GELS1_CAEEL
ID GELS1_CAEEL Reviewed; 475 AA.
AC Q21253;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Gelsolin-like protein 1 {ECO:0000303|PubMed:18640981};
GN Name=gsnl-1 {ECO:0000312|WormBase:K06A4.3}; ORFNames=K06A4.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH ACTIN.
RX PubMed=18640981; DOI=10.1074/jbc.m803618200;
RA Klaavuniemi T., Yamashiro S., Ono S.;
RT "Caenorhabditis elegans gelsolin-like protein 1 is a novel actin filament-
RT severing protein with four gelsolin-like repeats.";
RL J. Biol. Chem. 283:26071-26080(2008).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH ACTIN.
RX PubMed=20392036; DOI=10.1021/bi100215b;
RA Liu Z., Klaavuniemi T., Ono S.;
RT "Distinct roles of four gelsolin-like domains of Caenorhabditis elegans
RT gelsolin-like protein-1 in actin filament severing, barbed end capping, and
RT phosphoinositide binding.";
RL Biochemistry 49:4349-4360(2010).
RN [3] {ECO:0000312|EMBL:CAA94782.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
RN [4]
RP FUNCTION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF 387-ASP--ILE-391 AND
RP ASP-388.
RX PubMed=26074078; DOI=10.1016/j.celrep.2015.05.031;
RA Meng L., Mulcahy B., Cook S.J., Neubauer M., Wan A., Jin Y., Yan D.;
RT "The cell death pathway regulates synapse elimination through cleavage of
RT gelsolin in Caenorhabditis elegans neurons.";
RL Cell Rep. 11:1737-1748(2015).
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) (PubMed:18640981,
CC PubMed:20392036). Binds actin but does not nucleate actin
CC polymerization, albeit slows down elongation by blocking the barbed
CC ends (PubMed:18640981, PubMed:20392036). By promoting actin
CC depolymerization, required for the elimination of presynaptic
CC components downstream of the egl-1, ced-4 and ced-3 apoptotic pathway
CC during larval development (PubMed:26074078).
CC {ECO:0000269|PubMed:18640981, ECO:0000269|PubMed:20392036,
CC ECO:0000269|PubMed:26074078}.
CC -!- SUBUNIT: Monomer. Binds to actin monomers and filaments.
CC {ECO:0000269|PubMed:18640981, ECO:0000269|PubMed:20392036}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q07171}.
CC -!- PTM: Cleavage by caspase ced-3 activates its actin-severing function
CC and is required for the elimination of presynaptic components during
CC development. {ECO:0000269|PubMed:26074078}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000255}.
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DR EMBL; Z70755; CAA94782.1; -; Genomic_DNA.
DR PIR; T23355; T23355.
DR RefSeq; NP_505448.1; NM_073047.5.
DR AlphaFoldDB; Q21253; -.
DR SMR; Q21253; -.
DR BioGRID; 44366; 3.
DR IntAct; Q21253; 1.
DR STRING; 6239.K06A4.3; -.
DR EPD; Q21253; -.
DR PaxDb; Q21253; -.
DR PeptideAtlas; Q21253; -.
DR EnsemblMetazoa; K06A4.3.1; K06A4.3.1; WBGene00010593.
DR GeneID; 179328; -.
DR KEGG; cel:CELE_K06A4.3; -.
DR UCSC; K06A4.3; c. elegans.
DR CTD; 179328; -.
DR WormBase; K06A4.3; CE06107; WBGene00010593; gsnl-1.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000173475; -.
DR HOGENOM; CLU_002568_0_0_1; -.
DR InParanoid; Q21253; -.
DR OMA; LHSYKVG; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; Q21253; -.
DR Reactome; R-CEL-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q21253; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010593; Expressed in larva and 4 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; HDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR GO; GO:0051015; F:actin filament binding; IDA:WormBase.
DR GO; GO:0003785; F:actin monomer binding; IDA:WormBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:WormBase.
DR GO; GO:0030042; P:actin filament depolymerization; IMP:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; IDA:WormBase.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:WormBase.
DR GO; GO:1905808; P:positive regulation of synapse pruning; IMP:UniProtKB.
DR Gene3D; 3.40.20.10; -; 4.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 2.
DR Pfam; PF00626; Gelsolin; 4.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 4.
PE 1: Evidence at protein level;
KW Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat.
FT CHAIN 1..475
FT /note="Gelsolin-like protein 1"
FT /id="PRO_0000412119"
FT REPEAT 27..105
FT /note="Gelsolin-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 148..208
FT /note="Gelsolin-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 275..341
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 375..447
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REGION 1..239
FT /note="Necessary for barbed end capping activity"
FT /evidence="ECO:0000269|PubMed:20392036"
FT REGION 1..131
FT /note="Actin binding, actin severing, Ca-sensitive"
FT /evidence="ECO:0000269|PubMed:20392036"
FT REGION 70..73
FT /note="Actin-actin interfilament contact point"
FT /evidence="ECO:0000250|UniProtKB:Q07171"
FT REGION 106..147
FT /note="Required for synapse elimination during development"
FT /evidence="ECO:0000305|PubMed:26074078"
FT REGION 133..227
FT /note="Required for phosphatidylinositol 4,5-bisphosphate
FT binding and regulation"
FT /evidence="ECO:0000269|PubMed:20392036"
FT REGION 240..475
FT /note="F- and G-actin binding, Ca-independent"
FT /evidence="ECO:0000269|PubMed:20392036"
FT REGION 248..348
FT /note="Inhibitory for phosphatidylinositol 4,5-bisphosphate
FT binding activity"
FT /evidence="ECO:0000269|PubMed:20392036"
FT SITE 388..389
FT /note="Cleavage; probably by ced-3"
FT /evidence="ECO:0000269|PubMed:26074078"
FT MUTAGEN 387..391
FT /note="Missing: Loss of processing. Impaired elimination of
FT synapses in adults."
FT /evidence="ECO:0000269|PubMed:26074078"
FT MUTAGEN 388
FT /note="D->A: Loss of processing."
FT /evidence="ECO:0000269|PubMed:26074078"
SQ SEQUENCE 475 AA; 54592 MW; 70369567F80280F5 CRC64;
MGGTSLDPAL AEIGKKNGLL VWRINKFVLE PVPEVDHGVF YIGDAYIALY QKYDGCWDVH
FWLGKNASTD EIGVAAIKTV EIDDSLGGIP TQHREIQNYE SPLFLSYFPD GIRYVSGGYE
SGYRHVDDQF KNWKPHLFHC KGKRNVRCTE VECEVNSLNL GDVFILDLGK DLYVWMPPES
GRLERIKGMA RAKNIADHER MGIPKVHILD DVEWDNDSTF WSYFGGVSSV RKVSKGKDDD
DNYWKRLTEQ ITLWKVSDAS GAAKVSMVSQ GENIRKEQLD PKDAFILDAI NGGIFVWIGH
ECTLEERSKA LIWGQNYLKQ HHLPRWTQVT RVLESAESTQ FTQWFRDWVD EKKKNTFTPL
LFQVSDESGL LHVEEIANFT QEDLDGDDVM ILDALNSIYV WVGANANANE KKEALNTAKL
YLEKDKLPRH KKTAIDTIFQ GKEPPTFKKF FPSWDDNLFK NEVRSVQNMR RLLFH
