DBNL_BOVIN
ID DBNL_BOVIN Reviewed; 423 AA.
AC A6H7G2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Drebrin-like protein;
GN Name=DBNL;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adapter protein that binds F-actin and DNM1, 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 via its interaction with WASL and COBL. Does not bind G-actin
CC and promote actin polymerization by itself. Required for the formation
CC of organized podosome rosettes. May act as a common effector of antigen
CC receptor-signaling pathways in leukocytes. Acts as a key component of
CC the immunological synapse that regulates T-cell activation by bridging
CC TCRs and the actin cytoskeleton to gene activation and endocytic
CC processes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SHANK2, SHANK3, SYN1 and PRAM1. Interacts with
CC FGD1, DNM1 and MAP4K1. Interacts with ANKRD54. Interacts with COBL.
CC Interacts with WASL and WIPF1 (By 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}. Note=Associates with lamellipodial
CC actin and membrane ruffles. Colocalizes with actin and cortactin at
CC podosome dots and podosome rosettes. {ECO:0000250|UniProtKB:Q62418,
CC ECO:0000250|UniProtKB:Q9JHL4}.
CC -!- DOMAIN: The SH3 domain mediates interaction with SHANK2, SHANK3 and
CC PRAM1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABP1 family. {ECO:0000305}.
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DR EMBL; BT030669; ABS44985.1; -; mRNA.
DR EMBL; BC146234; AAI46235.1; -; mRNA.
DR RefSeq; NP_001092440.1; NM_001098970.1.
DR AlphaFoldDB; A6H7G2; -.
DR SMR; A6H7G2; -.
DR STRING; 9913.ENSBTAP00000023325; -.
DR iPTMnet; A6H7G2; -.
DR PaxDb; A6H7G2; -.
DR PeptideAtlas; A6H7G2; -.
DR PRIDE; A6H7G2; -.
DR GeneID; 514706; -.
DR KEGG; bta:514706; -.
DR CTD; 28988; -.
DR eggNOG; KOG3655; Eukaryota.
DR HOGENOM; CLU_013085_0_1_1; -.
DR InParanoid; A6H7G2; -.
DR OrthoDB; 885776at2759; -.
DR TreeFam; TF318935; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0071800; P:podosome assembly; ISS:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; IBA:GO_Central.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IBA:GO_Central.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0097178; P:ruffle assembly; IEA:InterPro.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
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; PF00018; SH3_1; 1.
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 Acetylation; Actin-binding; Adaptive immunity; Cell junction;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Endosome; Golgi apparatus;
KW Immunity; Membrane; Phosphoprotein; Reference proteome; SH3 domain;
KW Synapse; Transport.
FT CHAIN 1..423
FT /note="Drebrin-like protein"
FT /id="PRO_0000348225"
FT DOMAIN 2..133
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 364..423
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 185..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..227
FT /evidence="ECO:0000255"
FT COMPBIAS 240..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 357..358
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62418"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 285
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 288
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 330
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62418"
FT MOD_RES 340
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62418"
SQ SEQUENCE 423 AA; 47723 MW; D938ED80B9517B38 CRC64;
MAVNLSRNGP ALLEAYQQVV NEKSSTDWAL FTYEGNSNDI RVAGTGEGGL EEMVEELNSG
KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACANH VSTMAGFLKG AHVTINARAE
EDVEPECIMQ KVARASGANY TFHKESSRFQ DTGPQAPVGS VYQKTNAVSE IKRVGKDSFW
AKAEKEEENR RLEEKRRAEE ERQQLEQERR ERELREAALR EQRYQEQGGE AGLQRKYEQH
EVLSRNREEQ PAHPREIFKQ KERAMSTTSI SSPQPGKLKS PFLQKQLTQP DTPISRESPH
ATSRPRADLR EEPVPSIPPC SVQVEEEAVY EEPPEQETFY EEPPAVQQQD ASSEPIDHYP
GLSGKGLCAR ALYDYQAADE TEISFDPENL ITGIEVIDEG WWRGYGPDGH FGMFPANYVE
LIE
