Entry sw: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   30-NOV-2016, entry version 152.
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   Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAB42081.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DISRUPTION 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
RT   human myotonic dystrophy kinase and interacts genetically with a
RT   homolog of the regulatory subunit of smooth muscle myosin phosphatase
RT   to affect cell 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11102366;
RA   Piekny A.J., Wissmann A., Mains P.E.;
RT   "Embryonic morphogenesis in Caenorhabditis elegans integrates the
RT   activity of LET-502 Rho-binding kinase, MEL-11 myosin phosphatase,
RT   DAF-2 insulin 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;
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, ENZYME 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
CC       mlc-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
CC       in 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: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000250|UniProtKB:Q13464}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q13464};
CC   -!- ENZYME 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
CC       furrow {ECO:0000269|PubMed:12006612}. Note=Colocalizes with nmy-2
CC       myosin thick filaments at the cleavage furrow.
CC       {ECO:0000269|PubMed:12006612}.
CC   -!- TISSUE SPECIFICITY: Expressed in the lateral hypodermal seam cells
CC       at the onset of the elongation phase of morphogenesis (at protein
CC       level). {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
CC       of only maternal expression results in abnormal early cleavages,
CC       loss of 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}.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Contains 1 PH domain. {ECO:0000255}.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC       {ECO:0000255|PROSITE-ProRule:PRU00226}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
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   UniGene; Cel.5336; -.
DR   ProteinModelPortal; P92199; -.
DR   SMR; P92199; -.
DR   BioGrid; 37550; 11.
DR   STRING; 6239.C10H11.9; -.
DR   EPD; P92199; -.
DR   PaxDb; P92199; -.
DR   PeptideAtlas; P92199; -.
DR   PRIDE; P92199; -.
DR   EnsemblMetazoa; C10H11.9; C10H11.9; 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; ENOG410IT51; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   GeneTree; ENSGT00760000118994; -.
DR   HOGENOM; HOG000017259; -.
DR   InParanoid; P92199; -.
DR   KO; K04514; -.
DR   OMA; RHTRTNT; -.
DR   OrthoDB; EOG091G0BOR; -.
DR   PhylomeDB; P92199; -.
DR   Reactome; R-CEL-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-CEL-416482; G alpha (12/13) signalling events.
DR   Reactome; R-CEL-416572; Sema4D induced cell migration and growth-cone collapse.
DR   Reactome; R-CEL-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-CEL-5627117; RHO GTPases Activate ROCKs.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   SignaLink; P92199; -.
DR   PRO; PR:P92199; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00002694; -.
DR   GO; GO:0005913; C:cell-cell 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; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0005524; F:ATP binding; ISS:WormBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:WormBase.
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:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:WormBase.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:WormBase.
DR   GO; GO:0007266; P:Rho protein signal transduction; TAS:WormBase.
DR   CDD; cd00029; C1; 1.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR029875; LET-502.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH_dom-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22988:SF38; PTHR22988:SF38; 1.
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; SSF50729; SSF50729; 2.
DR   SUPFAM; SSF56112; SSF56112; 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; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Oogenesis; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1173       Rho-associated protein kinase let-502.
FT                                /FTId=PRO_0000389426.
FT   DOMAIN       68    330       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   DOMAIN      331    402       AGC-kinase C-terminal. {ECO:0000255}.
FT   DOMAIN      950   1144       PH. {ECO:0000255}.
FT   NP_BIND      74     82       ATP. {ECO:0000250|UniProtKB:P28523,
FT                                ECO:0000255|PROSITE-ProRule:PRU00159}.
FT   ZN_FING    1059   1112       Phorbol-ester/DAG-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00226}.
FT   COILED      438    709       {ECO:0000255}.
FT   COILED      735    928       {ECO:0000255}.
FT   ACT_SITE    190    190       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:P28523,
FT                                ECO:0000255|PROSITE-ProRule:PRU00159,
FT                                ECO:0000255|PROSITE-ProRule:PRU10027}.
FT   BINDING      97     97       ATP. {ECO:0000250|UniProtKB:P28523,
FT                                ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        68    330       iprf:PROTEIN_KINASE_DOM [T]
FT   MYHIT       186    198       ipat:PROTEIN_KINASE_ST [T]
FT   MYHIT        69    330       ipfam:Pkinase [T]
FT   MYHIT        68    330       ismart:S_TKc [T]
FT   MYHIT       331    402       iprf:AGC_KINASE_CTER [T]
FT   MYHIT      1060   1112       ismart:C1 [T]
FT   MYHIT        74     97       ipat:PROTEIN_KINASE_ATP [T]
FT   MYHIT       333    394       ismart:S_TK_X [T]
FT   MYHIT      1059   1112       iprf:ZF_DAG_PE_2 [T]
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
//