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Database: UniProt
Entry: A0A182UVL6_ANOME
LinkDB: A0A182UVL6_ANOME
Original site: A0A182UVL6_ANOME 
ID   A0A182UVL6_ANOME        Unreviewed;       595 AA.
AC   A0A182UVL6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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};
OS   Anopheles merus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM004417-PA, ECO:0000313|Proteomes:UP000075903};
RN   [1] {ECO:0000313|Proteomes:UP000075903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles merus MAF (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEM004417-PA}
RP   IDENTIFICATION.
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM004417-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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   AlphaFoldDB; A0A182UVL6; -.
DR   STRING; 30066.A0A182UVL6; -.
DR   EnsemblMetazoa; AMEM004417-RA; AMEM004417-PA; AMEM004417.
DR   VEuPathDB; VectorBase:AMEM004417; -.
DR   VEuPathDB; VectorBase:AMEM21_009079; -.
DR   VEuPathDB; VectorBase:AMEM21_014153; -.
DR   OrthoDB; 643105at2759; -.
DR   Proteomes; UP000075903; Unassembled WGS sequence.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR025875; Leu-rich_rpt_4.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR48051; -; 1.
DR   PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR   Pfam; PF12799; LRR_4; 1.
DR   Pfam; PF13855; LRR_8; 4.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00364; LRR_BAC; 13.
DR   SMART; SM00365; LRR_SD22; 9.
DR   SMART; SM00369; LRR_TYP; 16.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   PROSITE; PS51450; LRR; 7.
PE   3: Inferred from homology;
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  64249 MW;  685F2D3F0D3514A3 CRC64;
     MNLSSSGGGG TGTSANTSGS SGGSGGSYSA VGGGSVGAGG SSANGANVSA ATGSGGYGSG
     SGGSGSEMPA EIIRPKVVTV KHPESNKPKP TTKKGKAIQA DVDVIKEFQR CKEENIQRLD
     LSKSSITVIP ASVKDCTSLV EFYLYGNKIS SLPPEIGCLA NLKTLALNEN SLTSLPDSLQ
     NLKQLKVLDL RHNKLSDIPD VIYKLHTLTT LYLRFNRIRV VGDNLKNLSS LTMLSLRENK
     IHELPAAIGH LVNLTTLDLS HNHLKHLPEA IGNCVNLTAL DLQHNDLLDI PESIGNLSNL
     MRLGLRYNQL TSIPVSLKNC THMDEFNVEG NGISQLPDGL LASLSNLTTI TLSRNAFHSY
     PSGGPAQFTN VTSINLEHNQ IDKIQYGIFS RAKGLTKLNM KENALTSLPL DIGTWTQMVE
     LNFGTNSLTK LPDDIHCLQN LEILILSNNL LKRIPNTIGN LKKLRVLDLE ENRLESLPSE
     IGLLHDLQKL ILQSNQLSAL PRTIGHLTNL TYLSVGENNL QFLPEEIGTL ENLESLYIND
     NPSLIKLPYE LALCQNLAIM SIENCPLSAL PPEVVSGGPS LVIQYLKLHS PYRQM
//
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