ID A0A2C9M435_BIOGL Unreviewed; 545 AA.
AC A0A2C9M435;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Drebrin-like protein {ECO:0008006|Google:ProtNLM};
GN Name=106073898 {ECO:0000313|EnsemblMetazoa:BGLB038284-PC};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB038284-PC, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB038284-PC}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB038284-PC};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ABP1 family.
CC {ECO:0000256|ARBA:ARBA00011039}.
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DR RefSeq; XP_013090034.1; XM_013234580.1.
DR AlphaFoldDB; A0A2C9M435; -.
DR STRING; 6526.A0A2C9M435; -.
DR EnsemblMetazoa; BGLB038284-RC; BGLB038284-PC; BGLB038284.
DR KEGG; bgt:106073898; -.
DR VEuPathDB; VectorBase:BGLB038284; -.
DR OrthoDB; 101008at2759; -.
DR Proteomes; UP000076420; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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; PF14604; SH3_9; 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 SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 4..133
FT /note="ADF-H"
FT /evidence="ECO:0000259|PROSITE:PS51263"
FT DOMAIN 486..545
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 197..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 62799 MW; A89A783BA5523FDA CRC64;
MALDLRKNKD SLTNAYEKVI SDKDDTNWAL FGYEGQTTVL KVIETGNGGI EEMAEELSSG
KMLYAYCRVQ DPNTGLFKYV LIHWTGESVP ENLKLKYTSH LRDVQSFLKS IHVTFPARCE
EDIDEDEIVK KVAKSSGANY SFHKEQSKPV EPAGPVGTDY KRVVPTKEIN INSRDQFWAK
AEKEEIERQN AEKLRVEEER KKAEVERKER EMRETREREK KISEHSKEVT KLRQFEKKAE
VENRELEQKR WEQMQKESSI DENERGHRSD QLRKERAAEA AQLVSSSSTN ARDFFKQKSV
ERPSSVQKAL PPPKKIRGGF LENESNNTAA TPARKEPIKL PTSDESSSKP FRQPEPVRQQ
EPEPEPEPEA YSTYTEEQPS EPEQVSSPVF SHTPDLLRSN LPPRQDSDNE EDNEQEWNDS
KVEPPAEDFE FREKRVPSYH EDYSAETHHA DTQSHRVSGV QHYEEQEEEQ LEEVEATVPS
VNITPEMGKC ARALYDYQAS DDTEISFDPD QIITNIAEID DGWWQGFAPD GSYGMFPANY
VELIN
//
