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Database: UniProt
Entry: A0A2A3EPN3_APICC
LinkDB: A0A2A3EPN3_APICC
Original site: A0A2A3EPN3_APICC 
ID   A0A2A3EPN3_APICC        Unreviewed;      1736 AA.
AC   A0A2A3EPN3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Protein diaphanous {ECO:0000313|EMBL:PBC33464.1};
GN   ORFNames=APICC_09505 {ECO:0000313|EMBL:PBC33464.1};
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:PBC33464.1, ECO:0000313|Proteomes:UP000242457};
RN   [1] {ECO:0000313|EMBL:PBC33464.1, ECO:0000313|Proteomes:UP000242457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC33464.1};
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.
CC   -!- SIMILARITY: Belongs to the RHPN family.
CC       {ECO:0000256|ARBA:ARBA00010369}.
CC   -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC       subfamily. {ECO:0000256|ARBA:ARBA00008214}.
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DR   EMBL; KZ288203; PBC33464.1; -; Genomic_DNA.
DR   STRING; 94128.A0A2A3EPN3; -.
DR   Proteomes; UP000242457; Unassembled WGS sequence.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd09244; BRO1_Rhophilin; 1.
DR   CDD; cd11633; HR1_Rhophilin-1; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 1.20.58.630; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 6.10.30.30; -; 1.
DR   Gene3D; 1.25.40.280; alix/aip1 like domains; 1.
DR   Gene3D; 1.10.20.40; Formin, diaphanous GTPase-binding domain; 1.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR   Gene3D; 1.10.287.160; HR1 repeat; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR004328; BRO1_dom.
DR   InterPro; IPR038499; BRO1_sf.
DR   InterPro; IPR014767; DAD_dom.
DR   InterPro; IPR044933; DIA_GBD_sf.
DR   InterPro; IPR010465; Drf_DAD.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR036274; HR1_rpt_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR45691; PROTEIN DIAPHANOUS; 1.
DR   PANTHER; PTHR45691:SF6; PROTEIN DIAPHANOUS; 1.
DR   Pfam; PF03097; BRO1; 1.
DR   Pfam; PF06345; Drf_DAD; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   Pfam; PF02185; HR1; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM01041; BRO1; 1.
DR   SMART; SM01139; Drf_FH3; 1.
DR   SMART; SM01140; Drf_GBD; 1.
DR   SMART; SM00498; FH2; 1.
DR   SMART; SM00742; Hr1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   SUPFAM; SSF46585; HR1 repeat; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS51180; BRO1; 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS51860; REM_1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01207}; Reference proteome {ECO:0000313|Proteomes:UP000242457}.
FT   DOMAIN          57..414
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          594..993
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1014..1043
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   DOMAIN          1096..1170
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          1182..1571
FT                   /note="BRO1"
FT                   /evidence="ECO:0000259|PROSITE:PS51180"
FT   DOMAIN          1585..1664
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1031..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1669..1708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          439..480
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1147..1174
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1036..1058
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1677..1708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1736 AA;  196087 MW;  8578D1082AE45A9B CRC64;
     MANRKDKSST GFLDTWFGRP KKSGRGGGVR SGLGNNTIPR PHSGDDFNEI EQQRCIIERM
     DKETVNDKFE EMLANMNLTE EKKEPLRQQS EAKKREMLVL HYKGSIQENK SKFDKPADYI
     QYLAQPDLSV NKIYNCIESL RIALTNNPLS WVQEFGTKGL KQVLATLNEC YRNDNRYERI
     QYECIRCLKA IMNNTVGIKE MLAHQEALTI VARSLEPTKP SVMSEAVKLL GAVCLISSDS
     HKKVLDAITM NGEFKGRERF LPIVQGLMNK KNENLRVECL QLINSIISSA EELDFRLHLR
     NEIMRVGLAD ILETLEKNES EDLARHLKIF NDHKEEDYEE FVQRFDHVRL ELDDVNDCFE
     VIKNMVMETS AEPYFLSILQ HLLFVRDDAL VRPAYYKLIE ECVSQIVLHR SGCDPDFSAT
     KRFQIDVQPL IDTLVEKSRV EEERRLVEVL QKLEEAIASK QEAEAKLQHA ENKIRELEQG
     GIKSTNGNAK IGSVLSGLTG IGNLPPPPPP LPNASGSGII IAPPPPPPPP LPGGLCPPPP
     PLPGLGGPPP PPMPGMLAGP KPPPMPQSGP LPPMMAGINS AINTSQSLPL GLKPKKKWEV
     DAPLKRANWK AIMPHKLTEK SFWIKVQEDK LASPEILNGL SLKFASKPSG KKIDDVVDKS
     AASKKVKDLK VLDGKAAQNI LILLNGTLKH MSYEEVKSCL LKCEGPVISD NILQGLIQYL
     PPPDQLKKLH FYKDQYDDLT EAEQFCITIS TIKRLLPRLR SLSFMLRYEE LVQDVKPDIV
     AGTAACEEVK DSKKFARILE LILLLGNYMN SGSKNGQAFG FEISFLTKLT STKDVDNKQT
     LMHYLVDTIE QKFSECLSFT EELAHVDRAS RVSLENVQRT LRQMDSSIRN LEQDLSNAKI
     PQSDEDMFLH VMGPFAKKAR ESYEVLQNMF KNMDSLYTEI SEFFSFDKQK YTIEEFFGDI
     KTFKDDFMQA QKEIIKMRET EEKQRRAREA REKAEAEKAA RVARKIALVD MNAHETQEGV
     MDSLMEALQT GSAFSRPDQR RKRQTRAAGA ERRAQLNRSR SRTGLVGTGL LGRELSTIYL
     HYKLKLHVQL IVQGSDPRVA TCRGKLQNKR SKLNQEINKE LRLRAGAENL FKATTNRKLR
     ETVALELSFV NSNLQLLKEQ LAELNSSVEL YQNGDSEEPA MPMIPLGLKE TKDIDFQDPF
     KDFILEHYSE DGVNYEEAIA DLMETRQATR TPTRDTAGIA LLLRYYNQLY FVERRFFPPD
     RSLGIYFEWF DSLTGVPSCQ RTVAFEKASI LFNAAALYTQ LAAKQDRLST RGLDQAIDAF
     LRAAGTFRYI YENFTNAPSM DLGPDMLEML VQLMLAQARE CLFEKLELQS KDGRSIDVSL
     DLAQEASQVA AVYSDVHGLI SREPVRDYVP ETWISLILVK REHHMALAHK HLALGLFDRS
     ISEWRAETKL ALEHIQKSDG KTQLDIIVPR EENERKLLAK AHLREALVLH EESQRLQRMC
     RDLKAKQALA KVLKRIQEST VEDYNGIKNE DDFRELDPPD IIASTKFQLS ITHPDFGQHG
     VEDLFKSLGP VAIFSAKRHW TAPRLIQLQR GPEGEGFGFS VRGDSPVIIA AVDHNSLADL
     GGMKEGDFIV GIGDKDVKWS SHEQVVRLIK QSGDFINLKL VTPMDRNYLK KPGKINQQDK
     GSVSASSSSG ISSGQPSPAG SVTTAHVTKK LPWNPFKKSA TQRDSRDLTF DNVILR
//
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