ID A0A1B0BNR8_9MUSC Unreviewed; 707 AA.
AC A0A1B0BNR8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-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 Glossina palpalis gambiensis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=67801 {ECO:0000313|EnsemblMetazoa:GPPI035837-PA, ECO:0000313|Proteomes:UP000092460};
RN [1] {ECO:0000313|Proteomes:UP000092460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092460};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPPI035837-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPPI035837-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 EMBL; JXJN01017585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; JXJN01017586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; JXJN01017587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0BNR8; -.
DR STRING; 67801.A0A1B0BNR8; -.
DR EnsemblMetazoa; GPPI035837-RA; GPPI035837-PA; GPPI035837.
DR VEuPathDB; VectorBase:GPPI035837; -.
DR Proteomes; UP000092460; Unassembled WGS sequence.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; PF13855; LRR_8; 3.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00364; LRR_BAC; 11.
DR SMART; SM00365; LRR_SD22; 7.
DR SMART; SM00369; LRR_TYP; 14.
DR SUPFAM; SSF52058; L domain-like; 3.
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..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 80313 MW; E4CB49A2511C9760 CRC64;
MQRKMSAASS KPQTSAESFC RRSRAPPRRT ERPTLRNLNP IFRKREPSED NTILTEKLLK
LARLRGELNL SSRALATVPE KVYEINEPDE SVEVTLDGLV AKEEDAWWNQ VPIRSLDLSS
NQLTHLSPKI EKLNTLNALM LHDNALTSLP REIAQLERLL RLNLSHNKLC ELPHELFRLP
NLRYLNLSHN EFVELHPDIS DLHMLEVLVR KAVKVIKLLI HLILTNLNQK RTNLLIISTH
KSCHNHSYQS HLTITSNPSI IQQDVSNNQL KSLPRGVGFL VRLTTLSLAH NKIRELPNDV
VDMRSLQKLD LMNNDLLSLP EDMGSLRKLQ CLYAQHNDIT VLPHFEGCDL QELHVSNNFI
ERLPKRLCSS SPHLKILDLR DNKIAELPDE IGHLQSLIRL DLSNNSITNL PYSLSTLPHL
TSLQVEGNPI KSIQRHILQC GTVRILKTLR DRAESAEISS KSSNSSLLQN FDNRAMGGDG
LNSPRRQPVD EDSIFPDRYK MRKTRCLAVT MQQLNDVPGE VFEAAADENV NLVDFSRNRL
TTLPLGLLAM KDVATEIIFA NNLISYVPPF ISQFTRITLI NFSCNNLSTL PQEFGVLVTM
RELNISNNRF EYLPSCIFEL KSLEILLARD NRIKGIDATI NGLGSLQRLA TLDLRNNDIE
QVPPILGNLI NITTLDIIGN PFKLPRHQTL EKGTEAIMSY LRDRIPT
//
