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COF1B_XENLA
ID   COF1B_XENLA             Reviewed;         168 AA.
AC   P45593; Q5D0C1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Cofilin-1-B;
DE   AltName: Full=ADF/cofilin-2;
DE            Short=XAC2;
GN   Name=cfl1-b;
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 [MRNA].
RC   TISSUE=Oocyte;
RA   Wada A., Gotoh Y., Nishida E.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC       {ECO:0000305}.
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DR   EMBL; U26269; AAB00539.1; -; mRNA.
DR   EMBL; D38406; BAA07461.1; -; mRNA.
DR   EMBL; BC043803; AAH43803.1; -; mRNA.
DR   RefSeq; NP_001079485.1; NM_001086016.1.
DR   AlphaFoldDB; P45593; -.
DR   SMR; P45593; -.
DR   BioGRID; 97415; 1.
DR   DNASU; 379172; -.
DR   GeneID; 379172; -.
DR   KEGG; xla:379172; -.
DR   CTD; 379172; -.
DR   Xenbase; XB-GENE-6251620; cfl1.S.
DR   OMA; QEDIEWE; -.
DR   OrthoDB; 1370477at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 379172; Expressed in blastula 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-B"
FT                   /id="PRO_0000214905"
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;  19120 MW;  6DBCE7F8397EDFD1 CRC64;
     MASGVMVSDD VVKVFNDMKV RHQLSPEEAK KRKKAVIFCL SDDKKTIILE PGKEILQGDV
     GCNVEDPYKT FVKMLPRNDC RYALYDALYE TKETKKEDLV FVFWAPEEAS LKSKMIYASS
     KDAIRKRFTG IKHEWQTNTY DDINDPCNLA DKLGGNTVVS LEGKSLRS
 
 
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