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Rho-associated protein kinase 1 (EC 2.7.11.1) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK) (Fragment)

 ROCK1_PANTR             Reviewed;        1003 AA.
P61584;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
24-MAY-2004, sequence version 1.
12-SEP-2018, entry version 118.
RecName: Full=Rho-associated protein kinase 1;
EC=2.7.11.1;
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=p160 ROCK-1;
Short=p160ROCK;
Flags: Fragment;
Name=ROCK1;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=14962675; DOI=10.1016/j.ygeno.2003.08.017;
Dennehey B.K., Gutches D.G., McConkey E.H., Krauter K.S.;
"Inversion, duplication, and changes in gene context are associated
with human chromosome 18 evolution.";
Genomics 83:493-501(2004).
-!- 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}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-
27632 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with RHOA (activated
by GTP), RHOB, RHOC, GEM, MYLC2B, RHOE, PPP1R12A, LIMK1, LIMK2,
TSG101, CHORDC1, DAPK3, PFN1, PTEN and JIP3. Interacts with
ITGB1BP1 (via N-terminus and PTB domain) (By similarity).
Interacts with FHOD1 in a Src-dependent manner (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriole. 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}.
-!- 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}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY191612; AAP23262.1; -; Genomic_DNA.
ProteinModelPortal; P61584; -.
SMR; P61584; -.
STRING; 9598.ENSPTRP00000016847; -.
PaxDb; P61584; -.
PRIDE; P61584; -.
eggNOG; KOG0612; Eukaryota.
eggNOG; ENOG410XR1Q; LUCA.
HOGENOM; HOG000017259; -.
HOVERGEN; HBG053111; -.
InParanoid; P61584; -.
Proteomes; UP000002277; 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; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0051451; P:myoblast migration; ISS:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; IEA:InterPro.
GO; GO:0051492; P:regulation of stress fiber assembly; IEA:InterPro.
GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
CDD; cd00029; C1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR015008; Rho-bd_dom.
InterPro; IPR029876; ROCK1.
PANTHER; PTHR22988:SF33; PTHR22988:SF33; 1.
Pfam; PF08912; Rho_Binding; 1.
SMART; SM00109; C1; 1.
SMART; SM00233; PH; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS51860; REM_1; 1.
PROSITE; PS51859; RHO_BD; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
3: Inferred from homology;
Acetylation; 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.
CHAIN <1 1003 Rho-associated protein kinase 1.
/FTId=PRO_0000086621.
DOMAIN <1 58 AGC-kinase C-terminal.
DOMAIN 128 205 REM-1. {ECO:0000255|PROSITE-
ProRule:PRU01207}.
DOMAIN 598 664 RhoBD. {ECO:0000255|PROSITE-
ProRule:PRU01206}.
DOMAIN 767 966 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
ZN_FING 877 930 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 17 376 Interaction with FHOD1. {ECO:0000250}.
REGION 647 659 RHOA binding. {ECO:0000250}.
REGION 764 1003 Auto-inhibitory. {ECO:0000250}.
COILED 71 341 {ECO:0000255}.
COILED 660 751 {ECO:0000255}.
COMPBIAS 285 629 Glu-rich.
SITE 762 763 Cleavage; by caspase-3. {ECO:0000250}.
MOD_RES 296 296 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13464}.
MOD_RES 754 754 Phosphoserine.
{ECO:0000250|UniProtKB:Q13464}.
MOD_RES 757 757 Phosphoserine.
{ECO:0000250|UniProtKB:P70335}.
MOD_RES 977 977 Phosphoserine.
{ECO:0000250|UniProtKB:Q13464}.
NON_TER 1 1
SEQUENCE 1003 AA; 117524 MW; 18C6F52FBF012A83 CRC64;
VAPVVPDLSS DIDTSNFDDL EEDKGEEETF PIPKAFVGNQ LPFVGFTYYS NRRYLSSANP
NDNRTSSNAD KSLQESLQKT IYKLEEQLHN EMQLKDEMEQ KCRTSNIKLD KIMKELDEEG
NQRRNLESTV SQIEKEKMLL QHRINEYQRK AEQENEKRRN VENEVSTLKD QLEDLKKVSQ
NSQLANEKLS QLQKQLEEAN DLLRTESDTA VRLRKSHTEM SKSISQLESL NRELQERNRI
LENSKSQTDK DYYQLQAILE AERRDRGHDS EMIGDLQARI TSLQEEVKHL KHNLEKVEGE
RKEAQDMLNH SEKEKNNLEI DLNYKLKSLQ QRLEQEVNEH KVTKARLTDK HQSIEEAKSV
AMCEMEKKLK EEREAREKAE NRVVQIEKQC SMLDVDLKQS QQKLEHLTGN KERMEDEVKN
LTLQLEQESN KRLLLQNELK TQAFEADNLK GLEKQMKQEI NTLLEAKRLL EFELAQLTKQ
YRGNEGQMRE LQDQLEAEQY FSTLYKTQVK ELKEEIEEKN RENLKKIQEL QNEKETLATQ
LDLAETKAES EQLARGLLEE QYFELTQESK KAASRNRQEI TDKDHTVSRL EEANSMLTKD
IEILRRENEE LTEKMKKAEE EYKLEKEEEI SNLKAAFEKN INTERTLKTQ AVNKLAEIMN
RKDFKIDRKK ANTQDLRKKE KENRKLQLEL NQEREKFNQM VVKHQKELND MQAQLVEECA
HRNELQMQLA SKESDIEQLR AKLLDLSDST SVASFPSADE TDGNLPESRI EGWLSVPNRG
NIKRYGWKKQ YVVVSSKKIL FYNDEQDKEQ SNPSMVLDID KLFHVRPVTQ GDVYRAETEE
IPKIFQILYA NEGECRKDVE MEPVQQAEKT NFQNHKGHEF IPTLYHFPAN CDACAKPLWH
VFKPPPALEC RRCHVKCHRD HLDKKEDLIC PCKVSYDVTS ARDMLLLACS QDEQKKWVTH
LVKKIPKNPP SGFVRASPRT LSTRSTANQS FRKVVKNTSG KTR


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