UniProt Accession

 GELS_MOUSE; P13020; Q3UPB1; Q8R590 

Genbank Protein ID

 J04953; AK076156; AK089934; AK143664; BC023143 

Genbank Nucleotide ID

 AAA37677.1; BAC36223.1; BAC41004.1; BAE25485.1; AAH23143.2 

Protein Name

 Gelsolin 

Protein Synonyms/Alias

 Actin-depolymerizing factor; ADF; Brevin 

Gene Name

 Gsn 

Gene Synonyms/Alias

 Gsb 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
175	GGVASGFKHVVPNEV	ubiquitination	[1]
191	VQRLFQVKGRRVVRA	ubiquitination	[1]
243	LKATQVSKGIRDNER	ubiquitination	[1]
358	EERKAALKTASDFIS	ubiquitination	[1]
366	TASDFISKMQYPRQT	acetylation	[2, 3]
366	TASDFISKMQYPRQT	ubiquitination	[1]
392	PLFKQFFKNWRDPDQ	acetylation	[3]
540	LMSLFGGKPMIIYKG	acetylation	[4]
546	GKPMIIYKGGTSRDG	acetylation	[2]
582	RAVEVMPKSGALNSN	acetylation	[3, 4]
582	RAVEVMPKSGALNSN	ubiquitination	[1]
595	SNDAFVLKTPSAAYL	ubiquitination	[1]
621	TGAQELLKVLRSQHV	acetylation	[2, 3, 4]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 

Functional Description

 Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. 

Sequence Annotation

 REPEAT 74 124 Gelsolin-like 1.
 REPEAT 196 236 Gelsolin-like 2.
 REPEAT 312 354 Gelsolin-like 3.
 REPEAT 451 502 Gelsolin-like 4.
 REPEAT 574 614 Gelsolin-like 5.
 REPEAT 677 719 Gelsolin-like 6.
 REGION 51 174 Actin-severing (Potential).
 REGION 121 124 Actin-actin interfilament contact point.
 REGION 160 167 Polyphosphoinositide binding (By
 REGION 186 194 Polyphosphoinositide binding (By
 REGION 432 780 Actin-binding, Ca-sensitive (Potential).
 METAL 469 469 Calcium 1; via carbonyl oxygen (By
 METAL 470 470 Calcium 1 (By similarity).
 METAL 500 500 Calcium 1 (By similarity).
 METAL 549 549 Calcium 1; via carbonyl oxygen (By
 METAL 589 589 Calcium 2 (By similarity).
 METAL 589 589 Calcium 2; via carbonyl oxygen (By
 METAL 590 590 Calcium 2 (By similarity).
 METAL 612 612 Calcium 2 (By similarity).
 METAL 694 694 Calcium 3; via carbonyl oxygen (By
 METAL 695 695 Calcium 3 (By similarity).
 METAL 717 717 Calcium 3 (By similarity).
 MOD_RES 84 84 Phosphotyrosine (By similarity).
 MOD_RES 407 407 Phosphotyrosine (By similarity).
 MOD_RES 463 463 Phosphotyrosine (By similarity).
 MOD_RES 601 601 Phosphotyrosine (By similarity).
 MOD_RES 649 649 Phosphotyrosine (By similarity).
 DISULFID 213 226 In isoform 1 (By similarity).  

Keyword

 3D-structure; Acetylation; Actin capping; Actin-binding; Alternative initiation; Calcium; Cilium biogenesis/degradation; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disulfide bond; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 780 AA 

Protein Sequence

Gene Ontology

 GO:0015629; C:actin cytoskeleton; IEA:Compara.
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005576; C:extracellular region; ISS:UniProtKB.
 GO:0005615; C:extracellular space; IEA:Compara.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0030027; C:lamellipodium; IDA:MGI.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0001726; C:ruffle; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
 GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
 GO:0051014; P:actin filament severing; ISS:UniProtKB.
 GO:0007568; P:aging; IEA:Compara.
 GO:0006915; P:apoptotic process; IEA:Compara.
 GO:0071276; P:cellular response to cadmium ion; IEA:Compara.
 GO:0060271; P:cilium morphogenesis; ISS:UniProtKB.
 GO:0014003; P:oligodendrocyte development; IEA:Compara.
 GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:Compara.
 GO:0030155; P:regulation of cell adhesion; IEA:Compara.
 GO:0045471; P:response to ethanol; IEA:Compara.
 GO:0051593; P:response to folic acid; IEA:Compara.
 GO:0042246; P:tissue regeneration; IEA:Compara.
 GO:0016192; P:vesicle-mediated transport; IMP:MGI. 

Interpro

 IPR007123; Gelsolin_dom.
 IPR007122; Villin/Gelsolin. 

Pfam

 PF00626; Gelsolin 

SMART

 SM00262; GEL 

PROSITE

  

PRINTS

 PR00597; GELSOLIN.