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 03-AUG-2022, entry version 90.
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 Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC 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., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 (By similarity). {ECO:0000250|UniProtKB:P92199}.
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:0000250|UniProtKB:P92199}.
CC -!- SUBUNIT: Interacts with rho-1. {ECO:0000250|UniProtKB:P92199}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cleavage furrow {ECO:0000250}. Note=Colocalizes with
CC nmy-2 myosin thick filaments at the cleavage furrow.
CC {ECO:0000250|UniProtKB:P92199}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000255}.
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DR EMBL; HE600906; CAP24762.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WVU9; -.
DR SMR; A8WVU9; -.
DR STRING; 6238.CBG03960; -.
DR PRIDE; A8WVU9; -.
DR WormBase; CBG03960; CBP01010; WBGene00026716; Cbr-let-502.
DR eggNOG; KOG0612; Eukaryota.
DR HOGENOM; CLU_000288_140_0_1; -.
DR InParanoid; A8WVU9; -.
DR OMA; AFECKNC; -.
DR OrthoDB; 759391at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
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; IBA:GO_Central.
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:0048598; P:embryonic morphogenesis; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:1901888; P:regulation of cell junction assembly; IBA:GO_Central.
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 3: Inferred from homology;
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..1194
FT /note="Rho-associated protein kinase let-502"
FT /id="PRO_0000389425"
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 784..846
FT /note="RhoBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01206"
FT DOMAIN 961..1171
FT /note="PH"
FT /evidence="ECO:0000255"
FT ZN_FING 1085..1138
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT COILED 436..844
FT /evidence="ECO:0000255"
FT COILED 875..933
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 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
