ID H0VGZ3_CAVPO Unreviewed; 1368 AA.
AC H0VGZ3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568};
GN Name=ROCK1 {ECO:0000313|Ensembl:ENSCPOP00000009405.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000009405.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000009405.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000009405.3};
RG Ensembl;
RL Submitted (NOV-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|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 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: 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: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 EMBL; AAKN02020667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02020668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02020669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02020670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02020671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02020672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02020673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 10141.ENSCPOP00000009405; -.
DR Ensembl; ENSCPOT00000010568.3; ENSCPOP00000009405.3; ENSCPOG00000010474.4.
DR VEuPathDB; HostDB:ENSCPOG00000010474; -.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_0_1; -.
DR InParanoid; H0VGZ3; -.
DR OMA; XETLATQ; -.
DR TreeFam; TF313551; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000010474; Expressed in heart left ventricle and 12 other cell types or tissues.
DR GO; GO:0106003; C:amyloid-beta complex; IEA:Ensembl.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:Ensembl.
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:0072518; F:Rho-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0003383; P:apical constriction; IEA:Ensembl.
DR GO; GO:0032060; P:bleb assembly; IEA:Ensembl.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IEA:Ensembl.
DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl.
DR GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
DR GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0061157; P:mRNA destabilization; IEA:Ensembl.
DR GO; GO:0051451; P:myoblast migration; IEA:Ensembl.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; IEA:Ensembl.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IEA:Ensembl.
DR GO; GO:0140058; P:neuron projection arborization; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0090521; P:podocyte cell migration; IEA:Ensembl.
DR GO; GO:1900223; P:positive regulation of amyloid-beta clearance; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IEA:Ensembl.
DR GO; GO:1905205; P:positive regulation of connective tissue replacement; IEA:Ensembl.
DR GO; GO:0035306; P:positive regulation of dephosphorylation; IEA:Ensembl.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0110061; P:regulation of angiotensin-activated signaling pathway; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; IEA:Ensembl.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0045664; P:regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0090128; P:regulation of synapse maturation; IEA:Ensembl.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl.
DR GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
DR GO; GO:0071559; P:response to transforming growth factor beta; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR CDD; cd20874; C1_ROCK1; 1.
DR CDD; cd11639; HR1_ROCK1; 1.
DR CDD; cd01242; PH_ROCK; 1.
DR CDD; cd22250; ROCK_SBD; 1.
DR CDD; cd05622; STKc_ROCK1; 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; 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 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; SSF90257; Myosin rod fragments; 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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
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 479..556
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 949..1015
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1132..1331
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1242..1297
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 1333..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..898
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 938..979
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1020..1100
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1340..1368
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 1368 AA; 159915 MW; 0E984E124F05BF44 CRC64;
MSTGDSFETR FEKIDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK NIDNFLSRYK
DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSSRK VYAMKLLSKF EMIKRSDSAF
FWEERDIMAF ANSPWVVQLF YAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA
EVVLALDAIH SMGFIHRDVK PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY
ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP
DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFRN DQWAWETLRD TVAPVVPDLS
SDIDTSNFDD LEEDKGDEET FPIPKAFVGN QLPFVGFTYY SNRRHLSPAN PNDNRTSSNV
DKSVQESLQK TIYKLEEQLH NEMQLKDEME QKCRTSNIKL DKIMKELDEE GNQRRNLEST
VSQIEKEKML LQHRINEYQR KVEQENEKRR NVENEVSTLK DQLEDLKKVS QNSQLANEKL
AQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSVSQLES LNRELQERNR ILENSKSQAD
KDYYQLQAVL EAERRDRGHD SEMIGELQAR IISLQEEVKH LKHNLERVEG ERKEAQDMLN
HSEKEKNNLE IDLNYKLKSL QQRLEQEVNE HKVTKARLTD KHQSIEEAKS VAMCEMEKKL
KEERKTREKA ENRVVQIEKQ CSMLDVDLKQ AQQKLEHLTE NKERMEDEVK NLTLQLEQES
NKRLLLQNEL KTQAFEADNL KGLEKQMKQE INTVLEAKRL LEFELAQLTK QYRGNEGQMR
ELQDQLEAEQ YFSTLYKTQV KELKEELEEK NREHLKKIQE LQNEKEALST QLDLAETKAE
SEQLARGLLE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEEANSMLTK DNELLRKENE
ELMDKMKKAE EEYKLKKEEE ISNLKAAFEK NINTERTLKT QAVNKLAEIM NRKDFKIDRK
KANTQDLRKK EKENRKLQLE LNQEREKFNQ MVVKHQKELN EMQAQLVEEC THRNELQLQL
ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPVDS ACIPYLFIFY SCLLIEGWLS
VPNRGNIKRY GWKKQYVVVS SKKILFYNDE QDKEQSNPSM VLDIDKLFHV RPVTQGDVYR
AETEEIPKIF QILYANEGEC RKDVEMEPVQ QAEKTNFQNH KGHEFIPTLY HFPANCEACA
KPLWHVFKPP PALECRRCHV KCHRDHLDKK EDLISPCKVS YDITSARDML LLACSQDEQK
KWVTHLVKKI PKNPPSGFVR ASPRTLSTRS TANQSFRKVV KNTSGKTR
//
