MRCK_CAEEL
ID MRCK_CAEEL Reviewed; 1592 AA.
AC O01583;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Serine/threonine-protein kinase mrck-1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q5VT25};
DE AltName: Full=Myotonic dystrophy kinase-related CDC42-binding kinase homolog {ECO:0000312|WormBase:K08B12.5};
GN Name=mrck-1 {ECO:0000312|WormBase:K08B12.5};
GN ORFNames=K08B12.5 {ECO:0000312|WormBase:K08B12.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19675126; DOI=10.1242/dev.039412;
RA Gally C., Wissler F., Zahreddine H., Quintin S., Landmann F., Labouesse M.;
RT "Myosin II regulation during C. elegans embryonic elongation: LET-502/ROCK,
RT MRCK-1 and PAK-1, three kinases with different roles.";
RL Development 136:3109-3119(2009).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25743393; DOI=10.1038/ncomms7449;
RA Lant B., Yu B., Goudreault M., Holmyard D., Knight J.D., Xu P., Zhao L.,
RA Chin K., Wallace E., Zhen M., Gingras A.C., Derry W.B.;
RT "CCM-3/STRIPAK promotes seamless tube extension through endocytic
RT recycling.";
RL Nat. Commun. 6:6449-6449(2015).
CC -!- FUNCTION: Serine/threonine-protein kinase that may phosphorylate and
CC inactivate the phosphatase mel-11, and thereby contribute to the
CC regulation of myosin II contractility during embryonic elongation
CC (PubMed:19675126). Involved in controlling canal length and Golgi/ER
CC integrity during excretory canal elongation (PubMed:25743393).
CC {ECO:0000269|PubMed:25743393, ECO:0000305|PubMed:19675126}.
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:Q5VT25};
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:Q5VT25};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q5VT25};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19675126}.
CC Note=Forms parallel punctate bundles in dorsal and ventral epidermal
CC cells. {ECO:0000269|PubMed:19675126}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic and L4 larval seam cells and
CC in embryonic dorsal and ventral epidermal cells. Also expressed in the
CC pharynx throughout development and in sublateral nerve cords in the L4
CC larva. {ECO:0000269|PubMed:19675126}.
CC -!- DISRUPTION PHENOTYPE: Normal adult development, but progeny arrest at
CC either the L1 stage or during embryogenesis (PubMed:19675126). RNAi-
CC mediated knockdown causes excretory canal truncation, abnormal lumen
CC and cyst formation. In addition, causes a reduced distribution of Golgi
CC and ER components along the excretory canal length and a decrease in
CC cdc-42 activation (PubMed:25743393). {ECO:0000269|PubMed:19675126,
CC ECO:0000269|PubMed:25743393}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO081273; CCD70382.1; -; Genomic_DNA.
DR PIR; T25808; T25808.
DR RefSeq; NP_504599.2; NM_072198.5.
DR AlphaFoldDB; O01583; -.
DR SMR; O01583; -.
DR DIP; DIP-25790N; -.
DR STRING; 6239.K08B12.5.2; -.
DR EPD; O01583; -.
DR PaxDb; O01583; -.
DR PeptideAtlas; O01583; -.
DR EnsemblMetazoa; K08B12.5a.1; K08B12.5a.1; WBGene00006437.
DR EnsemblMetazoa; K08B12.5a.2; K08B12.5a.2; WBGene00006437.
DR GeneID; 179013; -.
DR UCSC; K08B12.5.1; c. elegans.
DR CTD; 179013; -.
DR WormBase; K08B12.5; CE30818; WBGene00006437; mrck-1.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_3_1; -.
DR InParanoid; O01583; -.
DR OMA; EFTIGYM; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; O01583; -.
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:O01583; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006437; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; O01583; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
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:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0010172; P:embryonic body morphogenesis; IGI:WormBase.
DR GO; GO:0048598; P:embryonic morphogenesis; IGI:WormBase.
DR GO; GO:0060562; P:epithelial tube morphogenesis; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:2001137; P:positive regulation of endocytic recycling; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; IMP:UniProtKB.
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; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 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; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1592
FT /note="Serine/threonine-protein kinase mrck-1"
FT /id="PRO_0000432383"
FT DOMAIN 83..351
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 352..426
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 1026..1154
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1181..1479
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT DOMAIN 1544..1557
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT ZN_FING 957..1007
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 782..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 444..782
FT /evidence="ECO:0000255"
FT COILED 811..871
FT /evidence="ECO:0000255"
FT COMPBIAS 782..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 89..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1592 AA; 180744 MW; F909FA8F5C9C876C CRC64;
MAEPPPDDSA PVRLKTLENI YMDGPSKKPE ALSFETLIDS LICLYDECCN STLRKEKCIA
EFVESVKTVI SKAKKLRLSR DDFEVLKVIG KGAFGEVAVV RMRGVGEIYA MKILNKWEMV
KRAETACFRE ERDVLVYGDR RWITNLHYAF QDEKNLYFVM DYYIGGDMLT LLSKFVDHIP
ESMAKFYIAE MVLAIDSLHR LGYVHRDVKP DNVLLDMQGH IRLADFGSCL RILADGSVAS
NVAVGTPDYI SPEILRAMED GRGRYGKECD WWSLGICMYE MLYGTTPFYS ERLVDTYGKI
MSHQDMLDFP DDEIDWVVSE EAKDLIRQLI CSSDVRFGRN GLSDFQLHPF FEGIDWNTIR
DSNPPYVPEV SSPEDTSNFD VDVCEDDFTP CLQETQPPRV LAAFTGNHLP FVGFSYTHGS
LLSDARSLTD EIRAIAQRCQ GDAELMEKSV DGFMVELENE KAELVQKLKE AQTIIAQHVA
ENPRSEEDRN YESTIAQLKD EIQILNKRLE DEALAQQQQK PKDEIVAESE KKLKELKERN
KQLVMEKSEI QRELDNINDH LDQVLVEKAT VVQQRDDMQA ELADVGDSLL TEKDSVKRLQ
DEAEKAKKQV ADFEEKLKEI ETEKIALIKK QEEVTIEARK SVETDDHLSE EVVAAKNTIA
SLQATNEERE TEIKKLKQRM DEERASHTAQ SEQEMKQLEA HYERAQKMLQ DNVEQMNVEN
RGLRDEIEKL SQQMAALPRG GLNEQQLHEI FNWVSEEKAT REEMENLTRK ITGEVESLKN
NSPLTTSNYI QNTPSGWGSR RMNNVARKDG LDLQRQLQAE IDAKLKLKAE LKNSQEQYLT
SAARLDDTEK RMASLMREVA MLKQQKNIEN SSDSAFSSTM GRGDLMISMN NDYEMSNSSL
MRQEMISRQS TPSYENAILL HDHQVPKRVD DLRYKQKPMK TASGIFSPVS ISAMERGHNF
ERMKIKTPTK CGHCTSILIG LDRQGLFCQS CQYACHVSCA ERVSQSCPVP EEERRPLGID
PTRGVGTAYE GLVKTPRAGG VRKGWQTAYV VVCDFKLYLY DCTVDRQNKM QDVKNEIRLV
LDMRDPDFTV CGVSEADVIH AQKGDIPKIF RVTTTQILNS SSEYSSSSKF YTLFMAETEE
EKRKWVVALS ELKTLLRRSK LADRKAFLVK EVFDVTTLPS IRVAQCCAII DRSKIVIGFS
DHGLYCIEIS RQLLIPVGGE KENKQRCVET VEYDEAEQLL MMIVGPAKDR HVRIVPSAAL
DGRDLKWIKV NDTKGCHLLA VGTNNPGGRA GFFAVAFKKS VTIFQIDRSE KRHKKWKDLA
MPGTPQSIAI FNGRLYVGFS HSFRSWSLVG VDSSPVGSGD ASGAVLQHIS LVNMEDTSLQ
FLNQQTSYEA KLIVNVPGSP DEYLLVFNMI GLYVNEMGRR SRLPEVMFPT QAKYFAYHEP
YLCVFSENEV DIFNVTLAEW VQTINLRSAK PLSGDGILST CLCNDSPIFV LLQNVLQDQD
SIEVPVNLAS GSTDGRKVTR RKFTFRTIGK DDRSASERRS HIQISTPSDF MHIVHMGPAP
VMELQQNFID LQSNHSHTSS DKDSLNRSVN ND
