ID A0A0M4EZR4_DROBS Unreviewed; 521 AA.
AC A0A0M4EZR4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=CG10083 {ECO:0000313|EMBL:ALC44250.1};
GN ORFNames=Dbus_chr3Lg1416 {ECO:0000313|EMBL:ALC44250.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC44250.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC44250.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC44250.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ABP1 family.
CC {ECO:0000256|ARBA:ARBA00011039}.
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; CP012525; ALC44250.1; -; Genomic_DNA.
DR RefSeq; XP_017843311.1; XM_017987822.1.
DR AlphaFoldDB; A0A0M4EZR4; -.
DR SMR; A0A0M4EZR4; -.
DR STRING; 30019.A0A0M4EZR4; -.
DR GeneID; 108600320; -.
DR OMA; FKEPRGA; -.
DR OrthoDB; 101008at2759; -.
DR Proteomes; UP000494163; Chromosome 3l sequence.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0044087; P:regulation of cellular component biogenesis; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR CDD; cd11281; ADF_drebrin_like; 1.
DR CDD; cd11960; SH3_Abp1_eu; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR035717; Drebrin-like_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1.
DR PANTHER; PTHR10829:SF25; DREBRIN-LIKE PROTEIN; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00102; ADF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF55753; Actin depolymerizing proteins; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51263; ADF_H; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 2..133
FT /note="ADF-H"
FT /evidence="ECO:0000259|PROSITE:PS51263"
FT DOMAIN 462..521
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 190..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 57823 MW; 30778DC5221C7EF5 CRC64;
MAISFEKHRA SIIDAWKDVL DDKSDTNWSL FGYEGQTNEL KVVGKGDGGV EELLEDLNSG
KIMYAFVRIE DPKTGLNKYL LINWQGEGAP VLRKGTCANH IHDVGKLLSG AHLTMNARNE
DDIDLERLLK KLSTVSSAYS FKEPRGAQEE QKLPVGTNYT RVIPTKDINA SVMQDFWKKE
EAEEQRRLVA EKEVKRQQQE NQDKEQRARE EKEHKEREKL VISTTKLQPA HVPIKTSPQP
LSPEKTAASS ANNLTEAERM RQARNQEARE LIGSRVGAAK AMFTKHTSEG QLQSKLNTQP
PAKPARNSIA QRINAFNQNQ TEETPAVPSP PRAVSPKAPP AALPVVAEQP VAAEVVSTVE
EDTQPIEDLP LAHESEQFST IKRSPHSKTN SVQSQSPDDT SSSNATDTAV YKEEEEEVRT
KVSVTVQQSQ AAKASGMSTL ERNALTDLVN EDDFICQDSL GDLGLRARAL YDYQAADESE
ITFDPGDVIT HIDQIDEGWW QGLGPDGTYG LFPANYVEII N
//