ID B0XKB4_CULQU Unreviewed; 211 AA.
AC B0XKB4;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Leucine-rich repeat protein soc-2 homolog {ECO:0000256|ARBA:ARBA00023904};
DE AltName: Full=Protein soc-2 homolog {ECO:0000256|ARBA:ARBA00032455};
DE AltName: Full=protein Sur-8 homolog {ECO:0000256|ARBA:ARBA00029588, ECO:0000256|ARBA:ARBA00029998};
GN Name=6054117 {ECO:0000313|EnsemblMetazoa:CPIJ019625-PA};
GN ORFNames=CpipJ_CPIJ019625 {ECO:0000313|EMBL:EDS31539.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS31539.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS31539.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ019625-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ019625-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
CC -!- FUNCTION: Acts as a Ras effector and participates in MAPK pathway
CC activation. Probably acts as a regulatory subunit of protein
CC phosphatase that specifically dephosphorylates Raf kinase and stimulate
CC Raf activity at specialized signaling complexes upon Ras activation.
CC {ECO:0000256|ARBA:ARBA00025612}.
CC -!- SIMILARITY: Belongs to the SHOC2 family.
CC {ECO:0000256|ARBA:ARBA00023786}.
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DR EMBL; DS233774; EDS31539.1; -; Genomic_DNA.
DR RefSeq; XP_001870086.1; XM_001870051.1.
DR AlphaFoldDB; B0XKB4; -.
DR STRING; 7176.B0XKB4; -.
DR EnsemblMetazoa; CPIJ019625-RA; CPIJ019625-PA; CPIJ019625.
DR KEGG; cqu:CpipJ_CPIJ019625; -.
DR VEuPathDB; VectorBase:CPIJ019625; -.
DR VEuPathDB; VectorBase:CQUJHB011010; -.
DR eggNOG; KOG4579; Eukaryota.
DR HOGENOM; CLU_070683_0_1_1; -.
DR InParanoid; B0XKB4; -.
DR OMA; WINVKSN; -.
DR OrthoDB; 4041863at2759; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR Pfam; PF00560; LRR_1; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002320}.
SQ SEQUENCE 211 AA; 24212 MW; 5935BFCECF4BAC23 CRC64;
MASFVARVVN RCEEANETKN LNLSECELIQ VPDAVYHLMR HTELKTCDLS GNVITKISPK
FAVKFSLITG LRKCRVELVV LEGDGLGFAL SKRYDQWHKS ELNLSHNQMA KLPDELADLH
SLQQLDISHN SFITLPAVVF KMPKLRELRA HNNAIIDIDR DEIITSDSLE LVDLRHNPLT
PMCHELLRNA NVSFRIELSE REKEEWEDLT I
//