GELS1_CAEBR
ID GELS1_CAEBR Reviewed; 474 AA.
AC A8XV95;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Gelsolin-like protein 1 {ECO:0000250|UniProtKB:Q21253};
GN Name=gsnl-1 {ECO:0000312|WormBase:CBG19286}; ORFNames=CBG19286;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP36562.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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). Binds actin but does not
CC nucleate actin polymerization, albeit slows down elongation by blocking
CC the barbed ends. By promoting actin depolymerization, required for the
CC elimination of presynaptic components downstream of the egl-1, ced-4
CC and ced-3 apoptotic pathway during larval development.
CC {ECO:0000250|UniProtKB:Q21253}.
CC -!- SUBUNIT: Monomer. Binds to actin monomers and filaments.
CC {ECO:0000250|UniProtKB:Q21253}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q07171}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000255}.
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DR EMBL; HE601047; CAP36562.1; -; Genomic_DNA.
DR RefSeq; XP_002637554.1; XM_002637508.1.
DR AlphaFoldDB; A8XV95; -.
DR SMR; A8XV95; -.
DR STRING; 6238.CBG19286; -.
DR EnsemblMetazoa; CBG19286.1; CBG19286.1; WBGene00038533.
DR GeneID; 8579549; -.
DR KEGG; cbr:CBG_19286; -.
DR CTD; 8579549; -.
DR WormBase; CBG19286; CBP11123; WBGene00038533; Cbr-gsnl-1.
DR eggNOG; KOG0443; Eukaryota.
DR HOGENOM; CLU_002568_0_0_1; -.
DR InParanoid; A8XV95; -.
DR OMA; LHSYKVG; -.
DR OrthoDB; 1376537at2759; -.
DR Proteomes; UP000008549; Chromosome V.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; IEA:EnsemblMetazoa.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:EnsemblMetazoa.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:1905808; P:positive regulation of synapse pruning; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
KW Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat.
FT CHAIN 1..474
FT /note="Gelsolin-like protein 1"
FT /id="PRO_0000412118"
FT REPEAT 27..105
FT /note="Gelsolin-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 147..202
FT /note="Gelsolin-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 272..337
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 374..446
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REGION 1..238
FT /note="Necessary for barbed end capping activity"
FT /evidence="ECO:0000250|UniProtKB:Q21253"
FT REGION 1..131
FT /note="Actin binding, actin severing, Ca-sensitive"
FT /evidence="ECO:0000250|UniProtKB:Q21253"
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:0000250|UniProtKB:Q21253"
FT REGION 133..226
FT /note="Required for phosphatidylinositol 4,5-bisphosphate
FT binding and regulation"
FT /evidence="ECO:0000250|UniProtKB:Q21253"
FT REGION 239..474
FT /note="F- and G-actin binding, Ca-independent"
FT /evidence="ECO:0000250|UniProtKB:Q21253"
FT REGION 247..347
FT /note="Inhibitory for phosphatidylinositol 4,5-bisphosphate
FT binding activity"
FT /evidence="ECO:0000250|UniProtKB:Q21253"
FT SITE 387..388
FT /note="Cleavage; probably by ced-3"
FT /evidence="ECO:0000250|UniProtKB:Q21253"
SQ SEQUENCE 474 AA; 54462 MW; 0203FD8882E6C55D CRC64;
MRPTSIDPAL AEIGKKNGLL VWRINKFELE PVPETEHGIF FIGDAYIVLN QKYEGCWDVH
FWLGKNASTD EIGVAAIKTV EIDDSLGGIP TQHREVQNYE SPLFLSYFTD GIRYVAGGYE
SGYNHVEDQF KNWKPHLFHC KGKRNVRCTE VECEVGSLNL GDVFILDLGK DIYIWMPPDS
GRLERVKGMA RAKNIADVER MGASKVHILD DEWDNDPTFW SYFGGVSSVK KVTKSKDDDD
NYWKRLSEQI TLWKVSDVTG AAKVTMVGQG ENLKKELLDS KDAFILDAIN GGIFVWIGRE
CTLEERSKAL IWGQNYLKQH HLPKWTQVTR VLDTAESTQF TQWFRDWVDE KKKNTFQPLL
FQVSDESGLL HVEEIANFTQ EDLDGDDVMI LDALNSIYVW VGSNANPNEK KEALNTAKSY
LEKDKLPRHK KTSIDTIYQG QEPPTFKKFF PSWDDALFKN QVRSVENMRR LLFH
