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Kinase suppressor of Ras A (EC 2.7.11.1)

 KSRA_CAEEL              Reviewed;         771 AA.
G5EFD2;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
16-JAN-2019, entry version 66.
RecName: Full=Kinase suppressor of Ras A {ECO:0000305};
EC=2.7.11.1 {ECO:0000305};
Name=ksr-1 {ECO:0000312|WormBase:F13B9.5};
ORFNames=F13B9.5 {ECO:0000312|WormBase:F13B9.5};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|EMBL:AAA92436.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF GLY-484;
GLY-494; ARG-531; PRO-630; PRO-696 AND CYS-727.
STRAIN=Bristol N2 {ECO:0000312|EMBL:AAA92436.1};
PubMed=8521513; DOI=10.1016/0092-8674(95)90205-8;
Sundaram M., Han M.;
"The C. elegans ksr-1 gene encodes a novel Raf-related kinase involved
in Ras-mediated signal transduction.";
Cell 83:889-901(1995).
[2] {ECO:0000312|EMBL:AAB35769.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF ARG-277;
GLY-549; PRO-630 AND PRO-696.
PubMed=8521514; DOI=10.1016/0092-8674(95)90206-6;
Kornfeld K., Hom D.B., Horvitz H.R.;
"The ksr-1 gene encodes a novel protein kinase involved in Ras-
mediated signaling in C. elegans.";
Cell 83:903-913(1995).
[3] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[4] {ECO:0000305}
FUNCTION, INTERACTION WITH MEK-2, AND MUTAGENESIS OF LYS-503; ARG-531
AND ASP-618.
PubMed=10409742; DOI=10.1128/MCB.19.8.5523;
Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.;
"Kinase suppressor of Ras forms a multiprotein signaling complex and
modulates MEK localization.";
Mol. Cell. Biol. 19:5523-5534(1999).
[5] {ECO:0000305}
FUNCTION.
PubMed=11882296; DOI=10.1016/S0960-9822(02)00690-5;
Ohmachi M., Rocheleau C.E., Church D., Lambie E., Schedl T.,
Sundaram M.V.;
"C. elegans ksr-1 and ksr-2 have both unique and redundant functions
and are required for MPK-1 ERK phosphorylation.";
Curr. Biol. 12:427-433(2002).
[6] {ECO:0000305}
FUNCTION.
PubMed=15268855; DOI=10.1016/j.cub.2004.07.022;
Nicholas H.R., Hodgkin J.;
"The ERK MAP kinase cascade mediates tail swelling and a protective
response to rectal infection in C. elegans.";
Curr. Biol. 14:1256-1261(2004).
[7] {ECO:0000305}
FUNCTION.
PubMed=23900546; DOI=10.1242/dev.094011;
Masoudi N., Fancsalszky L., Pourkarimi E., Vellai T., Alexa A.,
Remenyi A., Gartner A., Mehta A., Takacs-Vellai K.;
"The NM23-H1/H2 homolog NDK-1 is required for full activation of Ras
signaling in C. elegans.";
Development 140:3486-3495(2013).
-!- FUNCTION: Serine/threonine-protein kinase which positively
regulates Ras-mediated signaling probably acting at the level of
let-60/ras or/and lin-45/raf. Involved in sex myoblast migration
(PubMed:8521513, PubMed:11882296). Plays a role in responses to
M.nematophilum-mediated bacterial infection by promoting tail
swelling and preventing constipation (PubMed:15268855). Functions
redundantly with ksr-2 in the Ras-mediated regulation of larval
survival, the development of excretory canal and in mpk-1
phosphorylation in somatic cells (PubMed:8521513,
PubMed:11882296). In addition, involved in determining vulval
precursor cell fate during vulval induction independently of its
kinase activity (PubMed:8521514, PubMed:8521513, PubMed:10409742,
PubMed:11882296). Plays a role in egg-laying (PubMed:23900546).
{ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:11882296,
ECO:0000269|PubMed:15268855, ECO:0000269|PubMed:23900546,
ECO:0000269|PubMed:8521513, ECO:0000269|PubMed:8521514}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000305};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000305};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
-!- SUBUNIT: Interacts with mek-2. {ECO:0000269|PubMed:10409742}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
-!- CAUTION: The kinase may be catalytically inactive.
{ECO:0000303|PubMed:10409742}.
-----------------------------------------------------------------------
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EMBL; U38820; AAA92436.1; -; mRNA.
EMBL; S80647; AAB35769.1; -; mRNA.
EMBL; BX284606; CCD69410.1; -; Genomic_DNA.
RefSeq; NP_509396.1; NM_076995.6.
UniGene; Cel.11005; -.
ProteinModelPortal; G5EFD2; -.
SMR; G5EFD2; -.
ELM; G5EFD2; -.
STRING; 6239.F13B9.5.2; -.
EPD; G5EFD2; -.
PaxDb; G5EFD2; -.
PeptideAtlas; G5EFD2; -.
EnsemblMetazoa; F13B9.5.1; F13B9.5.1; WBGene00002239.
EnsemblMetazoa; F13B9.5.2; F13B9.5.2; WBGene00002239.
GeneID; 181082; -.
KEGG; cel:CELE_F13B9.5; -.
CTD; 181082; -.
WormBase; F13B9.5; CE25854; WBGene00002239; ksr-1.
eggNOG; KOG0193; Eukaryota.
eggNOG; ENOG410Y4UP; LUCA.
GeneTree; ENSGT00940000173084; -.
InParanoid; G5EFD2; -.
OMA; EVSPMRF; -.
OrthoDB; 281487at2759; -.
PhylomeDB; G5EFD2; -.
SignaLink; G5EFD2; -.
PRO; PR:G5EFD2; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00002239; Expressed in 5 organ(s), highest expression level in multi-cellular organism.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IGI:WormBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0001708; P:cell fate specification; IGI:WormBase.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0051451; P:myoblast migration; IMP:WormBase.
GO; GO:0002119; P:nematode larval development; IMP:WormBase.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IGI:WormBase.
GO; GO:0040026; P:positive regulation of vulval development; IGI:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IGI:WormBase.
GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
CDD; cd00029; C1; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00109; C1; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Kinase; Magnesium; Meiosis;
Metal-binding; Nucleotide-binding; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase;
Zinc; Zinc-finger.
CHAIN 1 771 Kinase suppressor of Ras A.
{ECO:0000305}.
/FTId=PRO_0000434554.
DOMAIN 477 748 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 215 269 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 483 491 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 318 321 Poly-Ser. {ECO:0000255}.
ACT_SITE 600 600 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 503 503 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MUTAGEN 277 277 R->H: In n2509; restores vulva
development in a let-60 n1046gf mutant
background. {ECO:0000269|PubMed:8521514}.
MUTAGEN 484 484 G->E: In ku113; restores vulva
development in a let-60 n1046gf mutant
background. {ECO:0000269|PubMed:8521513}.
MUTAGEN 494 494 G->E: In ku83; abnormal sex myoblast (SM)
migration. Restores vulva development in
a let-60 n1046gf mutant background.
{ECO:0000269|PubMed:8521513}.
MUTAGEN 503 503 K->M: Probable loss of kinase activity.
Does not rescue vulva development in a
let-60 n1046gf mutant background.
{ECO:0000269|PubMed:10409742}.
MUTAGEN 531 531 R->H: In ku68; egg-laying defect in 14
percent of mutants. Arrest at the larval
stage in 12 percent of mutants and
abnormal sex myoblast (SM) migration.
Restores vulva development in a let-60
n1046gf mutant background.
{ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:8521513}.
MUTAGEN 549 549 G->E: In n1860; arrest at the larval
stage in 12 percent of mutants. Restores
vulva development in a let-60 n1046gf
mutant background.
{ECO:0000269|PubMed:8521514}.
MUTAGEN 618 618 D->A: Probable loss of kinase activity.
Does not rescue vulva development in a
let-60 n1046gf mutant background.
{ECO:0000269|PubMed:10409742}.
MUTAGEN 630 630 P->L,S: In ku146 and n2522; restores
vulva development in a let-60 n1046gf
mutant background.
{ECO:0000269|PubMed:8521513,
ECO:0000269|PubMed:8521514}.
MUTAGEN 696 696 P->L: In n2519; restores vulva
development in a let-60 n1046gf mutant
background. {ECO:0000269|PubMed:8521513}.
MUTAGEN 727 727 C->Y: In ku148; restores vulva
development in a let-60 n1046gf mutant
background. {ECO:0000269|PubMed:8521513}.
SEQUENCE 771 AA; 86434 MW; B9EB1A3EDA4ACE44 CRC64;
MMQTQVASRA GYSNLPQFGA GIAQDIKTQA INNLKECLKL TTINRFLTSS YEEDAKSVER
KIFSAVYQMT KIGLIDREKR EINAIWFTFV GLSAQNIRHL EICSITDFNA LFSITNQELR
SLADRGRLDV ETKRKLLQST VILQNHWNAY HSRTSSGSTD EPSGQSTPAI VTPSPKFNVP
SLSVTSAKMI QSSSMGFATT PKSPKTSSRL VHAIPHKWHR STKFRFSGDA VCHFCQRPLG
FGFLNAWEKC RSCKWKVHTQ CKGRVGDSCG LTPDHLRFLF DKLIQENNGG MWKDPQSVPG
SRSMNEPAFQ FPDTAIDSSS STNSSAPSTP ALPAGISGNV SSLTAPYRSE RKFLFPDTEN
YSVHNRLPIL VISEGDHPTT TEIQQETENH NKSAAASMSG NIESEGTIVA NHEDSTGSQE
VDSEAAPSQE AVDKFNKRAD GGFTWERHAW NMSTIRGPNA QASWNEVTIQ FETIEFDKQA
PIIGRGRFGK VLRGFHYGDV AVKVYTMEHI SDASKKAEEF KLEVSAYKNT RHDNIALFLG
YFMSDGQYGM VMSLSKGSQS LYTLLHVVRE KLDLATTRKI AQQICQAVSY LHTKKILHKD
LRSKNILLES KNKVVITDFG ILSMKRLAHP KQKSGYLTSK FWTNYIAPEL AMAMRTEYDE
YECDDFPFSE NSDVYAFGCV WFEMLTGALP YAGELPHQIL FAKTQGIRPV LPNVKCTQEL
KELLVSCWNT APQDRPTLTD INLKLTALPK KPRVNRSPSF PVMMKSYEST F


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