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Database: UniProt
Entry: A0A2A3EII2_APICC
LinkDB: A0A2A3EII2_APICC
Original site: A0A2A3EII2_APICC 
ID   A0A2A3EII2_APICC        Unreviewed;      1091 AA.
AC   A0A2A3EII2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Active breakpoint cluster region-related protein {ECO:0000313|EMBL:PBC31520.1};
GN   ORFNames=APICC_07123 {ECO:0000313|EMBL:PBC31520.1};
OS   Apis cerana cerana (Oriental honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC31520.1, ECO:0000313|Proteomes:UP000242457};
RN   [1] {ECO:0000313|EMBL:PBC31520.1, ECO:0000313|Proteomes:UP000242457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC31520.1};
RA   Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA   Wu J.;
RT   "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT   insights into honey bee biology.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ288232; PBC31520.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3EII2; -.
DR   STRING; 94128.A0A2A3EII2; -.
DR   Proteomes; UP000242457; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd13368; PH_BCR_arthropod; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 4.10.280.30; Bcr-Abl oncoprotein oligomerisation domain; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR037769; Abr/Bcr.
DR   InterPro; IPR036481; Bcr-Abl_oncoprot_oligo_sf.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23182; BREAKPOINT CLUSTER REGION PROTEIN BCR; 1.
DR   PANTHER; PTHR23182:SF1; RHO GTPASE ACTIVATING PROTEIN AT 1A, ISOFORM E; 1.
DR   Pfam; PF19057; PH_19; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000242457}.
FT   DOMAIN          342..531
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          546..707
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          885..1073
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          142..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..218
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1091 AA;  123129 MW;  5E6B71B3E8D74997 CRC64;
     MSVFGDFQRV WVQRFPDSAL PAAWEEDVRA NLVKHKQKVT ALREELEKEE FYVEYLERLL
     ADVERHKQLA NSNIITSPDK QQPIESQNQH SCQAAENNLT NSTSTSHIQH VESSISSLPA
     SEDISKFQDK CVTELSSTLN TCKRPKSEIP RCPDKVPELR RNSDPDVPSN YVTVIEVTGS
     SKKDKNEESL KEEDEKDLEN AINEDGEDGD AEVSEEEPYY DSVALDQTGE YVYIDARVPP
     VGNNNGSRAP PRRPPSLPDS PGNQSNYVNI DYFIQHRVAD SEDEEGASPA PILLRALSTD
     NETGSSDAEP LSLSEGSLES PTPTTPRRQE KSKEREDDRT SMIKCIVNSV VESETIYVEC
     LNVMLQYMKA IRATLTTSQP VISEDEFGTM FYKIPELHAL HQTFLDGLRK KLEKWDIKTT
     IGEQFKVMAS NIGLYGAFLH NYARATDTVR RCSAHSTQFG EITRDIRLRG FPKGPGLSLE
     DLLHKPVARV QKNALVLHDL LKHTPVNHAD HAPLSEALAM TRNFLDEFNI IQTKSMFPSH
     DRAQRRLVKN SFVVELSDGH RKLRHLFLFN DVIACAKYKA SGRDKFTFEL KWYVPVAEAA
     VTEDGVEPRE TSPANVVALR SQACTVRDQI LWEERNDEKR IRLGGRGSEK NRKKLAELEA
     QLVLASPNLV LRVAHKSQHR VQNSYTFFLS SEFERSQWVE AVEALQQGGQ PPGPLPLSMY
     ELQAWVTACR TYLQTDMGSY LLRSGRDESL LLGDLHLTLL GLTPPGLDRV GDLYIIVEVD
     SYGHYFKRAR SRVARGQAPT WGETFVVELE GSQNVRILLY EECGTRSVLR GKCIQRLSRS
     WLQSDQIERS LNLGPATLDV ALRFVPSEVT LRRVPSAKPQ GLFGAKIQQV CKREKRDVPF
     IITACVREVE RRGVGEVGLY RVSGSASDLT KLRKSFESNS YEAEQLLKEI YYLYKVDVHS
     VTGVLKLYLR EMPEALFTDA LYPAFLEAFQ TGELSKGAAL RRVYESLPAV NKAVIDFLLA
     HLIRVNKHEA QNKMSLHNLA TVFGPTLLRP DAYATEQSVT LVERFLLIHR SVSCFLRVSL
     EIELAATYAV M
//
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