ID   DBNLB_XENLA             Reviewed;         376 AA.
AC   Q6GM14;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Drebrin-like protein B;
GN   Name=dbnl-b;
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=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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}.
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DR   EMBL; BC074277; AAH74277.1; -; mRNA.
DR   RefSeq; NP_001086163.1; NM_001092694.1.
DR   AlphaFoldDB; Q6GM14; -.
DR   SMR; Q6GM14; -.
DR   PRIDE; Q6GM14; -.
DR   GeneID; 444592; -.
DR   KEGG; xla:444592; -.
DR   CTD; 444592; -.
DR   Xenbase; XB-GENE-494570; dbnl.S.
DR   OrthoDB; 885776at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 444592; Expressed in brain 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; 2.
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..376
FT                   /note="Drebrin-like protein B"
FT                   /id="PRO_0000348227"
FT   DOMAIN          2..133
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   DOMAIN          317..376
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          202..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          175..231
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        202..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   376 AA;  42767 MW;  60205DE3FCCBA267 CRC64;
     MSVNLSKNGA ALQAAYKDVL DEKTKTDWAL YTYEGNSNDI RLAETGDGGL EELVEELSSG
     KVMYAFCRVK DPNSGLPKFV LINWTGEGVK DARKGMCANH VSTMASFLKG AHVTINARAE
     EDVEPESIME KVAKASGANY NFHKESNRGN EGPQGPVGSV YQKTNAMSEI KRVGKENFWA
     KAEKDEEERR IEEHRRANVE KDRLERERKE REQREAEERE RRFRERSKEI DGHRKQQEEV
     EKQQTVPASQ RSVNPREMFL QKERSLPESG SVSAQPEQFT ASQQEEENIY QDATENQNIY
     EDTPQEDPVY ETGVAEDSGM CARALYDYQA ADDTEISFDP DDVIIQIEMI DDGWWRGVAP
     SGHFGMFPAN YVELLE