ID A0A3B3BW45_ORYME Unreviewed; 1383 AA.
AC A0A3B3BW45;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568};
GN ORFNames=FQA47_010372 {ECO:0000313|EMBL:KAF6729050.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000009022.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000009022.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|EMBL:KAF6729050.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bigg-433 {ECO:0000313|EMBL:KAF6729050.1};
RX PubMed=32938378;
RA Liang P., Saqib H.S.A., Ni X., Shen Y.;
RT "Long-read sequencing and de novo genome assembly of marine medaka (Oryzias
RT melastigma).";
RL BMC Genomics 21:0-0(0).
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|ARBA:ARBA00001433,
CC 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|ARBA:ARBA00000775,
CC 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 Nucleus {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; WKFB01000267; KAF6729050.1; -; Genomic_DNA.
DR STRING; 30732.ENSOMEP00000009022; -.
DR PaxDb; 30732-ENSOMEP00000009022; -.
DR Ensembl; ENSOMET00000001473.1; ENSOMEP00000009022.1; ENSOMEG00000010220.1.
DR GeneTree; ENSGT01030000234517; -.
DR OMA; NSQWIVQ; -.
DR Proteomes; UP000261560; Unplaced.
DR Proteomes; UP000646548; Unassembled WGS sequence.
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-KW.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0060775; P:planar cell polarity pathway involved in gastrula mediolateral intercalation; IEA:Ensembl.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:InterPro.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
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 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); 2.
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; 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; 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; PF00433; Pkinase_C; 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; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01206}; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000646548};
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 84..346
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 347..417
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 968..1036
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1143..1344
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1255..1310
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 644..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..87
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 648..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037568-1"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR037568-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1383 AA; 160360 MW; 314C76FD9FB37330 CRC64;
MSGSAAMSAG AEKRMETRLK KLEDMLKDPK SALNLESLLD SLNALVLDLD YPALRKNKNI
ETFLNRYEKV TEELRDLQMK SEDFEKVKVI GRGAFGEVQL VRHKASQKVY AMKLLSKFEM
IKRSDSAFFW EERGIMAFAN SPWVVQLCCA FQDEHYLYMV MEYMPGGDLV NLTSTYDVPE
KWAKFYTAEV VMALDAIHSM GFIHRDVKPD NMLLDRHGHL KLADFGTCMK MDATGMVRCD
TAVGTPDYIS PEVLKSQGGD GCYGRECDWW SVGVFIFEML VGDTPFYADS LVGTYSKIMD
HKNSLHFPEE VEISADAKNI ICAFLTDREV RLGRNGVEEI KRHPFFKNDQ WTFDNVRETV
APVVPELSSD IDTSNFDEIE DDKGDVETFP TPKAFVGNQL PFVGFTYFKE DQLLNASNNS
SVNNENLKGE SVALQKKLRH LELQFNNDKQ ARDDLEQKYR TAASRLEKVT KELEEEVNCR
KGLESNLRQL EREKALLQHK SLESHRKAES EADRKRCLEN EVNGLRDQLD DLKRRNQNSH
ISNEKNIHLR RQLEEANALL RAETEAATRL RKTQTENSKQ LQQLEANVRE LQDKCCLLER
SKLSLEKECI SLQAALETER REQSQGSETI SDLMGRISAL EQEARQQRQA LSKAETEKRQ
LQDKLTDLEK EMSSKEIDLT YKLKVLQQEL EQEETSHKAT RALLADKSKI KVTIEGAKSE
SMKEMEQKLS EERSAKLRLE NRILELEKHS SMMDCDYKQA LQKLEELRRH KDHLTEEVKN
LTLKIEQETQ KRNLTQNDLK AQNQQLSILR ASEKQLKQET NHLLDIKRSL EKQNQELRKE
RQDTDGQMKE LQDQLEAEQY FSTLYKTQVR ELKEDCEERN KLYKEIQQSL QELQEERDSL
AAQLEITLTK ADSEQLARSI AEEQYSDLEK EKIMKELELK EMMARHRQEL NEKDITISSL
EEANRTLTSD VANLANEKEE LNNKLKEALE ESEKSKDWEQ QISQMKQGFE KQLQSERTLK
TQAVNKLAEI MNRKEIRGGG SRRGNDTDMR RKEKENRKLQ LELRSEKEKL NSIMIKYQRE
INEMQAQLSD ESQMRIELQM ALDSKDSDIE QLRNLLQTLS VQSMDSASVS SGPEFDTDDA
YTETRLEGWL SLPVRNNTKK FGWERKYVVV SSKKILFYNS EQDREQSIPY MVLDIDKLFH
VRPVTQTDVY RADAKEIPRI FQILYANEGE SKKEPEFPVE PLPIGEKSSY ICHKGHEFIP
TLYHFPTNCE ACTKPLWNMF KPPPALECRR CHIKCHKDHM DKKEEIIAPC KVNYDVSAAK
NLLLLAASQE EQQKWVSRLV KKIPKKPPPA EQFARSSPRA SMKVQASQSM RRPSRQLPTT
KSS
//
