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Rho-associated protein kinase 1 (EC 2.7.11.1) (Liver regeneration-related protein LRRG199) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p150 RhoA-binding kinase ROK beta) (p160 ROCK-1) (p160ROCK)

 ROCK1_RAT               Reviewed;        1369 AA.
Q63644; Q7TP31;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
20-DEC-2017, entry version 165.
RecName: Full=Rho-associated protein kinase 1;
EC=2.7.11.1;
AltName: Full=Liver regeneration-related protein LRRG199;
AltName: Full=Rho-associated, coiled-coil-containing protein kinase 1;
AltName: Full=Rho-associated, coiled-coil-containing protein kinase I;
Short=ROCK-I;
AltName: Full=p150 RhoA-binding kinase ROK beta;
AltName: Full=p160 ROCK-1;
Short=p160ROCK;
Name=Rock1; ORFNames=Ac2-154;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RHOA; RHOB
AND RHOC, AND TISSUE SPECIFICITY.
TISSUE=Brain, and Liver;
PubMed=8816443; DOI=10.1128/MCB.16.10.5313;
Leung T., Chen X.-Q., Manser E., Lim L.;
"The p160 RhoA-binding kinase ROK alpha is a member of a kinase family
and is involved in the reorganization of the cytoskeleton.";
Mol. Cell. Biol. 16:5313-5327(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Liver;
Xu C.S., Li W.Q., Li Y.C., Yang K.J., Yan H.M., Chang C.F., Zhao L.F.,
Ma H., Wang L., Wang S.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
"Liver regeneration after PH.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, ROLE IN SMOOTH MUSCLE CONTRACTION AND HYPERTENSION, AND
INHIBITION BY Y-27632.
PubMed=9353125; DOI=10.1038/40187;
Uehata M., Ishizaki T., Satoh H., Ono T., Kawahara T., Morishita T.,
Tamakawa H., Yamagami K., Inui J., Maekawa M., Narumiya S.;
"Calcium sensitization of smooth muscle mediated by a Rho-associated
protein kinase in hypertension.";
Nature 389:990-994(1997).
[4]
FUNCTION, INTERACTION WITH PPP1R12A, AND SUBCELLULAR LOCATION.
PubMed=19131646; DOI=10.1161/CIRCRESAHA.108.188524;
Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X.,
Surks H.K.;
"ROCK isoform regulation of myosin phosphatase and contractility in
vascular smooth muscle cells.";
Circ. Res. 104:531-540(2009).
-!- FUNCTION: Protein kinase which is a key regulator of actin
cytoskeleton and cell polarity. Involved in regulation of smooth
muscle contraction, actin cytoskeleton organization, stress fiber
and focal adhesion formation, neurite retraction, cell adhesion
and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2,
MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts
synergistically with it to promote SRC-dependent non-apoptotic
plasma membrane blebbing. Phosphorylates JIP3 and regulates the
recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a
suppressor of inflammatory cell migration by regulating PTEN
phosphorylation and stability. Acts as a negative regulator of
VEGF-induced angiogenic endothelial cell activation. Required for
centrosome positioning and centrosome-dependent exit from mitosis.
Plays a role in terminal erythroid differentiation. May regulate
closure of the eyelids and ventral body wall by inducing the
assembly of actomyosin bundles. Promotes keratinocyte terminal
differentiation. Involved in osteoblast compaction through the
fibronectin fibrillogenesis cell-mediated matrix assembly process,
essential for osteoblast mineralization (By similarity).
{ECO:0000250, ECO:0000269|PubMed:19131646,
ECO:0000269|PubMed:9353125}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by RHOA binding. Inhibited by Y-
27632.
-!- SUBUNIT: Homodimer (By similarity). Interacts with GEM, MYLC2B,
RHOE, LIMK1, LIMK2, TSG101, CHORDC1, DAPK3, PFN1, PTEN and JIP3
(By similarity). Interacts with FHOD1 in a Src-dependent manner
(By similarity). Interacts with ITGB1BP1 (via N-terminus and PTB
domain) (By similarity). Interacts with RHOA (activated by GTP),
RHOB, RHOC and PPP1R12A. {ECO:0000250,
ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:8816443}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19131646}.
Cytoplasm, cytoskeleton, microtubule organizing center,
centrosome, centriole {ECO:0000269|PubMed:19131646}. Golgi
apparatus membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Cell projection, bleb {ECO:0000250}. Cytoplasm,
cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Cell
projection, lamellipodium {ECO:0000250}. Cell projection, ruffle
{ECO:0000250}. Note=Associated with the mother centriole and an
intercentriolar linker. A small proportion is associated with
Golgi membranes. Colocalizes with ITGB1BP1 and ITGB1 at the cell
membrane predominantly in lamellipodia and membrane ruffles, but
also in retraction fibers. Localizes at the cell membrane in an
ITGB1BP1-dependent manner (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q63644-1; Sequence=Displayed;
Name=2;
IsoId=Q63644-2; Sequence=VSP_010449, VSP_010450;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in brain, spleen, lung,
liver, skeletal muscle, kidney and testis.
{ECO:0000269|PubMed:8816443}.
-!- DOMAIN: The C-terminal auto-inhibitory domain interferes with
kinase activity. RHOA binding leads to a conformation change and
activation of the kinase. Truncated ROCK1 is constitutively
activated.
-!- PTM: Autophosphorylated on serine and threonine residues.
-!- PTM: Cleaved by caspase-3 during apoptosis. This leads to
constitutive activation of the kinase and membrane blebbing (By
similarity). {ECO:0000250}.
-!- DISEASE: Note=May play a role in hypertension. Rock1-inhibitors
lower the blood pressure in spontaneous hypertensive, renal
hypertensive and deoxycorticosterone acetate-induced hypertensive
rats, but not in normal rats.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U61266; AAB37571.1; -; mRNA.
EMBL; AY325220; AAP92621.1; -; mRNA.
RefSeq; NP_112360.1; NM_031098.1. [Q63644-1]
UniGene; Rn.89756; -.
ProteinModelPortal; Q63644; -.
SMR; Q63644; -.
CORUM; Q63644; -.
IntAct; Q63644; 1.
STRING; 10116.ENSRNOP00000047378; -.
BindingDB; Q63644; -.
ChEMBL; CHEMBL5509; -.
iPTMnet; Q63644; -.
PhosphoSitePlus; Q63644; -.
PaxDb; Q63644; -.
PeptideAtlas; Q63644; -.
PRIDE; Q63644; -.
GeneID; 81762; -.
KEGG; rno:81762; -.
UCSC; RGD:620424; rat. [Q63644-1]
CTD; 6093; -.
RGD; 620424; Rock1.
eggNOG; KOG0612; Eukaryota.
eggNOG; ENOG410XR1Q; LUCA.
HOGENOM; HOG000017259; -.
HOVERGEN; HBG053111; -.
InParanoid; Q63644; -.
KO; K04514; -.
PhylomeDB; Q63644; -.
SABIO-RK; Q63644; -.
PRO; PR:Q63644; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0017049; F:GTP-Rho binding; IMP:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
GO; GO:0003383; P:apical constriction; ISO:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0032060; P:bleb assembly; ISO:RGD.
GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:RGD.
GO; GO:0007010; P:cytoskeleton organization; IMP:RGD.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
GO; GO:0050900; P:leukocyte migration; ISO:RGD.
GO; GO:0050901; P:leukocyte tethering or rolling; ISO:RGD.
GO; GO:0022614; P:membrane to membrane docking; ISO:RGD.
GO; GO:0051451; P:myoblast migration; ISS:UniProtKB.
GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; ISO:RGD.
GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; ISO:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
GO; GO:0032970; P:regulation of actin filament-based process; ISO:RGD.
GO; GO:2000114; P:regulation of establishment of cell polarity; IEA:InterPro.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:RGD.
GO; GO:0045616; P:regulation of keratinocyte differentiation; ISO:RGD.
GO; GO:0051492; P:regulation of stress fiber assembly; IEA:InterPro.
GO; GO:0007266; P:Rho protein signal transduction; IMP:MGI.
CDD; cd00029; C1; 1.
CDD; cd11639; HR1_ROCK1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR015008; Rho-bd_dom.
InterPro; IPR029876; ROCK1.
InterPro; IPR020684; ROCK1/ROCK2.
InterPro; IPR037310; ROCK1_HR1.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR22988:SF33; PTHR22988:SF33; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF08912; Rho_Binding; 1.
PIRSF; PIRSF037568; Rho_kinase; 1.
SMART; SM00109; C1; 1.
SMART; SM00233; PH; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF50729; SSF50729; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; ATP-binding;
Cell membrane; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Golgi apparatus; Kinase; Magnesium; Membrane;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q13464}.
CHAIN 2 1369 Rho-associated protein kinase 1.
/FTId=PRO_0000086623.
DOMAIN 76 338 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 341 409 AGC-kinase C-terminal.
REPEAT 458 542 REM.
DOMAIN 1133 1332 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
NP_BIND 82 90 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 1243 1298 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 368 727 Interaction with FHOD1. {ECO:0000250}.
REGION 998 1010 RHOA binding. {ECO:0000250}.
REGION 1115 1369 Auto-inhibitory. {ECO:0000250}.
COILED 422 613 {ECO:0000255}.
COILED 1011 1102 {ECO:0000255}.
COMPBIAS 636 980 Glu-rich.
ACT_SITE 198 198 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 105 105 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 1113 1114 Cleavage; by caspase-3. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q13464}.
MOD_RES 1105 1105 Phosphoserine.
{ECO:0000250|UniProtKB:Q13464}.
MOD_RES 1108 1108 Phosphoserine.
{ECO:0000250|UniProtKB:P70335}.
MOD_RES 1343 1343 Phosphoserine.
{ECO:0000250|UniProtKB:Q13464}.
VAR_SEQ 1 488 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_010449.
VAR_SEQ 1369 1369 S -> RLMPSSPCRVGVGIDKWRSHRDRKREGLLTEDVPGS
RLEKKLGRIGRAARRNKDGADIQPCLDINDLLCMCRLVPLL
GLPLVVTSGTAHVQFMHQVLVDR (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_010450.
CONFLICT 1118 1133 VGSACIPYLFIFYSSS -> E (in Ref. 2;
AAP92621). {ECO:0000305}.
CONFLICT 1283 1283 S -> C (in Ref. 2; AAP92621).
{ECO:0000305}.
CONFLICT 1296 1296 P -> S (in Ref. 2; AAP92621).
{ECO:0000305}.
CONFLICT 1316 1316 P -> S (in Ref. 2; AAP92621).
{ECO:0000305}.
CONFLICT 1334 1335 KA -> NP (in Ref. 2; AAP92621).
{ECO:0000305}.
SEQUENCE 1369 AA; 159626 MW; E29B9456D348C9D0 CRC64;
MSTGDSFETR FEKIDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK NIDNFLSRYK
DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK VYAMKLLSKF EMIKRSDSAF
FWEERDIMAF ANSPWVVQLF YAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA
EVVLALDAIH SMGFIHRDVK PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY
ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP
DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD TVAPVVPDLS
SDIDTSNFDD LEEDKGDEET FPIPKAFVGN QLPFVGFTYY SNRRYLPSAN PSENRSSSNV
DKNVQESLQK TIYKLEEQLH NEMQLKDEME QKCRTSNIKL DKIMKELDEE GNQRRNLESA
VSQIEKEKML LQHRINEYQR KVEQENEKRR NVENEVSTLK DQLEDLRKAS QSSQLANEKL
TQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSVSQLES LNRELQERNR MLENSKSQAD
KDYYQLQAVL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLERVEG ERKEAQDMLN
HSEKEKNNLE IDLNYKLKSI QQRLEQEVNE HKVTKARLTD KHQSIEEAKS VAMCEMEKKL
KEEREAREKA ENRVVETEKQ CSMLDVDLKQ SQQKLEHLTE NKERLEDAVK SLTLQLEQES
NKRILLQSEL KTQAFEADNL KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR
ELQDQLEAEQ YFSTLYKTQV KELKEEIEEK NRENLRKIQE LQSEKETLST QLDLAETKAE
SEQLARGILE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEEANNALTK DIELLRKENE
ELNERMRTAE EEYKLKKEEE ISNLKAAFEK NISTERTLKT QAVNKLAEIM NRKDFKIDRK
KANTQDLRKK EKENRKLQLE LNQEREKFNQ MVVKHQKELN DMQAQLVEEC THRNELQMQL
ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPVGS ACIPYLFIFY SSSSRIEGWL
SVPNRGNIKR YGWKKQYVVV SSKKMLFYND EQDKEQSSPS MVLDIDKLFH VRPVTQGDVY
RAETEEIPKI FQILYANEGE CRKDIEVEPV QQGEKTNFQN HKGHEFIPTL YHFPANCEAC
AKPLWHVFKP PPALECRRCH VKSHRDHLDK KEDLIPPCKV SYDVTSARDM LLLACPQDEQ
KKWVTHLVKK IPKKAPSGFV RASPRTLSTR STANQSFRKV VKNTSGKTS


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