DBNL_DICDI
ID DBNL_DICDI Reviewed; 481 AA.
AC Q557J6; Q6T3S4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Drebrin-like protein;
DE AltName: Full=Actin-binding protein 1;
DE Short=Dabp1;
DE AltName: Full=Actin-binding protein E;
GN Name=abpE-1; Synonyms=abp1-1; ORFNames=DDB_G0273447;
GN and
GN Name=abpE-2; Synonyms=abp1-2; ORFNames=DDB_G0273517;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA de la Roche M.A., Cote G.P.;
RT "Dictyostelium Dabp1 tethers PakB to the actin cytoskeleton.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16449327; DOI=10.1242/jcs.02742;
RA Wang Y., O'Halloran T.J.;
RT "Abp1 regulates pseudopodium number in chemotaxing Dictyostelium cells.";
RL J. Cell Sci. 119:702-710(2006).
CC -!- FUNCTION: Actin-binding adapter protein. Binds to F-actin but is not
CC involved in actin polymerization, capping or bundling. Does not bind G-
CC actin. Controls pseudopodium number and motility in early stages of
CC chemotactic aggregation. {ECO:0000269|PubMed:16449327}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16449327}. Cell projection, pseudopodium
CC {ECO:0000269|PubMed:16449327}.
CC -!- DOMAIN: The SH3 domain mediates the control of pseudopodium number.
CC -!- SIMILARITY: Belongs to the ABP1 family. {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; AY437927; AAR26472.1; -; mRNA.
DR EMBL; AAFI02000010; EAL70678.1; -; Genomic_DNA.
DR EMBL; AAFI02000010; EAL70713.1; -; Genomic_DNA.
DR RefSeq; XP_644611.1; XM_639519.1.
DR RefSeq; XP_644639.1; XM_639547.1.
DR AlphaFoldDB; Q557J6; -.
DR SMR; Q557J6; -.
DR STRING; 44689.DDB0201562; -.
DR PaxDb; Q557J6; -.
DR EnsemblProtists; EAL70678; EAL70678; DDB_G0273447.
DR EnsemblProtists; EAL70713; EAL70713; DDB_G0273517.
DR GeneID; 8618975; -.
DR GeneID; 8619002; -.
DR KEGG; ddi:DDB_G0273447; -.
DR KEGG; ddi:DDB_G0273517; -.
DR dictyBase; DDB_G0273447; abpE-1.
DR dictyBase; DDB_G0273517; abpE-2.
DR eggNOG; KOG3655; Eukaryota.
DR HOGENOM; CLU_567948_0_0_1; -.
DR InParanoid; Q557J6; -.
DR OMA; HYASQYD; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DDI-9013407; RHOH GTPase cycle.
DR Reactome; R-DDI-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DDI-9013422; RHOBTB1 GTPase cycle.
DR PRO; PR:Q557J6; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0097203; C:phagocytic cup lip; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; ISS:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0032037; F:myosin I heavy chain binding; IPI:dictyBase.
DR GO; GO:0005522; F:profilin binding; IPI:dictyBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:dictyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IGI:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IGI:dictyBase.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0090382; P:phagosome maturation; IMP:dictyBase.
DR GO; GO:0031269; P:pseudopodium assembly; IMP:dictyBase.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR Pfam; PF00018; SH3_1; 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 projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome; SH3 domain.
FT CHAIN 1..481
FT /note="Drebrin-like protein"
FT /id="PRO_0000348228"
FT DOMAIN 3..131
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 422..481
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 217..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 55338 MW; 0DA341CED0A949C9 CRC64;
MASLDISDPD ITKYIKLVQD GNPANRWIVF SYVPKSNNKI KFCDSGSGDL KELREELDDS
SIRFAYIRFV INNMPKFVYI PWCGDGVNGP IKGAFSGHAI EFSKSFKPIH HQVNARSEED
IDEKAITAAL NKATGASYDS GSKVQGATKG TFIPQSVSQG REAATKSNAE VKNVINKNDY
NKIQESAEYW KQNQANKSEP AKPTRPEYNL STERDDYWKQ QQAEKQKQQQ QQQQQQASRV
NAPPPSRTVG NKFQEQVSKP TETAPPQPRP APSKGSVLNR FPAATQQQQE PPAPSRPAAP
VPSRVNKPAA PVQPVYQEPV HEEPQYEEPQ YEEEQQQQYE EQPTEEQQYY QEEPQQQYEE
QPTEEQQYYQ EEQQQYEEQP TEEQQYYQEE QQQYEQPTED QQYYQEEQQQ YEQPAEEQYD
QSGYLQAKAL YDYNGENDGD LSFREGDIIT ILDQSDPDGW WQGSLPTGEQ GFFPSNFVQQ
L
