DBNLA_XENLA
ID DBNLA_XENLA Reviewed; 447 AA.
AC Q7ZXQ9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Drebrin-like protein A;
GN Name=dbnl-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adapter protein that binds F-actin and dynamin, and thereby
CC plays a role in receptor-mediated endocytosis. Plays a role in the
CC reorganization of the actin cytoskeleton, formation of cell
CC projections, such as neurites, in neuron morphogenesis and synapse
CC formation. Does not bind G-actin and promote actin polymerization by
CC itself, but excerts its functions by interaction with other proteins.
CC Required for the formation of organized podosome rosettes (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q62418}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q62418}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JHL4}. Synapse {ECO:0000250|UniProtKB:Q62418}.
CC Perikaryon {ECO:0000250|UniProtKB:Q62418}. Cell projection, neuron
CC projection {ECO:0000250|UniProtKB:Q62418}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9JHL4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q62418}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q62418}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q62418}. Cell projection, podosome
CC {ECO:0000250|UniProtKB:Q62418}. Early endosome
CC {ECO:0000250|UniProtKB:Q9UJU6}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9JHL4}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9JHL4}.
CC -!- SIMILARITY: Belongs to the ABP1 family. {ECO:0000305}.
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; BC044296; AAH44296.1; -; mRNA.
DR RefSeq; NP_001080114.1; NM_001086645.1.
DR AlphaFoldDB; Q7ZXQ9; -.
DR SMR; Q7ZXQ9; -.
DR DNASU; 379806; -.
DR GeneID; 379806; -.
DR KEGG; xla:379806; -.
DR CTD; 379806; -.
DR Xenbase; XB-GENE-17339832; dbnl.L.
DR OrthoDB; 885776at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 379806; Expressed in spleen and 20 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
DR GO; GO:0097178; P:ruffle assembly; IEA:InterPro.
DR GO; GO:0007416; P:synapse assembly; IEA:InterPro.
DR CDD; cd11960; SH3_Abp1_eu; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR029923; Dbnl.
DR InterPro; IPR035717; Drebrin-like_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10829:SF12; PTHR10829:SF12; 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; SSF50044; SSF50044; 1.
DR PROSITE; PS51263; ADF_H; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell junction; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endosome; Golgi apparatus;
KW Membrane; Reference proteome; SH3 domain; Synapse; Transport.
FT CHAIN 1..447
FT /note="Drebrin-like protein A"
FT /id="PRO_0000348226"
FT DOMAIN 2..133
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 388..447
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 141..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..245
FT /evidence="ECO:0000255"
FT COMPBIAS 184..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..329
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 50612 MW; 3BC6767EE6E3B521 CRC64;
MSVNLSKNGA ALQGAYKDVL DEKTKTDWAL YTYEGNSNDI RLAETGDGGL EELVEELSSG
KVMYAFCRVK DPNSGLPKFV LVNWTGEGVK DARKGACANH VSTMANFLKG AHVTINARAE
EDVEPESIME KVAKASGANY NFHKESKRGN EGPQGPVGSV YQKTNAMSEI KRVGKENFWA
KAEKDEEERR MEENRRANSE KDRLERERKE REQREAETRE QRFRERAKEI DAQRKEQEET
EKQQTVPASQ RSVNPRETFL QKERSLPESG PVSAQPGRLR SPFLQKSACQ PESSPPPSPV
HRVQEPPSPP VYPAHQTPPE SPVPPVSHPP ESTVHVKEQC TASQQEEENI YQDATEDQNI
YEDTTENQNI YEDTPQEEPV YEIEVEEEKG VCARALYDYQ AADDTEISFD PDDLITQIQF
IDEGWWRGFS PAGHFGMFPA NYVELLE
