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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//