG04003329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_019683462.1; XM_019827903.1.
DR Ensembl; ENSFCAT00000022114.4; ENSFCAP00000018052.4; ENSFCAG00000024216.4.
DR VGNC; VGNC:64715; ROCK2.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_0_1; -.
DR Proteomes; UP000011712; Chromosome A3.
DR Bgee; ENSFCAG00000024216; Expressed in embryonic head and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; 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:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:InterPro.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR CDD; cd20875; C1_ROCK2; 1.
DR CDD; cd11638; HR1_ROCK2; 1.
DR CDD; cd01242; PH_ROCK; 1.
DR CDD; cd22250; ROCK_SBD; 1.
DR CDD; cd05596; STKc_ROCK; 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; 1.20.5.730; Single helix bin; 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; IPR011072; HR1_rho-bd.
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; IPR020684; ROCK1/ROCK2.
DR InterPro; IPR037311; ROCK2_HR1.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF28; RHO-ASSOCIATED PROTEIN KINASE 2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR PIRSF; PIRSF037568; Rho_kinase; 1.
DR SMART; SM00109; C1; 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; SSF103652; G protein-binding 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; 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; PS51860; REM_1; 1.
DR PROSITE; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037568};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01207}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR037568};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR037568};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR037568};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR037568};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037568}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR037568};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037568};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 6..268
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 271..339
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 411..487
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 893..961
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1123..1322
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1233..1288
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 426..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 569..923
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 970..1015
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1336..1361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037568-1"
FT BINDING 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR037568-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1361 AA; 157810 MW; 450A23AD7C7C5256 CRC64;
MKAEDYDVVK VIGRGAFGEV QLVRHKASQK VYAMKLLSKF EMIKRSDSAF FWEERDIMAF
ANSPWVVQLF CAFQDDKYLY MVMEYMPGGD LVNLMSNYDV PEKWAKFYTA EVVLALDAIH
SMGLIHRDVK PDNMLLDKHG HLKLADFGTC MKMDETGMVH CDTAVGTPDY ISPEVLKSQG
GDGYYGRECD WWSVGVFLFE MLVGDTPFYA DSLVGTYSKI MDHKNSLCFP EDAEISKHAK
NLICAFLTDR EVRLGRNGVE EIKQHPFFKN DQWNWDNIRE TAAPVVPELS SDIDSSNFDD
IEDDKGDVET FPIPKAFVGN QLPFIGFTYY RENLLLSDSP SCRENDSIQS RKNEESQEIQ
KKLYTLEEHL STEIQAKEEL EQKCKSVNTR LEKVAKELEE EITLRKNVES ALRQLEREKA
LLQHKNAEYQ RKADHEADKK RNLENDVNSL KDQLEDLKKR NQNSQISTEK VNQLQRQLDE
TNALLRTESD TAARLRKTQA ESTKQIQQLE SNNRDLQDKN CLLETAKLKL EKDFINLQSV
LESERRDRTH GSEIINDLQG RISGLEEDLK NGKILLAKVE MEKRQLQERF TDLEKEKNNM
EIDMTYQLKV IQQSLEQEEA EHKATKARLA DKNKIYESIE EAKSEAMKEM EKNLSEERTL
KQKVENLLLE AEKRCSILDC DLKQSQQKIN ELLKQKDVLN EDIRNLTLKI EQETQKRCLT
QNDLKMQTQQ VNTLKMSEKQ LKQENNHLME MKMSLEKQNA ELRKERQDAD GQMKELQDQL
EAEQYFSTLY KTQVRELKEE CEEKTKLCKE LQQKKQEFED ERDSLAAQLE ITLTKADSEQ
LARSIAEEQY SDLEKEKIMK ELEIKEMMAR HKQELTEKDA TIASLEETNR TLTSDVANLA
NEKEELNNKL KDAQEQLSRL KDEEISAAAI KAQFEKQLLT ERTLKTQAVN KLAEIMNRKE
PVKRGSDTDV RRKEKENRKL HMELKSEREK LTQQMIKYQK ELNEMQAQIA EESQIRIELQ
MALDSKDSDI EQLRSQLQAL HIGLDSSSIG SGPGDAEADD GFPVHITQSR TMESLSFTYQ
RSSTSLNIAT KPSSSHMLLD SDSDSEEESL PYLPISSEPD GTESRLEGWL SLPVRNNTKK
FGWVKKYVIV SSKKILFYDS EQDKEQSNPY MVLDIDKLFH VRPVTQTDVY RADAKEIPRI
FQILYANEGE SKKEQEFPVE PVGEKSNYIC HKGHEFIPTL YHFPTNCEAC MKPLWHMFKP
PPALECRRCH IKCHKDHMDR KEEIIAPCKV YYDISTAKNL LLLANSTEEQ QKWVSRLVKK
IPKKPPAPDP FARSSPRTSM KIQQNQSIRR PSRQLAPNKP S
//
