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Database: UniProt
Entry: A0A6J2YHZ9_SITOR
LinkDB: A0A6J2YHZ9_SITOR
Original site: A0A6J2YHZ9_SITOR 
ID   A0A6J2YHZ9_SITOR        Unreviewed;      1557 AA.
AC   A0A6J2YHZ9;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   10-JUN-2026, entry version 25.
DE   SubName: Full=Rho GTPase-activating protein 100F isoform X3 {ECO:0000313|RefSeq:XP_030762749.1};
GN   Name=LOC115887457 {ECO:0000313|RefSeq:XP_030762749.1};
OS   Sitophilus oryzae (Rice weevil) (Curculio oryzae).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Dryophthorinae; Sitophilus.
OX   NCBI_TaxID=7048 {ECO:0000313|Proteomes:UP000504635, ECO:0000313|RefSeq:XP_030762749.1};
RN   [1] {ECO:0000313|RefSeq:XP_030762749.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_030762749.1};
RG   RefSeq;
RL   Submitted (JAN-2026) to UniProtKB.
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DR   RefSeq; XP_030762749.1; XM_030906889.1.
DR   GeneID; 115887457; -.
DR   CTD; 43758; -.
DR   OrthoDB; 120383at2759; -.
DR   Proteomes; UP000504635; Unplaced.
DR   GO; GO:0097060; C:synaptic membrane; IEA:TreeGrafter.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR   GO; GO:0030030; P:cell projection organization; IEA:TreeGrafter.
DR   GO; GO:0046578; P:regulation of Ras protein signal transduction; IEA:TreeGrafter.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00030; C2; 1.
DR   CDD; cd06718; PDZ_Par6-like; 1.
DR   FunFam; 2.30.42.10:FF:000163; rho GTPase-activating protein 100F isoform X1; 1.
DR   FunFam; 1.10.555.10:FF:000031; rho GTPase-activating protein 100F isoform X6; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR052118; Rho-GAP_regulator.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR057459; SYDE1/2_C2.
DR   PANTHER; PTHR46150; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR   PANTHER; PTHR46150:SF3; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR   Pfam; PF25336; C2_SYDE; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468, ECO:0000256|PROSITE-
KW   ProRule:PRU00172}; Reference proteome {ECO:0000313|Proteomes:UP000504635}.
FT   DOMAIN          122..192
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          747..886
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          927..1144
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          25..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1144..1338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1495..1557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..45
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..377
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1228..1241
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1256..1272
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1290..1312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1313..1325
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1513..1534
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1539..1550
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1557 AA;  169109 MW;  6E62EE1910BFF1F0 CRC64;
     MCDKNGKGCF FTRKDNGREA LDLTASPLRA PPTAPNNRPS HPPPMVIQGD FRKVSGISTE
     IFKQIEAVEN DHDASTAAAL EHVERRGEMI VRILDARHLG RSAVEQAKRF LAMQDAKHQV
     QFVEIVKRPG QTLGLYIREG NGQDRPDGVF ISRIALESAV YNSGCLKVGD EILAVNLVDV
     THMSLDDVVI IMSIPRRLVL ATRQRKGGKG GQGSPSVQPR AEHKPPPVVV IKRDLREDEG
     DEVDAPDQHR DPMRQRHTGD GREMNESRSR LGLGLSTLDR QTDRHSQQHS QQPDSNGLDL
     YYNSRPPDTS WGYQPPPPVI TEQPKSSQPH FPQYDRGYPN TLESLAEKVH SFGMGRRMSA
     GGQPVPSRMS SQQSPSSHYY VQHAGTGSRR IMPRSGSDQH LPQTEYTDYT SITQAGRHSL
     LRSSLKSGST LSRYNQRYVD QAAVAAQLQS KYGTTGSQYG TSTLRRNRGS LDYSSDTEAT
     IGSRAGYYYY RDRPSVPAPV PHSTIPTLAR QGSMAAPGGD ITTKFNSLPR DARGASRLAM
     NKRFGDRSVS GVPLLQDDAD GALSAPEMPS SIRRDRGRVP SSPSVFSSDE YRQWLSRTPS
     TSAIYEQIRA SRDVLNQQRA ARFTYSAENI HDALKNMESG IYSSYGRPGT TSTLDRHFSR
     SQQPSIPARS LSTQHITSAA LSSTRSPSMR RMRQLLDLDS VRSGGAPSPV PTPSGTLPRG
     QRQLDINPAE FLKYKIDKPG IPGTSSITGL SQLTSGTLGS TTDEPVSGML WVHLLAGRGL
     RASTGTSAAT TPVTPSGGVP TIGGSTGLRD LYCVLECDRV HKARTVVRTG DLVFDWDESF
     ELDLVNNREL DLLIYSWDPQ YRHKLCYKGS VYLPTLLKSG PIHQLALKIE PRGTLYLRLR
     YTDSQNLYRR RALTTLTLSR TTPLFGVDLE SVVNRENKTG GVPGGVATGL VTGSQHSIPI
     IVKRCVEEVE RRGLDIIGLY RLCGSATKKR ILREAFERNS RSVDLSPDNV PDINVITGVL
     KDYLRELPEP LFTKCLYQMM VDALGVCLPD DPEGNAKLMF SILDCLPRIN RATLIFLMDH
     LALVVSASDR NKMNAQNLAT ALAPPLMLHS GDTMTPTSAK SHDLEYQQPI SVLRYLLQIW
     PTPKHHSGRR GRLPGPRGDS RSACPAEVSG ARAAALGQSR PSAAPSPLPP RSAASAQPRG
     PLPPVPSHQI LGPSSASKGP YRPLSPRVAL PVAAGPASSG PVAPPGPIKP RHVIVSSPGS
     PSSSSDSQSG SDSVKHCLPS RVSSPAIRAS PSSQTMMRSS PSVTISSPGL RQSPSTTLSS
     SIGSPAGPRN SPSVTSISRA SPSLFSQVSR SSSPAMQASS AGLNVTLDGA TPQVSSLSGL
     QNTISNMNTT TGTMFGLYTQ PTTYASTNPF LTGAYMSYNP VESSYSDKFN TIGSTKDIKS
     FFENYSSDTT KYSTKSTTGY ETQSTYTMSE NKYNTIGSKY QDQKSSYLSS ISSAGEMKYS
     PNKNGERFES EQGRSQSSSG LLNVEETPTP TSSIETEDSN TREVGEKDVE GDGEQSD
//
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