ID   A0A3Q4GH06_NEOBR        Unreviewed;      1361 AA.
AC   A0A3Q4GH06;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   28-JUN-2023, entry version 22.
DE   RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000008196.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000008196.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-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}.
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   STRING; 32507.XP_006792165.1; -.
DR   Ensembl; ENSNBRT00000008431.1; ENSNBRP00000008196.1; ENSNBRG00000006322.1.
DR   GeneTree; ENSGT01030000234517; -.
DR   OMA; XETLATQ; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000006322; Expressed in blood and 9 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0003347; P:epicardial cell to mesenchymal cell transition; IEA:Ensembl.
DR   GO; GO:1903392; P:negative regulation of adherens junction organization; IEA:Ensembl.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR   CDD; cd20874; C1_ROCK1; 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); 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; 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:SF73; RHO-ASSOCIATED PROTEIN KINASE; 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   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|PIRNR:PIRNR037568};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR037568};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR037568};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
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          76..338
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          341..409
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          473..557
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          953..1019
FT                   /note="RhoBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51859"
FT   DOMAIN          1125..1324
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1235..1290
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          557..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1020..1039
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          749..790
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          826..895
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          928..976
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        557..574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1328..1361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037568-1"
FT   BINDING         105
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;  158647 MW;  0DDF7609A6E81E38 CRC64;
     MSAGDTMEAR FEKIDAMLKD PKSEINTDCL LDGLDALVYD LDFPALRKNK SIDNFLNRYK
     ETISKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKATSK VYAMKLLSKF EMIKRSDSAF
     FWEERDIMAF ANSSWVVQLF FAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA
     EVVLALDGIH SMGFIHRDVK PDNMLLDKAG HLKLADFGTC MKMNKDGMVR CDTAVGTPDY
     ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNALTFP
     DDSDISNDAK NLICAFLTDR EVRLGRNGVD EIKRHPFFKN DQWTWDNIRE TAAPVVPELS
     SDTDTSNFDD IEEDRGEEET FPIPKAFVGN QLPFVGFTYY SNQQSLTRWM SATLSDQLKW
     NVSVQLENLQ KRIYQLEEQL HSEMQLKDEL EQKCRTSNNK IEKIMKELDE EANLRKSAEA
     SLSLLEKDKL MQQHRFTEYQ RKADQESEKR RNLENEVSNL KEQLEDMKKI SQNSQASNDK
     ITQLQNQLEE ANDLLRAESD TAGRLRKSHT EMTKSMAHLE NLNRELQERS RAVEGEKAQL
     EKELLLLQST LDSERRNYSQ DSEEIRELQA RLSGLQEDNK NLKLSLSKME AERKQAQERS
     NNLEKEKNNL EIDLNYKLKT LQQRLEQEQT EHRVTRAQLT DKYESIEEAK SAAMSGMSQK
     MSEETGARMR AESRVVEVEK QCSMLEFDLK QSVQKMEQLM KQKERLEDEV KNLQIQVEQE
     SSKRIQIQND LKTRMQEMDR LRCSEKQLKQ EINTSLESKR SLEFQLAQLS KQYRGNEGQM
     RELQDQLEAE QYFSTLYKTQ VKELKEEIEE RNRQIQEANK KVQDLCNERD SLSAQLDLTV
     TKAESEQLAR ALQEEQYFEL SQENKKAVTR HKQEIGEKEA TIARLEESYK TLTKDVENLS
     REKTDLSEKL RIQDEEYVAQ KEEIEKSIKA NYEKILYTER TLKTQAVNKL AEIMNRKDMK
     LDQKKKGSTA DLRKKEKENR KLQLELNQEK EKFNHMAIKY QKELSEMQAQ LAEESTYRNE
     LQMQLDSKES DIEQLREKLN DLQQRMDNSS VTSLQTDETD SNIAESRLEG WLSIPNRANI
     KRYGWKKQYV VVSSKKILFY NDEQDKEQSN PSMVLDIDKL FHVRPVTQGD VYRAETDEIP
     RIFQILYANE GECRKEADLE TVPQGDKTNC LPHKGHEFIP TLYHFPSNCE ACAKPLWHVF
     KPPPALECRR CHVKCHKDHL DKKEDVIAPC KVNYDVTSAR DMLLLALTQD EQKKWIGHLG
     KKIPKTPPST FTRASPRSMS TRSGPNQSFR KNPKSNTGKL R
//