ROCK1_BOVIN
ID ROCK1_BOVIN Reviewed; 441 AA.
AC Q8MIT6;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Rho-associated protein kinase 1;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q13464};
DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase 1;
DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase I;
DE Short=ROCK-I;
DE AltName: Full=p160 ROCK-1;
DE Short=p160ROCK;
DE Flags: Fragment;
GN Name=ROCK1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=12034773; DOI=10.1083/jcb.200203034;
RA Chevrier V., Piel M., Collomb N., Saoudi Y., Frank R., Paintrand M.,
RA Narumiya S., Bornens M., Job D.;
RT "The Rho-associated protein kinase p160ROCK is required for centrosome
RT positioning.";
RL J. Cell Biol. 157:807-817(2002).
RN [2]
RP FUNCTION.
RX PubMed=9099667; DOI=10.1074/jbc.272.16.10333;
RA Kosako H., Amano M., Yanagida M., Tanabe K., Nishi Y., Kaibuchi K.,
RA Inagaki M.;
RT "Phosphorylation of glial fibrillary acidic protein at the same sites by
RT cleavage furrow kinase and Rho-associated kinase.";
RL J. Biol. Chem. 272:10333-10336(1997).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, INHIBITION BY Y-27632, AND FUNCTION.
RX PubMed=9353125; DOI=10.1038/40187;
RA Uehata M., Ishizaki T., Satoh H., Ono T., Kawahara T., Morishita T.,
RA Tamakawa H., Yamagami K., Inui J., Maekawa M., Narumiya S.;
RT "Calcium sensitization of smooth muscle mediated by a Rho-associated
RT protein kinase in hypertension.";
RL Nature 389:990-994(1997).
CC -!- FUNCTION: Protein kinase which is a key regulator of the actin
CC cytoskeleton and cell polarity (PubMed:9099667, PubMed:9353125).
CC Involved in regulation of smooth muscle contraction, actin cytoskeleton
CC organization, stress fiber and focal adhesion formation, neurite
CC retraction, cell adhesion and motility via phosphorylation of DAPK3,
CC GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A (PubMed:9099667,
CC PubMed:9353125). Phosphorylates FHOD1 and acts synergistically with it
CC to promote SRC-dependent non-apoptotic plasma membrane blebbing.
CC Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon
CC UVB-induced stress (By similarity). Acts as a suppressor of
CC inflammatory cell migration by regulating PTEN phosphorylation and
CC stability (By similarity). Acts as a negative regulator of VEGF-induced
CC angiogenic endothelial cell activation. Required for centrosome
CC positioning and centrosome-dependent exit from mitosis
CC (PubMed:12034773). Plays a role in terminal erythroid differentiation
CC (By similarity). Inhibits podocyte motility via regulation of actin
CC cytoskeletal dynamics and phosphorylation of CFL1 (By similarity).
CC Promotes keratinocyte terminal differentiation (By similarity).
CC Involved in osteoblast compaction through the fibronectin
CC fibrillogenesis cell-mediated matrix assembly process, essential for
CC osteoblast mineralization (By similarity). May regulate closure of the
CC eyelids and ventral body wall by inducing the assembly of actomyosin
CC bundles (By similarity). {ECO:0000250|UniProtKB:P70335,
CC ECO:0000250|UniProtKB:Q13464, ECO:0000269|PubMed:12034773,
CC ECO:0000269|PubMed:9099667, ECO:0000269|PubMed:9353125}.
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:0000250|UniProtKB:Q13464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:Q13464};
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:0000250|UniProtKB:Q13464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000250|UniProtKB:Q13464};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by RHOA binding (By similarity).
CC Inhibited by Y-27632. {ECO:0000250, ECO:0000269|PubMed:9353125}.
CC -!- SUBUNIT: Homodimer. Interacts with RHOA (activated by GTP), RHOB, RHOC,
CC GEM, MYLC2B, RHOE, PPP1R12A, LIMK1, LIMK2, TSG101, CHORDC1, DAPK3,
CC PFN1, PTEN and JIP3. Interacts with FHOD1 in a Src-dependent manner.
CC Interacts with ITGB1BP1 (via N-terminus and PTB domain). Interacts with
CC SHROOM3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q13464}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12034773}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:P70335}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P70335}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:12034773}. Cell projection, bleb
CC {ECO:0000250|UniProtKB:P70335}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P70335}. Cell membrane
CC {ECO:0000250|UniProtKB:P70335}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P70335}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:P70335}. Note=A small proportion is associated
CC with Golgi membranes (By similarity). Associated with the mother
CC centriole and an intercentriolar linker (By similarity). Colocalizes
CC with ITGB1BP1 and ITGB1 at the cell membrane predominantly in
CC lamellipodia and membrane ruffles, but also in retraction fibers (By
CC similarity). Localizes at the cell membrane in an ITGB1BP1-dependent
CC manner (By similarity). {ECO:0000250|UniProtKB:P70335}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AY052529; AAL13430.1; -; mRNA.
DR AlphaFoldDB; Q8MIT6; -.
DR SMR; Q8MIT6; -.
DR STRING; 9913.ENSBTAP00000053818; -.
DR PaxDb; Q8MIT6; -.
DR PRIDE; Q8MIT6; -.
DR eggNOG; KOG0612; Eukaryota.
DR InParanoid; Q8MIT6; -.
DR OrthoDB; 759391at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP 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; ISS:UniProtKB.
DR GO; GO:0072518; F:Rho-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:AgBase.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0048598; P:embryonic morphogenesis; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0051451; P:myoblast migration; ISS:UniProtKB.
DR GO; GO:0042326; P:negative regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0090521; P:podocyte cell migration; ISS:UniProtKB.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:AgBase.
DR GO; GO:1903431; P:positive regulation of cell maturation; IMP:AgBase.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:1901888; P:regulation of cell junction assembly; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:AgBase.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR Pfam; PF08912; Rho_Binding; 1.
DR PROSITE; PS51859; RHO_BD; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Golgi apparatus; Kinase;
KW Magnesium; Membrane; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN <1..>441
FT /note="Rho-associated protein kinase 1"
FT /id="PRO_0000086618"
FT DOMAIN 356..422
FT /note="RhoBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01206"
FT REGION 114..353
FT /note="SHROOM3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q13464"
FT COILED <1..99
FT /evidence="ECO:0000255"
FT COILED 418..>441
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 441
SQ SEQUENCE 441 AA; 52386 MW; 219A587DB09F9CBC CRC64;
NSKSQMDKDY YQLQAVLEAE RRDRGHDSEK IGDLQARITS LQEEVKHLKH NLERVEGERK
EAQDMLNHSE KEKNNLEIDL NYKLKSLQQR LEQEVNEHKV TKARLTDKHQ SIEEAKSVAM
CEMEKKLKEE RDAREKAENR VVQIEKQCSM LDVDLKQSQQ KLEHLIENKD RMEDEVKNLT
LQLEQESNKR LLLQNELKTQ AFEADNLKGL EKQMKQEINT LLEAKRLLEF ELAQLTKQYR
GNEGQMRELQ DQLEAEQYFS TLYKTQVKEL KEEIEEKNRE NLKKIQELQS EKETLATQLD
LAETKAESEQ LARGLLEEQY FELTQESKKA ASRNRQEITD KDHTLSRLEE TNSMLTKDIE
LLRKENEELT DKMRKAEEEY KLKKEEEINI LKAAFEKNIN TERTLKTQAV NKLAEIMNRK
DFKIDRKKAN TQDLRKKKKK K
