ID A0A3P9NJ93_POERE Unreviewed; 1263 AA.
AC A0A3P9NJ93;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Rho-associated protein kinase 1 {ECO:0000256|ARBA:ARBA00044069};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase 1 {ECO:0000256|ARBA:ARBA00044327};
DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase I {ECO:0000256|ARBA:ARBA00044326};
DE AltName: Full=p160 ROCK-1 {ECO:0000256|ARBA:ARBA00044332};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000009624.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000009624.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000009624.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:ARBA00001127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000256|ARBA:ARBA00001127};
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:ARBA00001416};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000256|ARBA:ARBA00001416};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cell projection, bleb {ECO:0000256|ARBA:ARBA00043945}. Cell projection,
CC ruffle {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000256|ARBA:ARBA00004114}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR STRING; 8081.ENSPREP00000009624; -.
DR Ensembl; ENSPRET00000009740.1; ENSPREP00000009624.1; ENSPREG00000006471.1.
DR GeneTree; ENSGT01030000234517; -.
DR OMA; XETLATQ; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000006471; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0005856; C:cytoskeleton; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR CDD; cd11639; HR1_ROCK1; 1.
DR CDD; cd22250; ROCK_SBD; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR037310; ROCK1_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:SF33; RHO-ASSOCIATED PROTEIN KINASE 1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF103652; G protein-binding domain; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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|PROSITE-
KW ProRule:PRU10141}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01207}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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..402
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 442..526
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 879..945
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1137..1192
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 1220..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 395..667
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 777..818
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 868..909
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 951..1038
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1230..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1263 AA; 146603 MW; 4951C9FEDA5F0131 CRC64;
MSAGDAMAAR FEKIDAMLQD PKSEINTDCL LDGLDALVYD LDFPALRKNK SIDNFLNRYK
KTISKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTCK VYAMKLLSKF EMIKRSDSAF
FWEERDIMAF ANSPWVVQLF FAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA
EVVLALDGIH SMGFIHRDVK PDNMLLDKAG HLKLADFGTC MKMNEDGMVQ CDTAVGTPDY
ISPEVLKSQG GNGNYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNALTFP
DDSDISNDAK NLICAFLTDR EVRLGRNGVD EIKRHPFFKN DQWTWDNIRE TAAPVVPELS
SDVDTSNFDD IEEDRGEEET FPIPKAFVGN QLPFLENLQK QIYQLEEQLH GEMQQKDELE
QKCRASNTKI EKIMKELDEE ANLRKSAEAS VSLLEKDKIM LQHRFTEYQR KADQEGEKRR
NLENEVSNLK EQLEDMRKIS QNSQASNDKI VQLQKQLEEA NDLLRAESDT AARLRKSHTE
MTKSMSQLET LNRELQERSR AADGEKAQLE KELLLLQSTL ESERRNYSEG SEEMRELQAR
LAGLQEDNRN LKINLSKVEG ERKQAQERSN YLEKEKNSLE IDLNYKLKTL QQRLEQEQTE
HRVTRAQLTD KYESIEEAKS AAMIGMPQKM SEETGARSRA EGRVVEVEKQ CSMLEFDLKQ
SVQKMEQLMK QKERLEDEVS KXLIYMGVFI CFDRQYRGNE GQMRELQDQL EAEQYFSTLY
KTQVRELKEE IEERNRQVQD AQKKVHDLIS ERESLSAQLD LTVTKAESEQ LARALQEEQY
FELTQESKKA TARHKQEIGE REATIAQVSL LEESNKTLTK DVEHLSKDNT ELSEKLRLQE
EEYLSQKEDI MASVKANYEK VLQTERTLKT QAVNKLAEIM NRKDMKLDQK KKGSTAELRK
KEKENRKLQQ ELNQEKEKFN HMAIKYQKEV NEMQAQLAEE STYRNELQMQ LASKESDIEQ
LREKLSDLQQ RVENSSITSL QTDETDSNTA VFAWYSVYTK KYCYTVVCSN FCNFLFFFPS
KLFHVRPVTQ GDVYRAETEE IPRIFQILYA NEGECRKEAD MEPVPQGEKT NCLAHKGHEF
IPTLYHFPSN CEACAKPLWH VFKPPPALEC RRCHVKCHRD HLDKKEDVIA PCKVNYDVTS
ARDMLLLAVT QEDQKKWIGH LGKKIPKTPP STFSRVSPRS MSTRSGPNQS FRKNPKSNTA
KLR
//
