DREB_CHICK
ID DREB_CHICK Reviewed; 652 AA.
AC P18302; Q91358; Q91359;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Drebrin;
DE AltName: Full=Developmentally-regulated brain protein;
GN Name=DBN1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS E1 AND E2).
RC TISSUE=Brain;
RX PubMed=3208110; DOI=10.1016/0169-328x(88)90027-7;
RA Kojima N., Kato Y., Shirao T., Obata K.;
RT "Nucleotide sequences of two embryonic drebrins, developmentally regulated
RT brain proteins, and developmental change in their mRNAs.";
RL Brain Res. 464:207-215(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A).
RX PubMed=8361332; DOI=10.1016/0169-328x(93)90154-h;
RA Kojima N., Shirao T., Obata K.;
RT "Molecular cloning of a developmentally regulated brain protein, chicken
RT drebrin A and its expression by alternative splicing of the drebrin gene.";
RL Brain Res. Mol. Brain Res. 19:101-114(1993).
CC -!- FUNCTION: Actin cytoskeleton-organizing protein that plays a role in
CC the formation of cell projections (By similarity). Plays a role in
CC dendritic spine morphogenesis and organization, including the
CC localization of the dopamine receptor DRD1 to the dendritic spines (By
CC similarity). Involved in synaptic plasticity (By similarity).
CC {ECO:0000250|UniProtKB:Q16643, ECO:0000250|UniProtKB:Q9QXS6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16643}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:Q16643}. Cytoplasm, cell
CC cortex {ECO:0000250|UniProtKB:Q16643}. Cell junction
CC {ECO:0000250|UniProtKB:Q16643}. Cell projection
CC {ECO:0000250|UniProtKB:Q9QXS6}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9QXS6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=P18302-1; Sequence=Displayed;
CC Name=E1;
CC IsoId=P18302-2; Sequence=VSP_004196;
CC Name=E2;
CC IsoId=P18302-3; Sequence=VSP_004197;
CC -!- TISSUE SPECIFICITY: Brain neurons.
CC -!- MISCELLANEOUS: Drebrins are classified into two forms of the embryonic
CC type (E1 and E2) and one form of the adult type (A). The time course of
CC their appearance are different from each other. Their structures are
CC closely related.
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; M36961; AAA48750.1; -; mRNA.
DR EMBL; S65296; AAB28012.1; -; Genomic_DNA.
DR EMBL; S65279; AAB28012.1; JOINED; Genomic_DNA.
DR EMBL; S65280; AAB28012.1; JOINED; Genomic_DNA.
DR EMBL; S65281; AAB28012.1; JOINED; Genomic_DNA.
DR EMBL; S65288; AAB28012.1; JOINED; Genomic_DNA.
DR EMBL; S65289; AAB28012.1; JOINED; Genomic_DNA.
DR EMBL; S65290; AAB28012.1; JOINED; Genomic_DNA.
DR EMBL; S65291; AAB28012.1; JOINED; Genomic_DNA.
DR EMBL; S65292; AAB28012.1; JOINED; Genomic_DNA.
DR EMBL; S65294; AAB28012.1; JOINED; Genomic_DNA.
DR EMBL; S65267; AAB28011.2; -; mRNA.
DR EMBL; S65230; AAB28010.1; -; mRNA.
DR PIR; A43776; A43776.
DR PIR; I51213; I51213.
DR RefSeq; NP_990830.1; NM_205499.1.
DR AlphaFoldDB; P18302; -.
DR SMR; P18302; -.
DR STRING; 9031.ENSGALP00000042083; -.
DR PRIDE; P18302; -.
DR Ensembl; ENSGALT00000062237; ENSGALP00000057425; ENSGALG00000033405. [P18302-1]
DR Ensembl; ENSGALT00000078180; ENSGALP00000056255; ENSGALG00000033405. [P18302-2]
DR GeneID; 396496; -.
DR KEGG; gga:396496; -.
DR CTD; 1627; -.
DR VEuPathDB; HostDB:geneid_396496; -.
DR eggNOG; KOG3655; Eukaryota.
DR GeneTree; ENSGT00940000159431; -.
DR InParanoid; P18302; -.
DR OMA; FAQSDEC; -.
DR OrthoDB; 885776at2759; -.
DR PhylomeDB; P18302; -.
DR Reactome; R-GGA-9013405; RHOD GTPase cycle.
DR Reactome; R-GGA-9013407; RHOH GTPase cycle.
DR Reactome; R-GGA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-GGA-9013422; RHOBTB1 GTPase cycle.
DR PRO; PR:P18302; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000033405; Expressed in brain and 10 other tissues.
DR ExpressionAtlas; P18302; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
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:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR028438; Drebrin.
DR PANTHER; PTHR10829:SF1; PTHR10829:SF1; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Alternative splicing; Cell junction;
KW Cell projection; Cytoplasm; Developmental protein; Differentiation;
KW Neurogenesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..652
FT /note="Drebrin"
FT /id="PRO_0000080007"
FT DOMAIN 5..134
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REGION 211..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 307..405
FT /note="Missing (in isoform E2)"
FT /evidence="ECO:0000303|PubMed:3208110"
FT /id="VSP_004197"
FT VAR_SEQ 317..362
FT /note="Missing (in isoform E1)"
FT /evidence="ECO:0000303|PubMed:3208110"
FT /id="VSP_004196"
FT CONFLICT 552
FT /note="E -> EE (in Ref. 1; AAA48750/AAB28011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 652 AA; 71535 MW; 8EF72CA549833E65 CRC64;
MAGVGFAAHR LELLASYQDV IGEDSPTDWA LYTYEDGSDD LKLAASGGGG LLELSGHFEI
QKVMYGFCSV KEPQAVLPKY VLVNWVGEDV PDARKCACAS HVAKIAEFFQ GVDVIVNASS
VEDIDPGAIG QRLSNGLARV SSPVLHRLRL REDENAEPVG TTYQKTDATV EMKRLNREQF
WEQAKKEEEL RKEEERKKAL DARLRFEQER MEQERLEQEE RERRYREREE QIEEHRRKQQ
SMEAEEARQR LKEQSIFGEQ QEEDDRQQLR KSESEVEEAA AIIAQRPDNP REFFKQQERV
ASGSGDAISP GSHRTGRLHC PFIKTADSGP PSSSSSSSSP PRTPFPYITC HRTPNLSSFF
PCSQSDYRKV SAAGCSPCES SPASTPLGEQ RTRAPAEETP ATPKDSPSPS TQVAEPAATE
QHWPFPGPED KAAEPPGDEP DPDPRPAWTA GADVLGDLVT LEPSEPSPAP AASEPQPVET
PGVAEPLIEL WQSDGAAPAA TSTWPLPDTP AGPPVPPEEG TLLGLDELPE PPATFCDAEQ
HEEVEEEEEE EEATAGEPHP TGLGYQEGYQ EGPEVPPITN GEMGPKDGTA GRGEQASEGY
FSQSQEEEAP PPEEPSAKAP QPVFYNKPPE IDITCWDTDP LPEEEESFGG GL
