Entry sw:ROCK_CAEBR

ID   ROCK_CAEBR              Reviewed;        1194 AA.
AC   A8WVU9;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   18-JAN-2017, entry version 63.
DE   RecName: Full=Rho-associated protein kinase let-502 {ECO:0000250|UniProtKB:P92199, ECO:0000250|UniProtKB:Q13464};
DE            EC=2.7.11.1;
DE   AltName: Full=Lethal protein 502 {ECO:0000250|UniProtKB:P92199};
DE   AltName: Full=Rho-binding kinase let-502 {ECO:0000250|UniProtKB:P92199};
GN   Name=let-502 {ECO:0000312|EMBL:CAP24762.2}; ORFNames=CBG03960;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP24762.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP24762.2};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A.,
RA   D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E.,
RA   Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R.,
RA   Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P.,
RA   Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M.,
RA   Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M.,
RA   Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for
RT   comparative genomics.";
RL   PLoS Biol. 1:166-192(2003).
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P92199}.
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:0000250|UniProtKB:P92199}.
CC   -!- SUBUNIT: Interacts with rho-1. {ECO:0000250|UniProtKB:P92199}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}. Cleavage furrow {ECO:0000250}.
CC       Note=Colocalizes with nmy-2 myosin thick filaments at the cleavage
CC       furrow. {ECO:0000250|UniProtKB:P92199}.
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; HE600906; CAP24762.2; -; Genomic_DNA.
DR   ProteinModelPortal; A8WVU9; -.
DR   STRING; 6238.CBG03960; -.
DR   PRIDE; A8WVU9; -.
DR   EnsemblMetazoa; CBG03960; CBG03960; WBGene00026716.
DR   WormBase; CBG03960; CBP01010; WBGene00026716; Cbr-let-502.
DR   eggNOG; ENOG410IT51; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000017259; -.
DR   InParanoid; A8WVU9; -.
DR   OMA; RHTRTNT; -.
DR   OrthoDB; EOG091G0BOR; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
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; 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   3: Inferred from homology;
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   1194       Rho-associated protein kinase let-502.
FT                                /FTId=PRO_0000389425.
FT   DOMAIN       68    330       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   DOMAIN      331    402       AGC-kinase C-terminal. {ECO:0000255}.
FT   DOMAIN      961   1171       PH. {ECO:0000255}.
FT   NP_BIND      74     82       ATP. {ECO:0000250|UniProtKB:P28523,
FT                                ECO:0000255|PROSITE-ProRule:PRU00159}.
FT   ZN_FING    1085   1138       Phorbol-ester/DAG-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00226}.
FT   COILED      436    844       {ECO:0000255}.
FT   COILED      875    933       {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       333    394       ismart:S_TK_X [T]
FT   MYHIT        68    330       iprf:PROTEIN_KINASE_DOM [T]
FT   MYHIT      1085   1138       iprf:ZF_DAG_PE_2 [T]
FT   MYHIT      1086   1138       ismart:C1 [T]
FT   MYHIT        74     97       ipat:PROTEIN_KINASE_ATP [T]
FT   MYHIT        69    330       ipfam:Pkinase [T]
FT   MYHIT        68    330       ismart:S_TKc [T]
FT   MYHIT       186    198       ipat:PROTEIN_KINASE_ST [T]
FT   MYHIT       331    402       iprf:AGC_KINASE_CTER [T]
SQ   SEQUENCE   1194 AA;  138925 MW;  39F6D40722166AA6 CRC64;
     MEQDELLHQL VDPKSPINIE SLLDTITALV NDCKIPVLMR MKSVDNFISR YERIVESVAA
     LRMKATDFRQ LKVIGRGAFG EVHLVRHTRT NTVYAMKMLN KDDMIKRADS AFFWEERDIM
     AHANSEWIVR LQYAFQDPRH LYMVMEYMPG GDLVNLMTSY EVSEKWTRFY TAEIVEALAA
     LHNMGYIHRD VKPDNMLISR SGHIKLADFG TCVKMNSNGV VRCSTAVGTP DYISPEVLRN
     QGKDSEFGKE VDWWSVGVFI YEMLVGETPF YAEALVSTYA NIMNHQTSLR FPDEPLISTQ
     AKDIIKKFLS AAPERLGKNN VDEIRNHKFF KNDEWTFETL KDATPPIVPS LKSDDDTTHF
     EEIETRDRDN ASDFQLPKTF NGNQLPFIGF TYSNEYSPVK KLLNGASSNG VQNGVENKPV
     VVQQPLTNGH STGIPEEQYE EVVIELDSKK RELESLKDSI SRTEIRAKLI ETEKNSLSSK
     INDLERELKD NKERLRLGAD SDTKVNELSV ELRMSKEYNG EMENELSKFR DKCEQLKEDL
     RKKSGELAQE KNETQRVLQQ KKNAEEAFAE IKRDHEMLQT REAEKSLQLK KALDERKENG
     AYQQSVAKAT DAEWERKMQY YEKQLEQATD DRKREEQKRT AAEFDQSRVA RKLAGIEANY
     ELLQNDYTNM KEARKDLERD LQDVIAEKRR LEIRVEQLMD SRNTDERVLN LCQEELLESQ
     EEAKYKEDGL RGKIDGIRNE LENEKMKSQT LEENLIVADK ERGMLKMEVQ ELMQRHKWEM
     ANKEQNLKHI ENQLEELKEH SRIESTEQES NDKKTIADLN KKLELEKAHK KAVINKLEEE
     MAKRQPLKKG DKGITKSALI KKEREIVGFK KCRTGRILMS LQQENQHLQQ KMTEMYMDSE
     KQGEHFSYQM QEMSQLIETL RDELKEYKDE YPQRHSVNRY EDKRSLDSRE GIPTSISHQN
     IQIDGWLSLR DMTKKSRKPK VVFKKKSDHQ LTLFFQWTNY FVILNEYAFT IYTDEKHLNS
     VVLTIEAGAM AHVRHVTSAD LRNVDDNQLP KIFHIMYDDT SSNSSRHASN SDLSICEPRE
     EGWKRHDFQE LSYHTRTYCD DCGKKLSDFI RPTPAFECKN CHYKTHKEHI AQGTITMCRY
     TGLSRELVLM GTHKEVCNQW VSQLRRFIEA SRPANVSVSR VSSRRHVGGP GSSA
//