COF1A_XENLA
ID COF1A_XENLA Reviewed; 168 AA.
AC P45695; Q5D0B5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cofilin-1-A;
DE AltName: Full=ADF/cofilin-1;
DE Short=XAC1;
GN Name=cfl1-a;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RC TISSUE=Tail bud;
RX PubMed=8603919; DOI=10.1083/jcb.132.5.871;
RA Abe H., Obinata T., Minamide L.S., Bamburg J.R.;
RT "Xenopus laevis actin-depolymerizing factor/cofilin: a phosphorylation-
RT regulated protein essential for development.";
RL J. Cell Biol. 132:871-885(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEPHOSPHORYLATION BY PDXP.
RX PubMed=15580268; DOI=10.1038/ncb1201;
RA Gohla A., Birkenfeld J., Bokoch G.M.;
RT "Chronophin, a novel HAD-type serine protein phosphatase, regulates
RT cofilin-dependent actin dynamics.";
RL Nat. Cell Biol. 7:21-29(2005).
CC -!- FUNCTION: May play a role in the regulation of cell morphology and
CC cytoskeletal organization (By similarity). Binds to F-actin and
CC exhibits pH-sensitive F-actin depolymerizing activity. Required for
CC formation of the cleavage furrow during cytokinesis. {ECO:0000250,
CC ECO:0000269|PubMed:8603919}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:8603919}. Membrane {ECO:0000269|PubMed:8603919}.
CC Note=Cellular localization varies throughout development and may be
CC related to phosphorylation levels. Shows diffuse cortical cytoplasm
CC localization in oocytes, with membrane-association increasing after
CC fertilization, particularly in the vegetal hemisphere.
CC -!- TISSUE SPECIFICITY: Expressed diffusely in both animal and vegetal
CC hemispheres of the oocyte. During cleavage, expression accumulates
CC around the cleavage furrow, along the vegetal membrane, and later in
CC the midbody. Strongly expressed in the animal hemisphere during
CC blastula stages, with most cells showing expression by gastrulation. By
CC stage 17, expression is highest in cells of the developing
CC neuroectoderm, and at stage 24 the notochord, neural tube, neural
CC crest, somites and some cells of the archenteron show high expression.
CC By stage 35, expression has declined in the notochord, but remains in
CC the neural tube, epidermis and a layer of cells in the archenteron.
CC Also highly expressed in the retina and neuronal cell bodies at the
CC base of the cement gland but not the cement gland itself. At stage 38,
CC expression is widespread, being highest in the nervous system and
CC retina. In the adult, expression is high in the brain, heart, oocyte,
CC stomach, and low in skeletal muscle. {ECO:0000269|PubMed:8603919}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Maternal expression is gradually replaced with zygotic expression
CC between the morula (stage 5) and tadpole (stage 34) stages.
CC {ECO:0000269|PubMed:8603919}.
CC -!- PTM: Inactive when phosphorylated. Phosphorylation levels vary during
CC development. Oocytes contain only the phosphorylated form, and 80-95%
CC of cfl1 protein is phosphorylated in unfertilized eggs. Rapid
CC dephosphorylation occurs within 30 minutes after fertilization.
CC Phosphorylation levels increase again between the morula and blastula
CC stages (5-8 hpf) and then decrease again as gastrulation approaches.
CC Dephosphorylated by pdxp. {ECO:0000269|PubMed:8603919}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; U26270; AAB00540.1; -; mRNA.
DR EMBL; BC044691; AAH44691.1; -; mRNA.
DR RefSeq; NP_001079571.1; NM_001086102.1.
DR AlphaFoldDB; P45695; -.
DR SMR; P45695; -.
DR BioGRID; 97501; 1.
DR IntAct; P45695; 1.
DR DNASU; 379258; -.
DR GeneID; 379258; -.
DR CTD; 379258; -.
DR Xenbase; XB-GENE-1016488; cfl1.L.
DR OrthoDB; 1370477at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 379258; Expressed in brain and 19 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IMP:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; 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 InterPro; IPR027234; Cofilin_1.
DR PANTHER; PTHR11913; PTHR11913; 1.
DR PANTHER; PTHR11913:SF53; PTHR11913:SF53; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR PRINTS; PR00006; COFILIN.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..168
FT /note="Cofilin-1-A"
FT /id="PRO_0000214904"
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"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 168 AA; 19066 MW; F3A4D8635A3683D6 CRC64;
MASGVMVSDD VIKVFNEMKV RHQLSPEDAK KRKKAVVFCL SDDKKTIILE PGKEILQGDI
GCNVEDPYKT FVKMLPRNDC RYALYDALYE TKETKKEDLV FVFWAPEEAS LKSKMIYASS
KDAIKKRLPG IKHEWQINTY EDVNDPCNLA DKLGGNTVVS LEGKSVRS
