COF2_XENLA
ID COF2_XENLA Reviewed; 167 AA.
AC Q5XHH8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Cofilin-2;
GN Name=cfl2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Controls reversibly actin polymerization and depolymerization
CC in a pH-sensitive manner. It has the ability to bind G- and F-actin in
CC a 1:1 ratio of cofilin to actin. It is the major component of
CC intranuclear and cytoplasmic actin rods (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}.
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; BC084079; AAH84079.1; -; mRNA.
DR RefSeq; NP_001088171.1; NM_001094702.1.
DR AlphaFoldDB; Q5XHH8; -.
DR SMR; Q5XHH8; -.
DR MaxQB; Q5XHH8; -.
DR DNASU; 494995; -.
DR GeneID; 494995; -.
DR KEGG; xla:494995; -.
DR CTD; 494995; -.
DR Xenbase; XB-GENE-6078566; cfl2.L.
DR OMA; ECKYAIY; -.
DR OrthoDB; 1370477at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 494995; Expressed in heart and 15 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; ISS:UniProtKB.
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 PRINTS; PR00006; COFILIN.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome.
FT CHAIN 1..167
FT /note="Cofilin-2"
FT /id="PRO_0000214911"
FT DOMAIN 4..153
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT MOTIF 30..34
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 167 AA; 18858 MW; 798B3B40D43A6B2C CRC64;
MASGVTVNDE VIKVFNEMKV RKSSTPEEIK KRKKAVLFCL SPDKKEIIVE ETKQILVGDI
GEAVQDPYRT FVNLLPLDDC RYGLYDATYE TKESKKEDLV FIFWAPDNAP LKSKMIYASS
KDAIKKKFTG IKHEWQVNGL DDIKDRCTLA DKLGGNVVVS LEGVPLK