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Protein

Drebrin-like protein

Gene

Dbnl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Required for the formation of organized podosome rosettes. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself.By similarity4 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • protein C-terminus binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Endocytosis, Immunity, Transport

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-RNO-264870. Caspase-mediated cleavage of cytoskeletal proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Drebrin-like protein
Alternative name(s):
Actin-binding protein 1
Short name:
Abp1
SH3 domain-containing protein 7
Gene namesi
Name:DbnlImported
Synonyms:Sh3p7Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi70941. Dbnl.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • clathrin-coated vesicle membrane Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB-SubCell
  • dendrite Source: RGD
  • early endosome Source: UniProtKB-SubCell
  • extracellular exosome Source: Ensembl
  • Golgi membrane Source: UniProtKB-SubCell
  • lamellipodium Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • podosome Source: UniProtKB
  • postsynaptic density Source: RGD
  • ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endosome, Golgi apparatus, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Drebrin-like proteinPRO_0000079795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261PhosphothreonineBy similarity
Modified residuei176 – 1761N6-acetyllysineBy similarity
Modified residuei277 – 2771PhosphoserineBy similarity
Modified residuei280 – 2801PhosphoserineBy similarity
Modified residuei283 – 2831PhosphoserineBy similarity
Modified residuei291 – 2911PhosphoserineCombined sources
Modified residuei296 – 2961N6-acetyllysineBy similarity
Modified residuei299 – 2991PhosphothreonineCombined sources
Modified residuei311 – 3111PhosphoserineCombined sources
Modified residuei340 – 3401PhosphotyrosineBy similarity
Modified residuei350 – 3501PhosphotyrosineBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei367 – 3682Cleavage; by caspase-3By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9JHL4.
PRIDEiQ9JHL4.

PTM databases

iPTMnetiQ9JHL4.
PhosphoSiteiQ9JHL4.

Expressioni

Tissue specificityi

Detected in brain (at protein level). Widely expressed in brain with highest levels in hippocampus and cerebral cortex. Located primarily in dendrites and, in moderate amounts, in cell bodies. Isoform 1 and isoform 3 are the predominant isoforms in brain.3 Publications

Gene expression databases

GenevisibleiQ9JHL4. RN.

Interactioni

Subunit structurei

Interacts with FGD1, MAP4K1 and PRAM1 (By similarity). Interacts with ANKRD54. Interacts with WASL and WIPF1 (By similarity). Interacts with SHANK2 and SHANK3. Interacts with both COBL and PACSIN1. Interacts with DNM1 and SYN1.By similarity5 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • protein C-terminus binding Source: RGD

Protein-protein interaction databases

IntActiQ9JHL4. 2 interactions.
MINTiMINT-4568258.
STRINGi10116.ENSRNOP00000017375.

Structurei

3D structure databases

ProteinModelPortaliQ9JHL4.
SMRiQ9JHL4. Positions 1-133, 379-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 133132ADF-HPROSITE-ProRule annotationAdd
BLAST
Domaini377 – 43660SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili178 – 23255Sequence analysisAdd
BLAST

Domaini

The SH3 domain mediates interaction with SHANK2, SHANK3 and PRAM1.

Sequence similaritiesi

Belongs to the ABP1 family.Curated
Contains 1 ADF-H domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiKOG3655. Eukaryota.
ENOG410XRVX. LUCA.
GeneTreeiENSGT00530000062953.
HOGENOMiHOG000008567.
HOVERGENiHBG051316.
InParanoidiQ9JHL4.
OMAiGYEGQTN.
OrthoDBiEOG7X3QR9.
PhylomeDBiQ9JHL4.
TreeFamiTF318935.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR029923. Dbnl.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10829:SF12. PTHR10829:SF12. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q9JHL4-1) [UniParc]FASTAAdd to basket

Also known as: SH3P7r11 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAVNLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL
60 70 80 90 100
EELVEELNSG KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACANH
110 120 130 140 150
VSTMANFLKG AHVTINARAE EDVEPECIME KVAKASGANY SFHKESSCFQ
160 170 180 190 200
DVGPQAPVGS VYQKTNAVSE IKRVGKDNFW AKAEKEEENR RLEEKRRAEE
210 220 230 240 250
EKQRLEEERR ERELQEAARR EQRYQEQHRS AGPPSPSSRT GELEQEVVSR
260 270 280 290 300
SRQEWESAGQ QAPHPREIFK QKERAMSTTS VSSSQPGKLR SPFLQKQFTQ
310 320 330 340 350
PEASYGREPT SPVSRPAAGV CEELAPSTPP SAQTDDEPTY EVPSEQETLY
360 370 380 390 400
EEPPPVQQPG AGSGHIDNYM QSQDLSGQGL CARALYDYQA ADDTEISFDP
410 420 430
ENLITGIEVI DEGWWRGYGP DGHFGMFPAN YVELIE
Length:436
Mass (Da):48,613
Last modified:October 1, 2000 - v1
Checksum:i064CA1E6BAF84444
GO
Isoform 21 Publication (identifier: Q9JHL4-2) [UniParc]FASTAAdd to basket

Also known as: SH3PQ624187r21 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     236-238: Missing.

Show »
Length:433
Mass (Da):48,341
Checksum:i952FFF81E6A6EDAA
GO
Isoform 31 Publication (identifier: Q9JHL4-3) [UniParc]FASTAAdd to basket

Also known as: SH3P7r31 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     235-238: Missing.

Show »
Length:432
Mass (Da):48,254
Checksum:iE2D5E5C1D325B641
GO
Isoform 41 Publication (identifier: Q9JHL4-4) [UniParc]FASTAAdd to basket

Also known as: SH3P7r41 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     235-238: Missing.
     256-256: Missing.

Show »
Length:431
Mass (Da):48,125
Checksum:iC44CEABB3E41399E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei235 – 2384Missing in isoform 3 and isoform 4. 1 PublicationVSP_050791
Alternative sequencei236 – 2383Missing in isoform 2. 1 PublicationVSP_050792
Alternative sequencei256 – 2561Missing in isoform 4. 1 PublicationVSP_050793

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038364 mRNA. Translation: BAA90866.1.
AB038365 mRNA. Translation: BAA90867.1.
AB039818 mRNA. Translation: BAA92708.1.
AB039819 mRNA. Translation: BAA92709.1.
AB009346 mRNA. Translation: BAA90819.1.
BC072483 mRNA. Translation: AAH72483.1.
RefSeqiNP_001264140.1. NM_001277211.1. [Q9JHL4-1]
NP_001264141.1. NM_001277212.1. [Q9JHL4-3]
NP_001264142.1. NM_001277213.1. [Q9JHL4-4]
NP_112642.1. NM_031352.2. [Q9JHL4-2]
UniGeneiRn.4115.

Genome annotation databases

EnsembliENSRNOT00000017375; ENSRNOP00000017375; ENSRNOG00000012378. [Q9JHL4-1]
GeneIDi83527.
KEGGirno:83527.
UCSCiRGD:70941. rat. [Q9JHL4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038364 mRNA. Translation: BAA90866.1.
AB038365 mRNA. Translation: BAA90867.1.
AB039818 mRNA. Translation: BAA92708.1.
AB039819 mRNA. Translation: BAA92709.1.
AB009346 mRNA. Translation: BAA90819.1.
BC072483 mRNA. Translation: AAH72483.1.
RefSeqiNP_001264140.1. NM_001277211.1. [Q9JHL4-1]
NP_001264141.1. NM_001277212.1. [Q9JHL4-3]
NP_001264142.1. NM_001277213.1. [Q9JHL4-4]
NP_112642.1. NM_031352.2. [Q9JHL4-2]
UniGeneiRn.4115.

3D structure databases

ProteinModelPortaliQ9JHL4.
SMRiQ9JHL4. Positions 1-133, 379-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JHL4. 2 interactions.
MINTiMINT-4568258.
STRINGi10116.ENSRNOP00000017375.

PTM databases

iPTMnetiQ9JHL4.
PhosphoSiteiQ9JHL4.

Proteomic databases

PaxDbiQ9JHL4.
PRIDEiQ9JHL4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017375; ENSRNOP00000017375; ENSRNOG00000012378. [Q9JHL4-1]
GeneIDi83527.
KEGGirno:83527.
UCSCiRGD:70941. rat. [Q9JHL4-1]

Organism-specific databases

CTDi28988.
RGDi70941. Dbnl.

Phylogenomic databases

eggNOGiKOG3655. Eukaryota.
ENOG410XRVX. LUCA.
GeneTreeiENSGT00530000062953.
HOGENOMiHOG000008567.
HOVERGENiHBG051316.
InParanoidiQ9JHL4.
OMAiGYEGQTN.
OrthoDBiEOG7X3QR9.
PhylomeDBiQ9JHL4.
TreeFamiTF318935.

Enzyme and pathway databases

ReactomeiR-RNO-264870. Caspase-mediated cleavage of cytoskeletal proteins.

Miscellaneous databases

PROiQ9JHL4.

Gene expression databases

GenevisibleiQ9JHL4. RN.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR029923. Dbnl.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10829:SF12. PTHR10829:SF12. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and dendritic localization of rat SH3P7."
    Yamazaki H., Takahashi H., Aoki T., Shirao T.
    Eur. J. Neurosci. 14:998-1008(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY.
    Tissue: HippocampusImported.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Heart.
  3. "Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase dynamin."
    Kessels M.M., Engqvist-Goldstein A.E., Drubin D.G., Qualmann B.
    J. Cell Biol. 153:351-366(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DNM1 AND SYN1, SUBCELLULAR LOCATION.
  4. "Linkage of the actin cytoskeleton to the postsynaptic density via direct interactions of Abp1 with the ProSAP/Shank family."
    Qualmann B., Boeckers T.M., Jeromin M., Gundelfinger E.D., Kessels M.M.
    J. Neurosci. 24:2481-2495(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHANK2 AND SHANK3, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  5. "Cordon-bleu is an actin nucleation factor and controls neuronal morphology."
    Ahuja R., Pinyol R., Reichenbach N., Custer L., Klingensmith J., Kessels M.M., Qualmann B.
    Cell 131:337-350(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH COBL AND PACSIN1, TISSUE SPECIFICITY.
  6. "Regulation of N-WASP and the Arp2/3 complex by Abp1 controls neuronal morphology."
    Pinyol R., Haeckel A., Ritter A., Qualmann B., Kessels M.M.
    PLoS ONE 2:E400-E400(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH WASL.
  7. "The actin nucleator Cobl is crucial for Purkinje cell development and works in close conjunction with the F-actin binding protein Abp1."
    Haag N., Schwintzer L., Ahuja R., Koch N., Grimm J., Heuer H., Qualmann B., Kessels M.M.
    J. Neurosci. 32:17842-17856(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH COBL, SUBCELLULAR LOCATION.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291; THR-299 AND SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDBNL_RAT
AccessioniPrimary (citable) accession number: Q9JHL4
Secondary accession number(s): Q9JM66, Q9JM67, Q9JM74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.