ID   GELS_XENLA              Reviewed;         417 AA.
AC   P14885;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Gelsolin;
DE   AltName: Full=Actin-depolymerizing factor;
DE            Short=ADF;
DE   AltName: Full=Brevin;
DE   Flags: Fragment;
GN   Name=gsn;
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].
RC   TISSUE=Ovary;
RX   PubMed=2844829; DOI=10.1083/jcb.107.4.1489;
RA   Ankenbauer T., Kleinschmidt J.A., Vandekerckhove J., Franke W.W.;
RT   "Proteins regulating actin assembly in oogenesis and early embryogenesis of
RT   Xenopus laevis: gelsolin is the major cytoplasmic actin-binding protein.";
RL   J. Cell Biol. 107:1489-1498(1988).
CC   -!- FUNCTION: Calcium-regulated, actin-modulating protein that binds to the
CC       plus (or barbed) ends of actin monomers or filaments, preventing
CC       monomer exchange (end-blocking or capping). It can promote the assembly
CC       of monomers into filaments (nucleation) as well as sever filaments
CC       already formed. May play a role in ciliogenesis (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=A
CC       cytoplasmic form may also exists. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR   EMBL; M36652; AAA49725.1; -; mRNA.
DR   EMBL; X13319; CAA31694.1; -; mRNA.
DR   PIR; A31142; A31142.
DR   AlphaFoldDB; P14885; -.
DR   SMR; P14885; -.
DR   IntAct; P14885; 1.
DR   MINT; P14885; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0051014; P:actin filament severing; IEA:InterPro.
DR   GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IEA:InterPro.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   Gene3D; 3.40.20.10; -; 4.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR030004; Gelsolin.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR007122; Villin/Gelsolin.
DR   PANTHER; PTHR11977; PTHR11977; 1.
DR   PANTHER; PTHR11977:SF27; PTHR11977:SF27; 1.
DR   Pfam; PF00626; Gelsolin; 3.
DR   PRINTS; PR00597; GELSOLIN.
DR   SMART; SM00262; GEL; 3.
PE   2: Evidence at transcript level;
KW   Actin capping; Actin-binding; Calcium; Cilium biogenesis/degradation;
KW   Cytoplasm; Cytoskeleton; Metal-binding; Reference proteome; Repeat.
FT   CHAIN           <1..417
FT                   /note="Gelsolin"
FT                   /id="PRO_0000218724"
FT   REPEAT          89..140
FT                   /note="Gelsolin-like 4"
FT   REPEAT          212..252
FT                   /note="Gelsolin-like 5"
FT   REPEAT          314..356
FT                   /note="Gelsolin-like 6"
FT   BINDING         107
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         331
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         332
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   417 AA;  46024 MW;  A4FD76DA22ACFE9E CRC64;
     FISKMGYPKQ TQVQVLPESG ETPLFKQFFK NWRDKEATDG MGVAYVPNHI AKIENVPFDV
     TVLHESPAMA AQHGMVDDGS GKKQIWRIEN CEKVPVLESH YGQFYGGDSY IILYHYKSGG
     KQGQIIYTWQ GDDSTKDEIT ASAILSAQLD EELGGGPVQV RVVQGKEPAH LISLFGGKPM
     IIYKGGTSRE GGQTKDANVR LFQVRTSSSG FSRAVEVDNT ASNLNSNDAF VLTTPSASYL
     WVGQGSTNVE KNGAKELLKI LGVSASEIPE GQETDDFWGA LGGKADYRTS ARLKDKLNAH
     PPRLFACSNK TGRFIIEEVP GEISQDDLAT DDVMLLDTWD QVYVWVGNEA QEDEKKEAIA
     SAYKYIESDP ANRDKRTPVA ITKQGFEPPT FIGWFLGWEA DYWDVDPLER AMAGLSS