ID A0A182U610_9DIPT Unreviewed; 435 AA.
AC A0A182U610;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 melas.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC014552-PA, ECO:0000313|Proteomes:UP000075902};
RN [1] {ECO:0000313|Proteomes:UP000075902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
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 melas CM1001059_A (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEC014552-PA}
RP IDENTIFICATION.
RC STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC014552-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; A0A182U610; -.
DR STRING; 34690.A0A182U610; -.
DR EnsemblMetazoa; AMEC014552-RA; AMEC014552-PA; AMEC014552.
DR VEuPathDB; VectorBase:AMEC014552; -.
DR Proteomes; UP000075902; Unassembled WGS sequence.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
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; PF00560; LRR_1; 2.
DR Pfam; PF13516; LRR_6; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 1.
PE 3: Inferred from homology;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 316..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 48249 MW; 5019D4A9394CB281 CRC64;
MKLICETCTI NRSVAGGKRA FQKTILAIGK GSERKGDETK IMLITTANKA GTKYSVLKNI
SKIFTRFLEE GKATISFVAP EHDVQIKSDK VQLTAFLKVL KLVLTGSGQP AEGTQPVTNP
FSPSAPLRLP CLTVGKKKAS ILDSPRVLAT KCVITNRKDY PTKGFSRLLV SLQITDVKLS
RFDSQILLLQ KLRFLNLSNN CLRSLPRALG QLRLSELDLS SNRLADCTWD WLLEPNIQSS
LQSLNISDNG LSFLPINVIN AGALVALTAN NNHIRKLPFA LWTMSRLRVL SLAKNQIDGV
PETLERIRLE RLDLSENNLS PDGGTAELHP SPSMQQRQPS TLFELAARTV IHRKLPYAMP
GLLPFTVVDI LRRVPLCGCG QPCFDAKVYQ RTKVINGRCS CLVLNANHLL IADSVFCSEK
CIRKANERRL HNRGF
//
