ID E2ARR6_CAMFO Unreviewed; 1185 AA.
AC E2ARR6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Phosphatidylinositol 3-kinase regulatory subunit alpha {ECO:0000313|EMBL:EFN63874.1};
GN ORFNames=EAG_11777 {ECO:0000313|EMBL:EFN63874.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN63874.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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DR EMBL; GL442166; EFN63874.1; -; Genomic_DNA.
DR RefSeq; XP_011262864.1; XM_011264562.2.
DR AlphaFoldDB; E2ARR6; -.
DR STRING; 104421.E2ARR6; -.
DR GeneID; 105255336; -.
DR KEGG; cfo:105255336; -.
DR InParanoid; E2ARR6; -.
DR OMA; EMIDVQV; -.
DR OrthoDB; 2880119at2759; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; 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; 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; 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; SM00454; SAM; 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 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EFN63874.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 361..424
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 468..519
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 541..733
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 789..883
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 1052..1145
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 106..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 933..1010
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 107..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1185 AA; 132338 MW; 5A791C11E579DC34 CRC64;
MKRVTSASVA AATAAATQVH HQARVQELFA PGPISTTMSA STAMVGDSCA DEQDKQLATI
STWLEPKGSP KISPGTNDDN KAKSTAMSRL LAVDSDNYML RKGAAATTAT PVTSSTASSS
SQPSSSLNGS AGVQLQRQMQ GLAIGSAAAP SILTTYGTSG GDHVNVGQLC DVTRTTSRST
GTYVSPRWYA GGNGNQVTRQ HREGTVTAEE QSPQQQLQLQ SRTATTSATL AEGVESELGF
TKFVCARLVS FHRYMCWCGT QPAGGLAEAV DANSIGDRAK GGKSAATPYE GPAARRTVRD
DSFNSSSLCC CMCGSLCPAE CHACFHIVCS DYSSQHLCQW STKGHALPGQ VHDKDKPVSE
WTSLNVVEWM SALNLYRYAD VFKSKDIKGS DLLHLDREKL MNMGIKDEFH QRSILVCIEE
LCQSSPPPPV ATETASSPVT TIPTSGVAAE SGCSLGVNYS GNNVVNKAHK LTQHSFSILE
KCGKCHKYLR GLLHQGFLCQ DCGLVAHRTC SKTGLPSNCI SVDTDNRIGR FTSVFGRGLC
LQFDIVTHSA PVLVERCTHA LEQRAFADTK LDLYKVYHNS NTPNEQTLEL RQKLNEDVYN
ADLSPYTPQC IASVLKKFLR ELPDPVIPVQ WYDRFLEASS MRSDEQCAAR LNQLVAELPE
HHRSTLCHLM AHFCRICQLQ HARAYTEQPT ILVQMLCHIF LRPPWERIIQ VVHNTEAHIR
IMELLLLHGD WNERLPEFAS PPQLPPRKVS RPHFSIVDPS LEGDAVDRTV QPGADQQPHR
PRTLQEAEWY WGDITRDDVN EMMIDSPDGT FLVRNASSKC GEYTLTLRKG GTNKLIKISH
RNGKYGFSDP YNFHSVIELV DYYRNCSLAQ YNAVLDIKLL YPVSRFQQED EITNTTDMAK
VLQKFLDLEK EVSDGIRQYH NCWDLYTKTS SEVELKTQAM EAFQEAIKMF EEQIRLQDEF
RKEAQPHEIS TLTDNSELLQ RRLKALRDSK IQLQENLNQQ TAYNRTLERE TCRLKSETGQ
LARQRDRYAL WLKKNGIKQN KDFAIHSDEK TWLYLQGSRP DADRILKGKP DGTFLVRRSR
TGQYALSIVC NGVVQHCIIY GTERGYGFAE PYNIHQSLKH LVLHYAQNSL EEHNECLTTT
LAYPAFAPPA ALAQLQSQQK QFQIYAQNQM PIARQPHENQ LMSHT
//
