ADF1_CAEEL
ID ADF1_CAEEL Reviewed; 212 AA.
AC Q07750; Q9UAU4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Actin-depolymerizing factor 1, isoforms a/b;
DE AltName: Full=Uncoordinated protein 60;
GN Name=unc-60; ORFNames=C38C3.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8107682; DOI=10.1007/bf00280425;
RA McKim K.S., Matheson C., Marra M.A., Wakarchuk M.F., Baillie D.L.;
RT "The Caenorhabditis elegans unc-60 gene encodes proteins homologous to a
RT family of actin-binding proteins.";
RL Mol. Gen. Genet. 242:346-357(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND INTERACTION WITH F-ACTIN.
RX PubMed=17684058; DOI=10.1242/jcs.013516;
RA Yamashiro S., Gimona M., Ono S.;
RT "UNC-87, a calponin-related protein in C. elegans, antagonizes ADF/cofilin-
RT mediated actin filament dynamics.";
RL J. Cell Sci. 120:3022-3033(2007).
CC -!- FUNCTION: Depolymerizes growing actin filaments in muscle cells;
CC required for the assembly of actin filaments into the functional
CC contractile myofilament lattice of muscle (PubMed:8107682). Competes
CC with unc-87 for actin binding and inhibits the actin-bundling activity
CC of unc-87 (PubMed:17684058). {ECO:0000269|PubMed:17684058,
CC ECO:0000303|PubMed:8107682}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000269|PubMed:17684058}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Isoforms only share an exon that codes for the initiator
CC Met.;
CC Name=b;
CC IsoId=Q07750-2; Sequence=Displayed;
CC Name=a; Synonyms=ADF1;
CC IsoId=Q07750-1; Sequence=VSP_020111, VSP_020112;
CC Name=c; Synonyms=ADF2;
CC IsoId=Q07749-1; Sequence=External;
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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; L18963; AAC14458.1; -; Genomic_DNA.
DR EMBL; FO080816; CCD67021.1; -; Genomic_DNA.
DR EMBL; FO080816; CCD67022.1; -; Genomic_DNA.
DR PIR; S41728; S41728.
DR RefSeq; NP_503425.2; NM_071024.5. [Q07750-1]
DR PDB; 2MP4; NMR; -; A=1-156.
DR PDBsum; 2MP4; -.
DR AlphaFoldDB; Q07750; -.
DR BMRB; Q07750; -.
DR SMR; Q07750; -.
DR BioGRID; 43707; 65.
DR IntAct; Q07750; 2.
DR STRING; 6239.C38C3.5b.2; -.
DR EPD; Q07750; -.
DR PaxDb; Q07750; -.
DR PeptideAtlas; Q07750; -.
DR PRIDE; Q07750; -.
DR EnsemblMetazoa; F53E2.2.1; F53E2.2.1; WBGene00302980. [Q07750-1]
DR GeneID; 41657006; -.
DR KEGG; cel:CELE_F53E2.2; -.
DR UCSC; C38C3.5b.1; c. elegans. [Q07750-1]
DR CTD; 41657006; -.
DR WormBase; C38C3.5a; CE20547; WBGene00006794; unc-60. [Q07750-1]
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR InParanoid; Q07750; -.
DR OrthoDB; 1370477at2759; -.
DR PhylomeDB; Q07750; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00302980; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IPI:WormBase.
DR GO; GO:0005865; C:striated muscle thin filament; IDA:WormBase.
DR GO; GO:0051015; F:actin filament binding; IDA:WormBase.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:WormBase.
DR GO; GO:0030043; P:actin filament fragmentation; IBA:GO_Central.
DR GO; GO:0051014; P:actin filament severing; IDA:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0071689; P:muscle thin filament assembly; IMP:WormBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:WormBase.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:WormBase.
DR CDD; cd11286; ADF_cofilin_like; 1.
DR Gene3D; 3.40.20.10; -; 2.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR017904; ADF/Cofilin.
DR PANTHER; PTHR11913; PTHR11913; 2.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Reference proteome.
FT CHAIN 1..212
FT /note="Actin-depolymerizing factor 1, isoforms a/b"
FT /id="PRO_0000214938"
FT DOMAIN 3..159
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT VAR_SEQ 157..165
FT /note="NCPDNAPVR -> KLGEKYGDH (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_020111"
FT VAR_SEQ 166..212
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_020112"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:2MP4"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2MP4"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:2MP4"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2MP4"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2MP4"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:2MP4"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:2MP4"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:2MP4"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:2MP4"
FT STRAND 82..92
FT /evidence="ECO:0007829|PDB:2MP4"
FT STRAND 98..109
FT /evidence="ECO:0007829|PDB:2MP4"
FT HELIX 116..133
FT /evidence="ECO:0007829|PDB:2MP4"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2MP4"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:2MP4"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:2MP4"
SQ SEQUENCE 212 AA; 23578 MW; 30616B9CC8F9D716 CRC64;
MSSGVMVDPD VQTSFQKLSE GRKEYRYIIF KIDENKVIVE AAVTQDQLGI TGDDYDDSSK
AAFDKFVEDV KSRTDNLTDC RYAVFDFKFT CSRVGAGTSK MDKIIFLQIC PDGASIKKKM
VYASSAAAIK TSLGTGKILQ FQVSDESEMS HKELLNNCPD NAPVRRRMLY ASSVRALKAS
LGLESLFQVQ ASEMSDLDEK SVKSDLMSNQ RI
