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Database: UniProt
Entry: A0A0M4EZR4_DROBS
LinkDB: A0A0M4EZR4_DROBS
Original site: A0A0M4EZR4_DROBS 
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}.
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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
//
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