ADF2_CAEEL
ID ADF2_CAEEL Reviewed; 152 AA.
AC Q07749;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Actin-depolymerizing factor 2, isoform c;
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).
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.
CC {ECO:0000303|PubMed:8107682}.
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=c; Synonyms=ADF2;
CC IsoId=Q07749-1; Sequence=Displayed;
CC Name=a; Synonyms=ADF1;
CC IsoId=Q07750-1; Sequence=External;
CC Name=b;
CC IsoId=Q07750-2; Sequence=External;
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; L18963; AAC14457.1; -; Genomic_DNA.
DR EMBL; FO080816; CCD67023.1; -; Genomic_DNA.
DR PIR; S41727; S41727.
DR RefSeq; NP_503427.2; NM_071026.7. [Q07749-1]
DR PDB; 2LXX; NMR; -; A=1-152.
DR PDBsum; 2LXX; -.
DR AlphaFoldDB; Q07749; -.
DR BMRB; Q07749; -.
DR SMR; Q07749; -.
DR BioGRID; 43707; 65.
DR World-2DPAGE; 0011:Q07749; -.
DR EPD; Q07749; -.
DR PeptideAtlas; Q07749; -.
DR EnsemblMetazoa; C38C3.5.1; C38C3.5.1; WBGene00006794. [Q07749-1]
DR GeneID; 178640; -.
DR KEGG; cel:CELE_C38C3.5; -.
DR UCSC; C38C3.5b.1; c. elegans. [Q07749-1]
DR CTD; 178640; -.
DR WormBase; C38C3.5c; CE20549; WBGene00006794; unc-60. [Q07749-1]
DR GeneTree; ENSGT00950000183000; -.
DR OMA; FVIYRIS; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006794; Expressed in larva and 3 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: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; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR017904; ADF/Cofilin.
DR PANTHER; PTHR11913; PTHR11913; 1.
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..152
FT /note="Actin-depolymerizing factor 2, isoform c"
FT /id="PRO_0000214939"
FT DOMAIN 4..147
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:2LXX"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:2LXX"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:2LXX"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:2LXX"
FT HELIX 50..61
FT /evidence="ECO:0007829|PDB:2LXX"
FT STRAND 68..85
FT /evidence="ECO:0007829|PDB:2LXX"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:2LXX"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:2LXX"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2LXX"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:2LXX"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:2LXX"
SQ SEQUENCE 152 AA; 17046 MW; BD912EE2DBEAC6DE CRC64;
MASGVKVDPS CKNAYDLLHN KHQHSYIIFK IDKNDTAIVV EKVGEKNAPY AEFVEEMKKL
VEDGKECRYA AVDVEVTVQR QGAEGTSTLN KVIFVQYCPD NAPVRRRMLY ASSVRALKAS
LGLESLFQVQ ASEMSDLDEK SVKSDLMSNQ RI
