ID GELS_MOUSE Reviewed; 780 AA.
AC P13020; Q3UPB1; Q8R590;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 3.
DT 27-MAR-2024, entry version 221.
DE RecName: Full=Gelsolin;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
DE AltName: Full=Brevin;
DE Flags: Precursor;
GN Name=Gsn; Synonyms=Gsb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=2546951; DOI=10.1016/s0021-9258(18)51626-4;
RA Dieffenbach C.W., Sengupta D.N., Krause D., Sawzak D., Silverman R.H.;
RT "Cloning of murine gelsolin and its regulation during differentiation of
RT embryonal carcinoma cells.";
RL J. Biol. Chem. 264:13281-13288(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Head, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 50-70 (ISOFORM 2), PROTEIN SEQUENCE OF 74-97; 146-160;
RP 167-186; 254-293; 301-336; 359-366; 372-388; 396-445; 456-479; 529-546;
RP 552-562; 583-621; 625-646; 667-673; 712-736 AND 739-746 (ISOFORMS 1/2),
RP CLEAVAGE OF INITIATOR METHIONINE (ISOFORM 2), ACETYLATION AT MET-1 (ISOFORM
RP 2), AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic fibroblast;
RA Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.;
RL Submitted (MAR-2008) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 51-73.
RC TISSUE=Fibroblast;
RX PubMed=7523108; DOI=10.1002/elps.11501501101;
RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
RT "Separation and sequencing of familiar and novel murine proteins using
RT preparative two-dimensional gel electrophoresis.";
RL Electrophoresis 15:735-745(1994).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH EIF2AK2.
RX PubMed=22633459; DOI=10.1016/j.immuni.2012.02.020;
RA Irving A.T., Wang D., Vasilevski O., Latchoumanin O., Kozer N.,
RA Clayton A.H., Szczepny A., Morimoto H., Xu D., Williams B.R., Sadler A.J.;
RT "Regulation of actin dynamics by protein kinase R control of gelsolin
RT enforces basal innate immune defense.";
RL Immunity 36:795-806(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-582, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9] {ECO:0007744|PDB:1NPH}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 439-767 IN COMPLEX WITH CALCIUM,
RP AND DOMAIN.
RX PubMed=12742020; DOI=10.1016/s0022-2836(03)00383-8;
RA Kolappan S., Gooch J.T., Weeds A.G., McLaughlin P.J.;
RT "Gelsolin domains 4-6 in active, actin-free conformation identifies sites
RT of regulatory calcium ions.";
RL J. Mol. Biol. 329:85-92(2003).
RN [10] {ECO:0007744|PDB:4CBU, ECO:0007744|PDB:4CBW, ECO:0007744|PDB:4CBX}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 50-174 IN COMPLEX WITH
RP P.FALCIPARUM ACT1; P.BERGHEI ACT2 AND CALCIUM, AND DOMAIN.
RX PubMed=24743229; DOI=10.1371/journal.ppat.1004091;
RA Vahokoski J., Bhargav S.P., Desfosses A., Andreadaki M., Kumpula E.P.,
RA Martinez S.M., Ignatev A., Lepper S., Frischknecht F., Siden-Kiamos I.,
RA Sachse C., Kursula I.;
RT "Structural differences explain diverse functions of Plasmodium actins.";
RL PLoS Pathog. 10:e1004091-e1004091(2014).
RN [11] {ECO:0007744|PDB:5MVV}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 50-174 IN COMPLEX WITH
RP P.FALCIPARUM ACT1 AND CALCIUM, AND DOMAIN.
RX PubMed=28695858; DOI=10.1107/s2059798317006970;
RA Panneerselvam S., Kumpula E.P., Kursula I., Burkhardt A., Meents A.;
RT "Rapid cadmium SAD phasing at the standard wavelength (1 A).";
RL Acta Crystallogr. D 73:581-590(2017).
RN [12] {ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E, ECO:0007744|PDB:6I4F, ECO:0007744|PDB:6I4G, ECO:0007744|PDB:6I4H, ECO:0007744|PDB:6I4I, ECO:0007744|PDB:6I4J, ECO:0007744|PDB:6I4K, ECO:0007744|PDB:6I4L, ECO:0007744|PDB:6I4M}
RP X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 50-174 IN COMPLEX P.FALCIPARUM
RP ACT1; P.BERGHEI ACT2 AND CALCIUM, AND DOMAIN.
RX PubMed=31199804; DOI=10.1371/journal.pbio.3000315;
RA Kumpula E.P., Lopez A.J., Tajedin L., Han H., Kursula I.;
RT "Atomic view into Plasmodium actin polymerization, ATP hydrolysis, and
RT fragmentation.";
RL PLoS Biol. 17:e3000315-e3000315(2019).
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 (By similarity). Plays a role in ciliogenesis (By
CC similarity). {ECO:0000250|UniProtKB:P06396}.
CC -!- SUBUNIT: Binds to actin and to fibronectin. Identified in a complex
CC composed of ACTA1, COBL, GSN and TMSB4X (By similarity). Interacts with
CC the inactive form of EIF2AK2/PKR. {ECO:0000250,
CC ECO:0000269|PubMed:22633459}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=Secreted, Plasma;
CC IsoId=P13020-1; Sequence=Displayed;
CC Name=2; Synonyms=Cytoplasmic;
CC IsoId=P13020-2; Sequence=VSP_018960;
CC -!- DOMAIN: Comprises six structurally related gelsolin-like (G1-G6)
CC domains, that, in a calcium-free environment, are packed together to
CC form a compact globular structure in which the putative actin-binding
CC sequences are not sufficiently exposed to enable binding to occur (By
CC similarity). Binding calcium may release the connections that join the
CC N- and C-terminal halves of gelsolin, enabling each half to bind actin
CC relatively independently (By similarity). G1 and G4 bind two Ca(2+) in
CC a type I and in a type II manner (PubMed:24743229, PubMed:28695858,
CC PubMed:31199804). G2, G3, G5 and G6 bind only one Ca(2+) in a type II
CC manner (PubMed:12742020, PubMed:24743229, PubMed:28695858,
CC PubMed:31199804). Type I Ca(2+) binding sites are shared between actin
CC and gelsolin-like repeats G1 and G4 (PubMed:24743229, PubMed:31199804).
CC Type I binding governs the strength of interactions between gelsolin
CC and actin by direct participation at the binding interface (By
CC similarity). Ca(2+) binding to G2 and G6 disrupts the interactions
CC between G2 and G6, releases the C-terminal tail, and induces large
CC interdomain rearrangements that result in the exposure of the F-actin-
CC binding site on G2 and contributes to the activation of gelsolin (By
CC similarity). Binding to phosphoinositides may inhibit the severing and
CC capping properties of gelsolin (By similarity).
CC {ECO:0000250|UniProtKB:P06396, ECO:0000269|PubMed:12742020,
CC ECO:0000269|PubMed:24743229, ECO:0000269|PubMed:28695858,
CC ECO:0000269|PubMed:31199804}.
CC -!- PTM: Phosphorylated on tyrosine residues in vitro. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; J04953; AAA37677.1; -; mRNA.
DR EMBL; AK076156; BAC36223.1; -; mRNA.
DR EMBL; AK089934; BAC41004.1; -; mRNA.
DR EMBL; AK143664; BAE25485.1; -; mRNA.
DR EMBL; BC023143; AAH23143.2; -; mRNA.
DR CCDS; CCDS15960.1; -. [P13020-1]
DR CCDS; CCDS79785.1; -. [P13020-2]
DR RefSeq; NP_666232.2; NM_146120.4. [P13020-1]
DR PDB; 1NPH; X-ray; 3.00 A; A=439-767.
DR PDB; 4CBU; X-ray; 1.30 A; G=50-174.
DR PDB; 4CBW; X-ray; 2.50 A; G=50-174.
DR PDB; 4CBX; X-ray; 2.20 A; G=50-174.
DR PDB; 5MVV; X-ray; 1.40 A; G=50-174.
DR PDB; 6I4D; X-ray; 1.24 A; G=50-174.
DR PDB; 6I4E; X-ray; 1.22 A; G=50-174.
DR PDB; 6I4F; X-ray; 1.50 A; G=50-174.
DR PDB; 6I4G; X-ray; 2.00 A; G/H=50-174.
DR PDB; 6I4H; X-ray; 1.40 A; G=50-174.
DR PDB; 6I4I; X-ray; 1.90 A; G=50-174.
DR PDB; 6I4J; X-ray; 1.50 A; G=50-174.
DR PDB; 6I4K; X-ray; 1.83 A; G=50-174.
DR PDB; 6I4L; X-ray; 1.83 A; G=50-174.
DR PDB; 6I4M; X-ray; 1.87 A; G=50-174.
DR PDBsum; 1NPH; -.
DR PDBsum; 4CBU; -.
DR PDBsum; 4CBW; -.
DR PDBsum; 4CBX; -.
DR PDBsum; 5MVV; -.
DR PDBsum; 6I4D; -.
DR PDBsum; 6I4E; -.
DR PDBsum; 6I4F; -.
DR PDBsum; 6I4G; -.
DR PDBsum; 6I4H; -.
DR PDBsum; 6I4I; -.
DR PDBsum; 6I4J; -.
DR PDBsum; 6I4K; -.
DR PDBsum; 6I4L; -.
DR PDBsum; 6I4M; -.
DR AlphaFoldDB; P13020; -.
DR SMR; P13020; -.
DR BioGRID; 230683; 26.
DR CORUM; P13020; -.
DR DIP; DIP-31941N; -.
DR IntAct; P13020; 14.
DR MINT; P13020; -.
DR STRING; 10090.ENSMUSP00000028239; -.
DR GlyGen; P13020; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P13020; -.
DR PhosphoSitePlus; P13020; -.
DR SwissPalm; P13020; -.
DR REPRODUCTION-2DPAGE; P13020; -.
DR CPTAC; non-CPTAC-3366; -.
DR CPTAC; non-CPTAC-3514; -.
DR EPD; P13020; -.
DR jPOST; P13020; -.
DR MaxQB; P13020; -.
DR PaxDb; 10090-ENSMUSP00000028239; -.
DR PeptideAtlas; P13020; -.
DR ProteomicsDB; 272952; -. [P13020-1]
DR ProteomicsDB; 272953; -. [P13020-2]
DR Pumba; P13020; -.
DR Antibodypedia; 3387; 850 antibodies from 47 providers.
DR DNASU; 227753; -.
DR Ensembl; ENSMUST00000028239.8; ENSMUSP00000028239.7; ENSMUSG00000026879.15. [P13020-1]
DR Ensembl; ENSMUST00000201185.4; ENSMUSP00000144561.2; ENSMUSG00000026879.15. [P13020-2]
DR GeneID; 227753; -.
DR KEGG; mmu:227753; -.
DR UCSC; uc008jkc.2; mouse. [P13020-1]
DR AGR; MGI:95851; -.
DR CTD; 2934; -.
DR MGI; MGI:95851; Gsn.
DR VEuPathDB; HostDB:ENSMUSG00000026879; -.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000155591; -.
DR InParanoid; P13020; -.
DR OMA; NRVVHVK; -.
DR PhylomeDB; P13020; -.
DR TreeFam; TF313468; -.
DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 227753; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Gsn; mouse.
DR EvolutionaryTrace; P13020; -.
DR PRO; PR:P13020; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P13020; Protein.
DR Bgee; ENSMUSG00000026879; Expressed in skin of external ear and 296 other cell types or tissues.
DR ExpressionAtlas; P13020; baseline and differential.
DR Genevisible; P13020; MM.
DR GO; GO:0030478; C:actin cap; ISO:MGI.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0061831; C:apical ectoplasmic specialization; ISO:MGI.
DR GO; GO:0061832; C:basal ectoplasmic specialization; ISO:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0097426; C:glial filament; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0002102; C:podosome; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0016528; C:sarcoplasm; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0045159; F:myosin II binding; ISO:MGI.
DR GO; GO:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; IPI:BHF-UCL.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:BHF-UCL.
DR GO; GO:0051693; P:actin filament capping; IDA:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; IMP:BHF-UCL.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; IMP:UniProtKB.
DR GO; GO:0008154; P:actin polymerization or depolymerization; ISO:MGI.
DR GO; GO:1990000; P:amyloid fibril formation; ISO:MGI.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0086003; P:cardiac muscle cell contraction; IMP:BHF-UCL.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
DR GO; GO:0071346; P:cellular response to type II interferon; IDA:MGI.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0097284; P:hepatocyte apoptotic process; ISO:MGI.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:MGI.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
DR GO; GO:0051127; P:positive regulation of actin nucleation; ISO:MGI.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1902174; P:positive regulation of keratinocyte apoptotic process; ISO:MGI.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; IMP:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR GO; GO:1903903; P:regulation of establishment of T cell polarity; ISO:MGI.
DR GO; GO:1903906; P:regulation of plasma membrane raft polarization; ISO:MGI.
DR GO; GO:0071801; P:regulation of podosome assembly; ISO:MGI.
DR GO; GO:1903909; P:regulation of receptor clustering; ISO:MGI.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IMP:BHF-UCL.
DR GO; GO:0097017; P:renal protein absorption; ISO:MGI.
DR GO; GO:0035994; P:response to muscle stretch; IMP:BHF-UCL.
DR GO; GO:0042989; P:sequestering of actin monomers; ISO:MGI.
DR GO; GO:0014891; P:striated muscle atrophy; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:MGI.
DR CDD; cd11290; gelsolin_S1_like; 1.
DR CDD; cd11289; gelsolin_S2_like; 1.
DR CDD; cd11292; gelsolin_S3_like; 1.
DR CDD; cd11293; gelsolin_S4_like; 1.
DR CDD; cd11288; gelsolin_S5_like; 1.
DR CDD; cd11291; gelsolin_S6_like; 1.
DR Gene3D; 3.40.20.10; Severin; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977:SF29; GELSOLIN; 1.
DR PANTHER; PTHR11977; VILLIN; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SUPFAM; SSF55753; Actin depolymerizing proteins; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin capping; Actin-binding;
KW Alternative initiation; Calcium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Disulfide bond; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..780
FT /note="Gelsolin"
FT /id="PRO_0000036387"
FT REPEAT 74..155
FT /note="Gelsolin-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 196..268
FT /note="Gelsolin-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 315..387
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 453..534
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 575..640
FT /note="Gelsolin-like 5"
FT /evidence="ECO:0000255"
FT REPEAT 679..754
FT /note="Gelsolin-like 6"
FT /evidence="ECO:0000255"
FT REGION 51..174
FT /note="Actin-severing"
FT /evidence="ECO:0000255"
FT REGION 121..124
FT /note="Actin-actin interfilament contact point"
FT REGION 244..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..780
FT /note="Actin-binding, Ca-sensitive"
FT /evidence="ECO:0000255"
FT COMPBIAS 244..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="type II"
FT /evidence="ECO:0000269|PubMed:24743229,
FT ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:31199804,
FT ECO:0007744|PDB:4CBU, ECO:0007744|PDB:4CBW,
FT ECO:0007744|PDB:4CBX, ECO:0007744|PDB:5MVV,
FT ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E,
FT ECO:0007744|PDB:6I4F, ECO:0007744|PDB:6I4G,
FT ECO:0007744|PDB:6I4H, ECO:0007744|PDB:6I4I,
FT ECO:0007744|PDB:6I4J, ECO:0007744|PDB:6I4K,
FT ECO:0007744|PDB:6I4L, ECO:0007744|PDB:6I4M"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="type II"
FT /evidence="ECO:0000269|PubMed:24743229,
FT ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:31199804,
FT ECO:0007744|PDB:4CBU, ECO:0007744|PDB:4CBW,
FT ECO:0007744|PDB:4CBX, ECO:0007744|PDB:5MVV,
FT ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E,
FT ECO:0007744|PDB:6I4F, ECO:0007744|PDB:6I4G,
FT ECO:0007744|PDB:6I4H, ECO:0007744|PDB:6I4I,
FT ECO:0007744|PDB:6I4J, ECO:0007744|PDB:6I4K,
FT ECO:0007744|PDB:6I4L, ECO:0007744|PDB:6I4M"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="type II"
FT /evidence="ECO:0000269|PubMed:24743229,
FT ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:31199804,
FT ECO:0007744|PDB:4CBU, ECO:0007744|PDB:4CBW,
FT ECO:0007744|PDB:4CBX, ECO:0007744|PDB:5MVV,
FT ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E,
FT ECO:0007744|PDB:6I4F, ECO:0007744|PDB:6I4G,
FT ECO:0007744|PDB:6I4H, ECO:0007744|PDB:6I4I,
FT ECO:0007744|PDB:6I4J, ECO:0007744|PDB:6I4K,
FT ECO:0007744|PDB:6I4L, ECO:0007744|PDB:6I4M"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="type I"
FT /evidence="ECO:0000269|PubMed:24743229,
FT ECO:0000269|PubMed:31199804, ECO:0007744|PDB:4CBU,
FT ECO:0007744|PDB:4CBW, ECO:0007744|PDB:4CBX,
FT ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E,
FT ECO:0007744|PDB:6I4F, ECO:0007744|PDB:6I4H,
FT ECO:0007744|PDB:6I4I, ECO:0007744|PDB:6I4J,
FT ECO:0007744|PDB:6I4K, ECO:0007744|PDB:6I4L,
FT ECO:0007744|PDB:6I4M"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="type I"
FT /evidence="ECO:0000269|PubMed:24743229,
FT ECO:0000269|PubMed:31199804, ECO:0007744|PDB:4CBU,
FT ECO:0007744|PDB:4CBW, ECO:0007744|PDB:4CBX,
FT ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E,
FT ECO:0007744|PDB:6I4F, ECO:0007744|PDB:6I4H,
FT ECO:0007744|PDB:6I4I, ECO:0007744|PDB:6I4J,
FT ECO:0007744|PDB:6I4K, ECO:0007744|PDB:6I4L,
FT ECO:0007744|PDB:6I4M"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="type I"
FT /evidence="ECO:0000269|PubMed:24743229,
FT ECO:0000269|PubMed:31199804, ECO:0007744|PDB:4CBU,
FT ECO:0007744|PDB:4CBW, ECO:0007744|PDB:4CBX,
FT ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E,
FT ECO:0007744|PDB:6I4F, ECO:0007744|PDB:6I4H,
FT ECO:0007744|PDB:6I4I, ECO:0007744|PDB:6I4J,
FT ECO:0007744|PDB:6I4K, ECO:0007744|PDB:6I4L,
FT ECO:0007744|PDB:6I4M"
FT BINDING 160..167
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 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="type II"
FT /evidence="ECO:0000269|PubMed:24743229,
FT ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:31199804,
FT ECO:0007744|PDB:4CBU, ECO:0007744|PDB:4CBW,
FT ECO:0007744|PDB:4CBX, ECO:0007744|PDB:5MVV,
FT ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E,
FT ECO:0007744|PDB:6I4F, ECO:0007744|PDB:6I4G,
FT ECO:0007744|PDB:6I4H, ECO:0007744|PDB:6I4I,
FT ECO:0007744|PDB:6I4J, ECO:0007744|PDB:6I4K,
FT ECO:0007744|PDB:6I4L, ECO:0007744|PDB:6I4M"
FT BINDING 186..194
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 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="type II"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="type II"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="type II"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="type II"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /ligand_note="type II"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /ligand_note="type II"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /ligand_note="type II"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /ligand_note="type II"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /ligand_note="type II"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /ligand_note="type II"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 512
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /ligand_note="type I"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /ligand_note="type I"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /ligand_note="type I"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 549
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /ligand_note="type II"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT BINDING 589
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /ligand_note="type II"
FT /evidence="ECO:0000269|PubMed:12742020,
FT ECO:0007744|PDB:1NPH"
FT BINDING 590
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /ligand_note="type II"
FT /evidence="ECO:0000269|PubMed:12742020,
FT ECO:0007744|PDB:1NPH"
FT BINDING 612
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /ligand_note="type II"
FT /evidence="ECO:0000269|PubMed:12742020,
FT ECO:0007744|PDB:1NPH"
FT BINDING 694
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /ligand_note="type II"
FT /evidence="ECO:0000269|PubMed:12742020,
FT ECO:0007744|PDB:1NPH"
FT BINDING 695
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /ligand_note="type II"
FT /evidence="ECO:0000269|PubMed:12742020,
FT ECO:0007744|PDB:1NPH"
FT BINDING 717
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /ligand_note="type II"
FT /evidence="ECO:0000269|PubMed:12742020,
FT ECO:0007744|PDB:1NPH"
FT MOD_RES 84
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 407
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 463
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 582
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 601
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 649
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 740
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT DISULFID 213..226
FT /note="In isoform 1"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:2546951"
FT /id="VSP_018960"
FT CONFLICT 262..263
FT /note="GG -> ET (in Ref. 1; AAA37677)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="P -> H (in Ref. 2; BAC41004)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="R -> K (in Ref. 1; AAA37677)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="E -> K (in Ref. 2; BAC41004)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="A -> P (in Ref. 1; AAA37677)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="A -> G (in Ref. 1; AAA37677)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="G -> A (in Ref. 1; AAA37677)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="A -> G (in Ref. 1; AAA37677)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="A -> S (in Ref. 1; AAA37677)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="D -> N (in Ref. 1; AAA37677)"
FT /evidence="ECO:0000305"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:6I4E"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:6I4E"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6I4E"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6I4E"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6I4E"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:6I4E"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:6I4E"
FT HELIX 120..136
FT /evidence="ECO:0007829|PDB:6I4E"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:6I4E"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:6I4E"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:6I4E"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:6I4E"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:1NPH"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 470..477
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:1NPH"
FT HELIX 498..514
FT /evidence="ECO:0007829|PDB:1NPH"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 519..525
FT /evidence="ECO:0007829|PDB:1NPH"
FT HELIX 531..535
FT /evidence="ECO:0007829|PDB:1NPH"
FT TURN 536..539
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 542..546
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 560..568
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 574..579
FT /evidence="ECO:0007829|PDB:1NPH"
FT HELIX 583..585
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 590..595
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 600..604
FT /evidence="ECO:0007829|PDB:1NPH"
FT HELIX 610..623
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 627..631
FT /evidence="ECO:0007829|PDB:1NPH"
FT HELIX 637..643
FT /evidence="ECO:0007829|PDB:1NPH"
FT HELIX 653..656
FT /evidence="ECO:0007829|PDB:1NPH"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 666..671
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 678..681
FT /evidence="ECO:0007829|PDB:1NPH"
FT HELIX 688..690
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 695..700
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 705..709
FT /evidence="ECO:0007829|PDB:1NPH"
FT HELIX 715..729
FT /evidence="ECO:0007829|PDB:1NPH"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:1NPH"
FT STRAND 742..746
FT /evidence="ECO:0007829|PDB:1NPH"
FT HELIX 752..755
FT /evidence="ECO:0007829|PDB:1NPH"
FT INIT_MET P13020-2:1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES P13020-2:1
FT /note="N-acetylmethionine; alternate"
FT /evidence="ECO:0000269|Ref.4"
SQ SEQUENCE 780 AA; 85942 MW; AE94297BE457FF2D CRC64;
MAPYRSSLLC ALLLLALCAL SPSHAATTSR GRAQERAPQS RVSEARPSTM VVEHPEFLKA
GKEPGLQIWR VEKFDLVPVP PNLYGDFFTG DAYVILKTVQ LRNGNLQYDL HYWLGNECSQ
DESGAAAIFT VQLDDYLNGR AVQHREVQGF ESSTFSGYFK SGLKYKKGGV ASGFKHVVPN
EVVVQRLFQV KGRRVVRATE VPVSWDSFNN GDCFILDLGN NIYQWCGSGS NKFERLKATQ
VSKGIRDNER SGRAQVHVSE EGGEPEAMLQ VLGPKPALPE GTEDTAKEDA ANRRLAKLYK
VSNGAGSMSV SLVADENPFA QGALRSEDCF ILDHGRDGKI FVWKGKQANM EERKAALKTA
SDFISKMQYP RQTQVSVLPE GGETPLFKQF FKNWRDPDQT DGPGLGYLSS HIANVERVPF
DAATLHTSTA MAAQHGMDDD GTGQKQIWRI EGSNKVPVDP ATYGQFYGGD SYIILYNYRH
GGRQGQIIYN WQGAQSTQDE VAASAILTAQ LDEELGGTPV QSRVVQGKEP AHLMSLFGGK
PMIIYKGGTS RDGGQTAPAS IRLFQVRASS SGATRAVEVM PKSGALNSND AFVLKTPSAA
YLWVGAGASE AEKTGAQELL KVLRSQHVQV EEGSEPDAFW EALGGKTAYR TSPRLKDKKM
DAHPPRLFAC SNRIGRFVIE EVPGELMQED LATDDVMLLD TWDQVFVWVG KDSQEEEKTE
ALTSAKRYIE TDPANRDRRT PITVVRQGFE PPSFVGWFLG WDDNYWSVDP LDRALAELAA
//
