ID A0A182H115_AEDAL Unreviewed; 883 AA.
AC A0A182H115;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=RP20_CCG019558 {ECO:0000313|EMBL:KXJ81470.1};
OS Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7160 {ECO:0000313|EnsemblMetazoa:AALF019558-PA.1, ECO:0000313|Proteomes:UP000069940};
RN [1] {ECO:0000313|EMBL:KXJ81470.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ81470.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ81470.1};
RX PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA Yan G., Tu Z.J., Fang X., James A.A.;
RT "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT insights into its biology, genetics, and evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN [2] {ECO:0000313|EMBL:KXJ81470.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ81470.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ81470.1};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:AALF019558-PA.1}
RP IDENTIFICATION.
RC STRAIN=Foshan {ECO:0000313|EnsemblMetazoa:AALF019558-PA.1};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
CC -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC {ECO:0000256|ARBA:ARBA00009442}.
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DR EMBL; JXUM01022810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; JXUM01022811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KQ560642; KXJ81470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182H115; -.
DR STRING; 7160.A0A182H115; -.
DR EnsemblMetazoa; AALF019558-RA; AALF019558-PA; AALF019558.
DR VEuPathDB; VectorBase:AALC636_030050; -.
DR VEuPathDB; VectorBase:AALF019558; -.
DR VEuPathDB; VectorBase:AALFPA_058616; -.
DR Proteomes; UP000069940; Unplaced.
DR Proteomes; UP000249989; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20830; C1_PIK3R-like_rpt2; 1.
DR CDD; cd12923; iSH2_PI3K_IA_R; 1.
DR CDD; cd00159; RhoGAP; 1.
DR CDD; cd09930; SH2_cSH2_p85_like; 1.
DR CDD; cd09942; SH2_nSH2_p85_like; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR032498; PI3K_P85_iSH2.
DR InterPro; IPR035020; PI3kinase_P85_cSH2.
DR InterPro; IPR035022; PI3kinase_P85_nSH2.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR PANTHER; PTHR46075; CHIMERIN FAMILY MEMBER; 1.
DR PANTHER; PTHR46075:SF5; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT ALPHA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF16454; PI3K_P85_iSH2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF00017; SH2; 2.
DR PRINTS; PR00678; PI3KINASEP85.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000249989};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..55
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 96..146
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 178..374
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 495..589
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 775..868
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 423..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 619..646
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 683..717
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 423..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 98445 MW; BCAED62FAB7E8BEA CRC64;
MAANNLYTYA DVFKAKDIKG CDLSNLDRDK LGQMGIKNEF HQQTILASIK DLLTSAEKPI
QSGGSLRTIS GGSGIVLKSA GEDSSSLDPA SGGKHSHDLV NHSFLKLVKC DKCQQYLRGL
IHQGLLCKQC NLIVHRQCSA TGLMPCAALG TAMDTGGGGG GSRTTVLPTS RIQPVFGVGL
CHQFNVDQLP APQIVIILCN ELEQKALCDD NLDLYKLYRT TQSSYDEVNK LRDSLNENLI
NTDLSNYSPE CVATVLKKFL RELPDPIIPV LFYDKFIEAS KITSDAVAAE TLRLLIHELP
IHHGNTLKHI MVHLIRICRM QCQRGIDSQP TILIQVWCHI LLRPPWEKIV QIVSNTENHL
RIMELLLYKI DWHEKLPEFA SAPAVPPRKI SRSTAALQQQ SVSQPFLQQT LGTSTSTAFQ
AAASGSSLRK QPTTATITSP AAPVIPSTPL VGPIYNNTGS SGGGGSTASG DTRGTAMFRM
VGDADTPADL RAAEWYWGNI SRDEVKEKMT DVPDGSFLVR DASSGNGEYT LTLKKDGTDR
VIKIFHTQDK YGFTRDGSHN SVVDLINFYR NVSLKEYNTI LDIKLLYPIS RFEDDSYISS
TEDDTPRLAQ KFIEISQSLN EKLHEREKLQ EDLTMSKNQV DLKKQAQEAF IEAEKLFQDQ
LAIQTRFVSE AQPHEKQGIS TNNKLIRDRM QELNQCRDQL QEDMKNEKTR IWQLEREINK
LNPIIMSQSK EKTSYIEELK RQGINESQIK QMETDGYFSH SHGSQEMPHN DETTWLAPTF
NRTDAEKELA SKPNGTFVIR TGSGGHFALS IKCNDTVNHC IIQQTERGFG FAEPYNIYES
LKSLVLHYAS NSLEEHNDTL QTTLKYPLLA TGGGSSSSKQ QST
//
