ROCK_CAEEL
ID ROCK_CAEEL Reviewed; 1173 AA.
AC P92199;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Rho-associated protein kinase let-502 {ECO:0000250|UniProtKB:Q13464, ECO:0000303|PubMed:9042856};
DE EC=2.7.11.1;
DE AltName: Full=Lethal protein 502;
DE AltName: Full=Rho-binding kinase let-502 {ECO:0000303|PubMed:9042856};
GN Name=let-502; ORFNames=C10H11.9;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB42081.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAB42081.1};
RX PubMed=9042856; DOI=10.1101/gad.11.4.409;
RA Wissmann A., Ingles J., McGhee J.D., Mains P.E.;
RT "Caenorhabditis elegans LET-502 is related to Rho-binding kinases and human
RT myotonic dystrophy kinase and interacts genetically with a homolog of the
RT regulatory subunit of smooth muscle myosin phosphatase to affect cell
RT shape.";
RL Genes Dev. 11:409-422(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11102366; DOI=10.1093/genetics/156.4.1671;
RA Piekny A.J., Wissmann A., Mains P.E.;
RT "Embryonic morphogenesis in Caenorhabditis elegans integrates the activity
RT of LET-502 Rho-binding kinase, MEL-11 myosin phosphatase, DAF-2 insulin
RT receptor and FEM-2 PP2c phosphatase.";
RL Genetics 156:1671-1689(2000).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11687661; DOI=10.1073/pnas.241504098;
RA Spencer A.G., Orita S., Malone C.J., Han M.;
RT "A RHO GTPase-mediated pathway is required during P cell migration in
RT Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13132-13137(2001).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12006612; DOI=10.1242/jcs.115.11.2271;
RA Piekny A.J., Mains P.E.;
RT "Rho-binding kinase (LET-502) and myosin phosphatase (MEL-11) regulate
RT cytokinesis in the early Caenorhabditis elegans embryo.";
RL J. Cell Sci. 115:2271-2282(2002).
RN [6] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH RHO-1, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17537791; DOI=10.1242/dev.005074;
RA Diogon M., Wissler F., Quintin S., Nagamatsu Y., Sookhareea S.,
RA Landmann F., Hutter H., Vitale N., Labouesse M.;
RT "The RhoGAP RGA-2 and LET-502/ROCK achieve a balance of actomyosin-
RT dependent forces in C. elegans epidermis to control morphogenesis.";
RL Development 134:2469-2479(2007).
CC -!- FUNCTION: Negatively regulates mel-11 to relieve the inhibition of mlc-
CC 4, allowing contraction of the circumferentially oriented
CC microfilaments in epidermal cells and thereby regulating myosin II
CC contractility during spermathecal contraction, cleavage furrow
CC contraction in early embryos, and embryonic elongation and
CC morphogenesis. Required for P-cell migration. May also play a role in
CC oocyte cellularization. {ECO:0000269|PubMed:11102366,
CC ECO:0000269|PubMed:11687661, ECO:0000269|PubMed:12006612,
CC ECO:0000269|PubMed:17537791, ECO:0000269|PubMed:9042856}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q13464};
CC -!- ACTIVITY REGULATION: Activated by rho-1 binding.
CC {ECO:0000269|PubMed:17537791}.
CC -!- SUBUNIT: Interacts with rho-1. {ECO:0000269|PubMed:17537791}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12006612}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12006612}. Cleavage furrow
CC {ECO:0000269|PubMed:12006612}. Note=Colocalizes with nmy-2 myosin thick
CC filaments at the cleavage furrow. {ECO:0000269|PubMed:12006612}.
CC -!- TISSUE SPECIFICITY: Expressed in the lateral hypodermal seam cells at
CC the onset of the elongation phase of morphogenesis (at protein level).
CC {ECO:0000269|PubMed:9042856}.
CC -!- DISRUPTION PHENOTYPE: Loss of both zygotic and maternal expression
CC causes defects in embryonic elongation and P-cell migration, loss of
CC only maternal expression results in abnormal early cleavages, loss of
CC only zygotic expression results in sterility.
CC {ECO:0000269|PubMed:11102366, ECO:0000269|PubMed:11687661,
CC ECO:0000269|PubMed:12006612, ECO:0000269|PubMed:17537791,
CC ECO:0000269|PubMed:9042856}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000255}.
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DR EMBL; U85515; AAB42081.1; -; mRNA.
DR EMBL; FO080502; CCD64221.1; -; Genomic_DNA.
DR PIR; T25539; T25539.
DR RefSeq; NP_491440.1; NM_059039.5.
DR AlphaFoldDB; P92199; -.
DR SMR; P92199; -.
DR BioGRID; 37550; 12.
DR STRING; 6239.C10H11.9; -.
DR EPD; P92199; -.
DR PaxDb; P92199; -.
DR PeptideAtlas; P92199; -.
DR PRIDE; P92199; -.
DR EnsemblMetazoa; C10H11.9.1; C10H11.9.1; WBGene00002694.
DR GeneID; 172088; -.
DR KEGG; cel:CELE_C10H11.9; -.
DR UCSC; C10H11.9; c. elegans.
DR CTD; 172088; -.
DR WormBase; C10H11.9; CE08098; WBGene00002694; let-502.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_0_1; -.
DR InParanoid; P92199; -.
DR OMA; AFECKNC; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; P92199; -.
DR Reactome; R-CEL-5625900; RHO GTPases activate CIT.
DR Reactome; R-CEL-8980692; RHOA GTPase cycle.
DR Reactome; R-CEL-9013026; RHOB GTPase cycle.
DR Reactome; R-CEL-9013106; RHOC GTPase cycle.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR PRO; PR:P92199; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002694; Expressed in embryo and 4 other tissues.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0043292; C:contractile fiber; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004674; F:protein serine/threonine kinase activity; ISS:WormBase.
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:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
DR GO; GO:0048598; P:embryonic morphogenesis; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:1905905; P:pharyngeal gland morphogenesis; IMP:UniProtKB.
DR GO; GO:0060465; P:pharynx development; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:WormBase.
DR GO; GO:1901888; P:regulation of cell junction assembly; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IMP:WormBase.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029875; LET-502.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988:SF71; PTHR22988:SF71; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 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; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Oogenesis; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1173
FT /note="Rho-associated protein kinase let-502"
FT /id="PRO_0000389426"
FT DOMAIN 68..330
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 331..402
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 786..848
FT /note="RhoBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01206"
FT DOMAIN 950..1144
FT /note="PH"
FT /evidence="ECO:0000255"
FT ZN_FING 1059..1112
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1154..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 438..709
FT /evidence="ECO:0000255"
FT COILED 735..928
FT /evidence="ECO:0000255"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 74..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1173 AA; 135774 MW; 8E43A80DCA69D417 CRC64;
MEQDELRDQL VDPKSPINIE SLLDTITALV NDCKIPVLMR MKSVDNFISR YERVVESLAA
LRMKAADFRQ LKVIGRGAFG EVHLVRHTRT NTVYAMKMLN KDDMIKRADS AFFWEERDIM
AHANSEWIVR LQYAFQDPRH LYMVMEYMPG GDLVNLMTSY EVSEKWTRFY TAEIVEALAA
LHSMGYIHRD VKPDNMLISI SGHIKLADFG TCVKMNANGV VRCSTAVGTP DYISPEVLRN
QGQDAEFGKE VDWWSVGVFI YEMLVGETPF YAEALVSTYT NIMNHKTSLK FPDEPLISTQ
AKDIIKKFLS AAPDRLGRNS VDDIRNHKFF VNDEWTFATL REASPPVIPS LKSDDDTTHF
EEIETRDRDN AGDFQLPKTF NGNQLPFIGF TYSNEYSPVK NLLKGHGAGS KQNGIEQHKP
QTVVEQPLTN GHASGVPEEK YEAVKMELDS KNREFELLKD SIARNEIRAK MIENEKNSLS
TKISDLEREL KDNKDKLRHG ADSDAKVNEL AVELRMSKEY NSEMESELSK FRDKCEQLKE
DLRKKSGELA QEKNETQRVF QQKKDADEAF AEIKRDYELL QTRENEKSVQ LKKALDERKE
NGAYQQSVAK ATDAEWERKM QFYEKQLEHA NDERKREEQK RTAAEFDQSR VARKLAGIEA
NYELLQNDYK SMKEARKDLE RDLQDVITEK RRLEIRVEQL MDSRNTDERV LSLCQDELVE
SQEEAKYKED GLRGKIDGFK HELENEKMKT QTLEENLLVA DKERGMLKME VQELMQRHKW
EITNKDQTLK HLETQLDEIK QQSKIESSEQ ESNDKQTIAD LRKKLDLEKA HKKAVINKLE
EEMAKRQPLK KGEKGVTKSA LIKKEREIMA LEQERDTMSK RIAALFYEND KQAEHFNIAI
QDMQTTQDAL RDELKECKEE LANRNVNTRY EDKRSLDSRE GIPSSLSNQH IQMEGWLSLR
DNTKKSRKPK WTNCFVALNE YSFTIYVDEK AVSVILLIEA GAMAHVRHVT AADLRNVDDS
QLPKIFHIMY DDASCNSSRH ASNSDLSMIE SFREESWKRH DFQELSYHIR TFCDVCNKKL
SDIIRPTPAF ECKNCHFKTH KDHVAQGSLP MCRYNTGLSR ELVLMAPQTD NCNKWVSQLR
RFIESSRSAA VSVSRVSSRR HAPGSSNSST IYQ
