DBNL_RAT
ID DBNL_RAT Reviewed; 436 AA.
AC Q9JHL4; Q9JM66; Q9JM67; Q9JM74;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Drebrin-like protein;
DE AltName: Full=Actin-binding protein 1;
DE Short=Abp1;
DE AltName: Full=SH3 domain-containing protein 7;
GN Name=Dbnl {ECO:0000312|EMBL:AAH72483.1};
GN Synonyms=Sh3p7 {ECO:0000312|EMBL:BAA90867.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA90867.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Hippocampus {ECO:0000312|EMBL:BAA90867.1};
RX PubMed=11595038; DOI=10.1046/j.0953-816x.2001.01727.x;
RA Yamazaki H., Takahashi H., Aoki T., Shirao T.;
RT "Molecular cloning and dendritic localization of rat SH3P7.";
RL Eur. J. Neurosci. 14:998-1008(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, INTERACTION WITH DNM1 AND SYN1, AND SUBCELLULAR LOCATION.
RX PubMed=11309416; DOI=10.1083/jcb.153.2.351;
RA Kessels M.M., Engqvist-Goldstein A.E., Drubin D.G., Qualmann B.;
RT "Mammalian Abp1, a signal-responsive F-actin-binding protein, links the
RT actin cytoskeleton to endocytosis via the GTPase dynamin.";
RL J. Cell Biol. 153:351-366(2001).
RN [4]
RP INTERACTION WITH SHANK2 AND SHANK3, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15014124; DOI=10.1523/jneurosci.5479-03.2004;
RA Qualmann B., Boeckers T.M., Jeromin M., Gundelfinger E.D., Kessels M.M.;
RT "Linkage of the actin cytoskeleton to the postsynaptic density via direct
RT interactions of Abp1 with the ProSAP/Shank family.";
RL J. Neurosci. 24:2481-2495(2004).
RN [5]
RP FUNCTION, INTERACTION WITH COBL AND PACSIN1, AND TISSUE SPECIFICITY.
RX PubMed=17956734; DOI=10.1016/j.cell.2007.08.030;
RA Ahuja R., Pinyol R., Reichenbach N., Custer L., Klingensmith J.,
RA Kessels M.M., Qualmann B.;
RT "Cordon-bleu is an actin nucleation factor and controls neuronal
RT morphology.";
RL Cell 131:337-350(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WASL.
RX PubMed=17476322; DOI=10.1371/journal.pone.0000400;
RA Pinyol R., Haeckel A., Ritter A., Qualmann B., Kessels M.M.;
RT "Regulation of N-WASP and the Arp2/3 complex by Abp1 controls neuronal
RT morphology.";
RL PLoS ONE 2:E400-E400(2007).
RN [7]
RP FUNCTION, INTERACTION WITH COBL, AND SUBCELLULAR LOCATION.
RX PubMed=23223303; DOI=10.1523/jneurosci.0843-12.2012;
RA Haag N., Schwintzer L., Ahuja R., Koch N., Grimm J., Heuer H., Qualmann B.,
RA Kessels M.M.;
RT "The actin nucleator Cobl is crucial for Purkinje cell development and
RT works in close conjunction with the F-actin binding protein Abp1.";
RL J. Neurosci. 32:17842-17856(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291; THR-299 AND SER-311, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Adapter protein that binds F-actin and DNM1, and thereby
CC plays a role in receptor-mediated endocytosis. Required for the
CC formation of organized podosome rosettes. May act as a common effector
CC of antigen receptor-signaling pathways in leukocytes. Acts as a key
CC component of the immunological synapse that regulates T-cell activation
CC by bridging TCRs and the actin cytoskeleton to gene activation and
CC endocytic processes (By similarity). Plays a role in the reorganization
CC of the actin cytoskeleton, formation of cell projections, such as
CC neurites, in neuron morphogenesis and synapse formation via its
CC interaction with WASL and COBL. Does not bind G-actin and promote actin
CC polymerization by itself. {ECO:0000250, ECO:0000269|PubMed:11309416,
CC ECO:0000269|PubMed:17476322, ECO:0000269|PubMed:17956734,
CC ECO:0000269|PubMed:23223303}.
CC -!- SUBUNIT: Interacts with FGD1, MAP4K1 and PRAM1 (By similarity).
CC Interacts with ANKRD54. Interacts with WASL and WIPF1 (By similarity).
CC Interacts with SHANK2 and SHANK3. Interacts with both COBL and PACSIN1.
CC Interacts with DNM1 and SYN1. {ECO:0000250,
CC ECO:0000269|PubMed:11309416, ECO:0000269|PubMed:15014124,
CC ECO:0000269|PubMed:17476322, ECO:0000269|PubMed:17956734,
CC ECO:0000269|PubMed:23223303}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23223303}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:23223303}. Cell projection, ruffle
CC {ECO:0000269|PubMed:23223303}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:23223303}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:23223303}. Cell membrane
CC {ECO:0000269|PubMed:23223303}; Peripheral membrane protein; Cytoplasmic
CC side. Synapse {ECO:0000269|PubMed:15014124}. Perikaryon
CC {ECO:0000250|UniProtKB:Q62418}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q62418}. Cell projection, dendrite
CC {ECO:0000269|PubMed:15014124}. Postsynaptic density
CC {ECO:0000269|PubMed:15014124}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane protein;
CC Cytoplasmic side. Cell projection, podosome
CC {ECO:0000250|UniProtKB:Q62418}. Early endosome
CC {ECO:0000250|UniProtKB:Q9UJU6}. Note=Associates with lamellipodial
CC actin and membrane ruffles. Colocalizes with actin and cortactin at
CC podosome dots and podosome rosettes. {ECO:0000269|PubMed:23223303}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:11595038}; Synonyms=SH3P7r1
CC {ECO:0000303|PubMed:11595038};
CC IsoId=Q9JHL4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11595038}; Synonyms=SH3PQ624187r2
CC {ECO:0000303|PubMed:11595038};
CC IsoId=Q9JHL4-2; Sequence=VSP_050792;
CC Name=3 {ECO:0000269|PubMed:11595038}; Synonyms=SH3P7r3
CC {ECO:0000303|PubMed:11595038};
CC IsoId=Q9JHL4-3; Sequence=VSP_050791;
CC Name=4 {ECO:0000269|PubMed:11595038}; Synonyms=SH3P7r4
CC {ECO:0000303|PubMed:11595038};
CC IsoId=Q9JHL4-4; Sequence=VSP_050791, VSP_050793;
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level). Widely
CC expressed in brain with highest levels in hippocampus and cerebral
CC cortex. Located primarily in dendrites and, in moderate amounts, in
CC cell bodies. Isoform 1 and isoform 3 are the predominant isoforms in
CC brain. {ECO:0000269|PubMed:11595038, ECO:0000269|PubMed:15014124,
CC ECO:0000269|PubMed:17956734}.
CC -!- DOMAIN: The SH3 domain mediates interaction with SHANK2, SHANK3 and
CC PRAM1.
CC -!- SIMILARITY: Belongs to the ABP1 family. {ECO:0000305}.
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DR EMBL; AB038364; BAA90866.1; -; mRNA.
DR EMBL; AB038365; BAA90867.1; -; mRNA.
DR EMBL; AB039818; BAA92708.1; -; mRNA.
DR EMBL; AB039819; BAA92709.1; -; mRNA.
DR EMBL; AB009346; BAA90819.1; -; mRNA.
DR EMBL; BC072483; AAH72483.1; -; mRNA.
DR RefSeq; NP_001264140.1; NM_001277211.1. [Q9JHL4-1]
DR RefSeq; NP_001264141.1; NM_001277212.1. [Q9JHL4-3]
DR RefSeq; NP_001264142.1; NM_001277213.1. [Q9JHL4-4]
DR RefSeq; NP_112642.1; NM_031352.2. [Q9JHL4-2]
DR AlphaFoldDB; Q9JHL4; -.
DR SMR; Q9JHL4; -.
DR BioGRID; 249745; 3.
DR IntAct; Q9JHL4; 2.
DR MINT; Q9JHL4; -.
DR STRING; 10116.ENSRNOP00000017375; -.
DR iPTMnet; Q9JHL4; -.
DR PhosphoSitePlus; Q9JHL4; -.
DR jPOST; Q9JHL4; -.
DR PaxDb; Q9JHL4; -.
DR PRIDE; Q9JHL4; -.
DR Ensembl; ENSRNOT00000017375; ENSRNOP00000017375; ENSRNOG00000012378. [Q9JHL4-1]
DR GeneID; 83527; -.
DR KEGG; rno:83527; -.
DR UCSC; RGD:70941; rat. [Q9JHL4-1]
DR CTD; 28988; -.
DR RGD; 70941; Dbnl.
DR eggNOG; KOG3655; Eukaryota.
DR GeneTree; ENSGT00940000156732; -.
DR HOGENOM; CLU_013085_0_1_1; -.
DR InParanoid; Q9JHL4; -.
DR OMA; TNIDMVD; -.
DR OrthoDB; 885776at2759; -.
DR PhylomeDB; Q9JHL4; -.
DR TreeFam; TF318935; -.
DR Reactome; R-RNO-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9JHL4; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000012378; Expressed in spleen and 19 other tissues.
DR Genevisible; Q9JHL4; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
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:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
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; IDA:RGD.
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:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
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:0016601; P:Rac protein signal transduction; ISS:UniProtKB.
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; PF14604; SH3_9; 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 1: Evidence at protein level;
KW Acetylation; Actin-binding; Adaptive immunity; Alternative splicing;
KW Cell junction; 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..436
FT /note="Drebrin-like protein"
FT /id="PRO_0000079795"
FT DOMAIN 2..133
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 377..436
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 185..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 178..232
FT /evidence="ECO:0000255"
FT COMPBIAS 185..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 367..368
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 277
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 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 296
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 340
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62418"
FT MOD_RES 350
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62418"
FT VAR_SEQ 235..238
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11595038"
FT /id="VSP_050791"
FT VAR_SEQ 236..238
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11595038"
FT /id="VSP_050792"
FT VAR_SEQ 256
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11595038"
FT /id="VSP_050793"
SQ SEQUENCE 436 AA; 48613 MW; 064CA1E6BAF84444 CRC64;
MAVNLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EELVEELNSG
KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACANH VSTMANFLKG AHVTINARAE
EDVEPECIME KVAKASGANY SFHKESSCFQ DVGPQAPVGS VYQKTNAVSE IKRVGKDNFW
AKAEKEEENR RLEEKRRAEE EKQRLEEERR ERELQEAARR EQRYQEQHRS AGPPSPSSRT
GELEQEVVSR SRQEWESAGQ QAPHPREIFK QKERAMSTTS VSSSQPGKLR SPFLQKQFTQ
PEASYGREPT SPVSRPAAGV CEELAPSTPP SAQTDDEPTY EVPSEQETLY EEPPPVQQPG
AGSGHIDNYM QSQDLSGQGL CARALYDYQA ADDTEISFDP ENLITGIEVI DEGWWRGYGP
DGHFGMFPAN YVELIE
