GELS_DROME
ID GELS_DROME Reviewed; 798 AA.
AC Q07171; A4V2C8; A9UNC4; Q0KIE3; Q0KIE4; Q8MRF9; Q9VMZ1; Q9VMZ2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Gelsolin;
DE Flags: Precursor;
GN Name=Gel; ORFNames=CG1106;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAF52163.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8386771; DOI=10.1006/jmbi.1993.1191;
RA Heintzelman M.B., Frankel S.A., Artavanis-Tsakonas S., Mooseker M.S.;
RT "Cloning of a secretory gelsolin from Drosophila melanogaster.";
RL J. Mol. Biol. 230:709-716(1993).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8175883; DOI=10.1083/jcb.125.3.607;
RA Stella M.C., Schauerte H., Straub K.L., Leptin M.;
RT "Identification of secreted and cytosolic gelsolin in Drosophila.";
RL J. Cell Biol. 125:607-616(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000269|PubMed:8175883}.
CC -!- SUBUNIT: Binds to actin and to fibronectin.
CC {ECO:0000269|PubMed:8175883}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:8175883, ECO:0000305}; Synonyms=B
CC {ECO:0000269|PubMed:8175883, ECO:0000305}, D
CC {ECO:0000312|FlyBase:FBgn0010225}, F {ECO:0000312|FlyBase:FBgn0010225},
CC Secreted {ECO:0000269|PubMed:8175883, ECO:0000305};
CC IsoId=Q07171-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:8175883, ECO:0000305}; Synonyms=A
CC {ECO:0000269|PubMed:8175883, ECO:0000305}, Cytoplasmic
CC {ECO:0000269|PubMed:8175883, ECO:0000305};
CC IsoId=Q07171-2; Sequence=VSP_007010;
CC Name=K {ECO:0000312|FlyBase:FBgn0010225};
CC IsoId=Q07171-6; Sequence=VSP_058364;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are ubiquitously expressed
CC in early embryo. Isoform 1 is expressed in the fat body, and is
CC abundant in hemolymph. Isoform 2 is expressed in parts of the gut.
CC {ECO:0000269|PubMed:8175883}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
CC -!- CAUTION: Lacks one of the cysteines to make the disulfide bridge in
CC isoform 1. It is replaced by Val-233. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28568.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM50316.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM50316.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM50316.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=ABY20529.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA53295.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L08794; AAA28568.1; ALT_INIT; mRNA.
DR EMBL; X75629; CAA53294.1; -; mRNA.
DR EMBL; X75630; CAA53295.1; ALT_INIT; mRNA.
DR EMBL; AE014297; AAF52162.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF52163.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF52164.3; -; Genomic_DNA.
DR EMBL; AE014297; AAN13333.3; -; Genomic_DNA.
DR EMBL; AE014297; AAO41510.1; -; Genomic_DNA.
DR EMBL; AY119662; AAM50316.1; ALT_SEQ; mRNA.
DR EMBL; BT031288; ABY20529.1; ALT_INIT; mRNA.
DR PIR; A53909; A53909.
DR RefSeq; NP_001036657.2; NM_001043192.3. [Q07171-2]
DR RefSeq; NP_524865.2; NM_080126.4. [Q07171-1]
DR RefSeq; NP_730788.1; NM_164319.4. [Q07171-2]
DR RefSeq; NP_730790.2; NM_164321.5. [Q07171-1]
DR RefSeq; NP_788571.1; NM_176394.3. [Q07171-1]
DR RefSeq; NP_996148.2; NM_206426.4. [Q07171-6]
DR RefSeq; NP_996149.3; NM_206427.4. [Q07171-1]
DR AlphaFoldDB; Q07171; -.
DR SMR; Q07171; -.
DR BioGRID; 70060; 6.
DR IntAct; Q07171; 4.
DR STRING; 7227.FBpp0078607; -.
DR PaxDb; Q07171; -.
DR PRIDE; Q07171; -.
DR DNASU; 46008; -.
DR EnsemblMetazoa; FBtr0078968; FBpp0078607; FBgn0010225. [Q07171-1]
DR EnsemblMetazoa; FBtr0078969; FBpp0078608; FBgn0010225. [Q07171-1]
DR EnsemblMetazoa; FBtr0078971; FBpp0078610; FBgn0010225. [Q07171-2]
DR EnsemblMetazoa; FBtr0078973; FBpp0078612; FBgn0010225. [Q07171-1]
DR EnsemblMetazoa; FBtr0309256; FBpp0301195; FBgn0010225. [Q07171-1]
DR EnsemblMetazoa; FBtr0309257; FBpp0301196; FBgn0010225. [Q07171-6]
DR EnsemblMetazoa; FBtr0336707; FBpp0307688; FBgn0010225. [Q07171-2]
DR GeneID; 46008; -.
DR KEGG; dme:Dmel_CG1106; -.
DR CTD; 46008; -.
DR FlyBase; FBgn0010225; Gel.
DR VEuPathDB; VectorBase:FBgn0010225; -.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000173475; -.
DR InParanoid; Q07171; -.
DR OMA; DNRTKTH; -.
DR PhylomeDB; Q07171; -.
DR Reactome; R-DME-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q07171; -.
DR BioGRID-ORCS; 46008; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Bsg; fly.
DR GenomeRNAi; 46008; -.
DR PRO; PR:Q07171; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010225; Expressed in embryonic/larval hemocyte (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q07171; baseline and differential.
DR Genevisible; Q07171; DM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005884; C:actin filament; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
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 Gene3D; 3.40.20.10; -; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 3.
DR Pfam; PF00626; Gelsolin; 5.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Calcium; Cytoplasm; Cytoskeleton;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..798
FT /note="Gelsolin"
FT /id="PRO_0000036393"
FT REPEAT 78..131
FT /note="Gelsolin-like 1"
FT REPEAT 203..243
FT /note="Gelsolin-like 2"
FT REPEAT 322..365
FT /note="Gelsolin-like 3"
FT REPEAT 474..524
FT /note="Gelsolin-like 4"
FT REPEAT 583..625
FT /note="Gelsolin-like 5"
FT REPEAT 689..730
FT /note="Gelsolin-like 6"
FT REGION 57..181
FT /note="Actin-severing"
FT /evidence="ECO:0000255"
FT REGION 128..131
FT /note="Actin-actin interfilament contact point"
FT /evidence="ECO:0000250"
FT REGION 451..792
FT /note="Actin-binding, Ca-sensitive"
FT /evidence="ECO:0000255"
FT BINDING 167..174
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 193..201
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 623
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 705
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 728
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 90
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000305"
FT MOD_RES 612
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000305"
FT MOD_RES 662
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8175883"
FT /id="VSP_007010"
FT VAR_SEQ 1..14
FT /note="MDASGAATMAVLSS -> MF (in isoform K)"
FT /id="VSP_058364"
FT CONFLICT 498
FT /note="N -> S (in Ref. 2; CAA53294/CAA53295)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="G -> S (in Ref. 2; CAA53294/CAA53295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 798 AA; 88375 MW; 79828666DC0965CC CRC64;
MDASGAATMA VLSSLLVFLA LSSSLCSAGT LNARPAFPVQ SGEIQPSGQN SKQAARRVMH
PSFANAGRTP GLEIWRIENF EPVIYPKTNY GKFYTGDSFI VLNTIENKKD KKLSWDVHFW
LGLETSTDEA GAAAILTVQL DDLLNGGPVQ HREVQDHESQ LFLSYFKNGI RYEQGGVGTG
FKHVETNAQG ETRLFQVKGK RNVRVRQVNL SVSSMNTGDC FILDAGSDIY VYVGSQAKRV
EKLKAISAAN QIRDQDHNGR ARVQIVDDFS TDADKQHFFD VLGSGSADQV PDESTADEDS
AFERTDAAAV SLYKVSDASG KLKVDIIGQK PLTQAMLDTR ECFILDTGSG IFVWVGKGAT
QKEKTDAMAK AQEFLRTKKY PAWTQIHRIV EGSESAPFKQ YFDTWRDAGM SHSRLIRSAL
GIGSDELLND DEIDSVVTQL KKSGGRAFGF MPDHGQNVIE TITQYVAKPG SDEIVVSTVP
FDEKLPLLGF ASYVLTYNYE ANNGDTGSLT YVWHGVKASA AARKRAFEEG LVGSKDGLLV
QTNQGHEPRH FYKIFKGKLL TSFTALPVTA QLFRIRGTVE SDVHASEVAA DSSSLASSDA
FVLHSGKSHK IYIWNGLGAS AFEKQAAVDR FSDYWDDVEL EQVEEGAEPD EFWEELNGEG
QYDRSLGDDG APLLESRLFH CHLSSGGFLK VEEVAQYEQE DLDSDDIMLL DAGDEIYLWV
GYGVSEEENG KLLDTAKLYF NLEPTARSFD TVSIIRVPQG KEPRVFKRMF PNWDDNYWQN
QPSYEDMKQL VIDANNEV
