ID   A0A0N0BED4_9HYME        Unreviewed;      1217 AA.
AC   A0A0N0BED4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   ORFNames=WN51_01687 {ECO:0000313|EMBL:KOX71414.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX71414.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX71414.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX71414.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX71414.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ435840; KOX71414.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0BED4; -.
DR   STRING; 166423.A0A0N0BED4; -.
DR   OrthoDB; 3677323at2759; -.
DR   Proteomes; UP000053105; Unassembled WGS sequence.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR48051; -; 1.
DR   PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00364; LRR_BAC; 11.
DR   SMART; SM00369; LRR_TYP; 10.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51450; LRR; 5.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          693..918
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          990..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1012
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1036
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1217 AA;  136471 MW;  7993263B4BC5F806 CRC64;
     MVYLGDLMAI MEERDFDRDA IDTDSLESEA IQLSTCPKQL DLSNGGLSRI PDSAIAFPAI
     EELVLGQNQL TNGNNNMMLL HRKHQIVMKK IVYRQGLKSV KLIEFLSITK VPETSYPPSG
     VQRAEENTTG ITGAHGVELP QSLRQQNRKN SGRHKPAYQL SSVVERCEGC SRSSETSTLF
     KHQAKNKERR GEVRSGRVLC PTRFQFYFKK LKVCDDTDAY CMQEGFHHNS KLSTQVHILL
     KELILDRNEI KELPHELVQL KNLRNISLAG NCLSSLPPFF NMRALALTDV LTKTEHSKGC
     KDDKNNQNLY KVNLRNNQLK GNIILGNYGN LTHLDVSENS IEKLDISALQ ELRSVRCARN
     ILTELTVCGR NIVSLIAGNN KLKKLTIEPV PVNLEHLDVS YNNLDTLPEW IPDLPLLRAL
     FASHNALTAL PDRLLTQPSR LEVLHLPHNR LQALPPPRKP LNIVHLTLQD NALTALPTSF
     FLNTEKMKVL NLSNNRLSEL PHLGEGNKNR HTNHNLEKLY LTANCLTDTA LDTLAKLTSL
     RVLHIAYNTL DTLPESCIAS WRDLEELVLS GNRLQYLPDN VANLRHLRVL RVHSNRLLTC
     PTFNKTASLK VLDLAHNHLD RVNLATLVPP QLQFLDISCN SRLHVDPRQF QVYRSQRPIS
     LVDVSGQNRP SLPSHPHQQE IVSAEKGLEQ PWRLGFSETA GSRERLYVSQ VRMPSFCNVE
     GLFGVFDGGS NQEAPCALQE MIPRLLLEER TVRETSKEYL KYTLLSAHRE LKEKGQKYGI
     DATLVHILRI QAQQGYPKTS AKYSLKVATS GDAKAVLCRA AGPLTLATSK KVTVKNQLGN
     AAMFPLVVPD PIFEEIDLED DDEFVIIGNR RLWEVLSVQE AVREARAEAS PVLAAKRLQD
     LAQAYGAEDN LSIVVVRLTG PNQGDLDQLM RELRHAVGKN RSQTEAGCPC ACCVPPAAHK
     PPGPCCCHAN EGYYLNGVLK SIVNRSNKAH NESGRYFKNR RSAQENESPP YKDDRSSPSG
     QSDQASDSTF KSRHPSGRVW SGNAASRATN KARQNVLGNE NGTRKVSTCI TAQEDTVSER
     SGALSEEQFR CWEYMLEQNT QLLFDKELDT LTRTPLRRGQ SRSTPQLTGN LPFLSKRFGS
     ARSFNPSLPR PPIVRFGSGR RLLNGGPNAA YFGSLQRLMP YNLEYDFAVI QERNGLDSLE
     QDATRMQQYW GVATTEL
//