GELS_RAT
ID GELS_RAT Reviewed; 780 AA.
AC Q68FP1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Gelsolin;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
DE AltName: Full=Brevin;
DE Flags: Precursor;
GN Name=Gsn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [2]
RP PROTEIN SEQUENCE OF 301-325; 396-417; 583-595 AND 614-621, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
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. Plays a role in ciliogenesis (By similarity).
CC {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=A cytoplasmic form may also exist. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=Secreted, Plasma;
CC IsoId=Q68FP1-1; Sequence=Displayed;
CC Name=2; Synonyms=Cytoplasmic;
CC IsoId=Q68FP1-2; Sequence=VSP_036722;
CC -!- PTM: Phosphorylated on tyrosine residues in vitro. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {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; BC079472; AAH79472.1; -; mRNA.
DR RefSeq; NP_001004080.1; NM_001004080.1. [Q68FP1-1]
DR RefSeq; XP_006234102.1; XM_006234040.2. [Q68FP1-2]
DR AlphaFoldDB; Q68FP1; -.
DR SMR; Q68FP1; -.
DR BioGRID; 255439; 5.
DR CORUM; Q68FP1; -.
DR IntAct; Q68FP1; 7.
DR MINT; Q68FP1; -.
DR STRING; 10116.ENSRNOP00000025857; -.
DR iPTMnet; Q68FP1; -.
DR PhosphoSitePlus; Q68FP1; -.
DR jPOST; Q68FP1; -.
DR PaxDb; Q68FP1; -.
DR PeptideAtlas; Q68FP1; -.
DR PRIDE; Q68FP1; -.
DR Ensembl; ENSRNOT00000025857; ENSRNOP00000025857; ENSRNOG00000018991. [Q68FP1-1]
DR GeneID; 296654; -.
DR KEGG; rno:296654; -.
DR UCSC; RGD:1303089; rat. [Q68FP1-1]
DR CTD; 2934; -.
DR RGD; 1303089; Gsn.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000155591; -.
DR InParanoid; Q68FP1; -.
DR OMA; DNRTKTH; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; Q68FP1; -.
DR Reactome; R-RNO-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q68FP1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000018991; Expressed in lung and 20 other tissues.
DR Genevisible; Q68FP1; RN.
DR GO; GO:0030478; C:actin cap; ISO:RGD.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:RGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0002102; C:podosome; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0001726; C:ruffle; IDA:RGD.
DR GO; GO:0016528; C:sarcoplasm; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0045159; F:myosin II binding; ISO:RGD.
DR GO; GO:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0051693; P:actin filament capping; ISO:RGD.
DR GO; GO:0030042; P:actin filament depolymerization; ISO:RGD.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0090527; P:actin filament reorganization; ISO:RGD.
DR GO; GO:0051014; P:actin filament severing; IMP:RGD.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:1990000; P:amyloid fibril formation; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IDA:RGD.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0086003; P:cardiac muscle cell contraction; ISO:RGD.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0071276; P:cellular response to cadmium ion; IDA:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
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:RGD.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:RGD.
DR GO; GO:0014003; P:oligodendrocyte development; IEP:RGD.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISO:RGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:RGD.
DR GO; GO:0051127; P:positive regulation of actin nucleation; ISO:RGD.
DR GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1902174; P:positive regulation of keratinocyte apoptotic process; ISO:RGD.
DR GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; ISO:RGD.
DR GO; GO:0031648; P:protein destabilization; ISO:RGD.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:RGD.
DR GO; GO:1903903; P:regulation of establishment of T cell polarity; ISO:RGD.
DR GO; GO:1903906; P:regulation of plasma membrane raft polarization; ISO:RGD.
DR GO; GO:0071801; P:regulation of podosome assembly; ISO:RGD.
DR GO; GO:1903909; P:regulation of receptor clustering; ISO:RGD.
DR GO; GO:0055119; P:relaxation of cardiac muscle; ISO:RGD.
DR GO; GO:0097017; P:renal protein absorption; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0051593; P:response to folic acid; IEP:RGD.
DR GO; GO:0035994; P:response to muscle stretch; ISO:RGD.
DR GO; GO:0042989; P:sequestering of actin monomers; ISO:RGD.
DR GO; GO:0014891; P:striated muscle atrophy; ISO:RGD.
DR GO; GO:0042246; P:tissue regeneration; IEP:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
DR Gene3D; 3.40.20.10; -; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR030004; Gelsolin.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF27; PTHR11977:SF27; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
PE 1: Evidence at protein level;
KW Acetylation; Actin capping; Actin-binding; Alternative initiation; Calcium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disulfide bond; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..780
FT /note="Gelsolin"
FT /id="PRO_0000288477"
FT REPEAT 74..124
FT /note="Gelsolin-like 1"
FT REPEAT 196..236
FT /note="Gelsolin-like 2"
FT REPEAT 312..354
FT /note="Gelsolin-like 3"
FT REPEAT 451..502
FT /note="Gelsolin-like 4"
FT REPEAT 574..614
FT /note="Gelsolin-like 5"
FT REPEAT 677..719
FT /note="Gelsolin-like 6"
FT REGION 28..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..174
FT /note="Actin-severing"
FT /evidence="ECO:0000255"
FT REGION 121..124
FT /note="Actin-actin interfilament contact point"
FT /evidence="ECO:0000250"
FT REGION 244..286
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 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 549
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 589
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 590
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 612
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 694
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 695
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 717
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
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:0000250|UniProtKB:P13020"
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 /evidence="ECO:0000250"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036722"
SQ SEQUENCE 780 AA; 86068 MW; E9B6A20C5A80D0E8 CRC64;
MAPYCSSLRS ALLVLALCAL SPSHAATASR GRAQERAPQS RVSETRPSTM VVEHPEFLKA
GKEPGLQIWR VEKFDLVPVP PNLYGDFFTG DAYVILKTVQ LRNGNLQYDL HYWLGNECSQ
DESGAAAIFT VQLDDYLNGR AVQHREVQGF ESSTFQGYFK SGLKYKKGGV ASGFKHVVPN
EVVVQRLFQV KGRRVVRATE VPVSWDSFNN GDCFILDLGN NIYQWCGSGS NKFERLKATQ
VSKGIRDNER SGRAQVHVSE EGSEPEAMLQ VLGPKPDLPQ GTEDTAKEDA ANRRLAKLYK
VSNSGGSMSV SLVADENPFA QSALRSEDCF ILDHGRDGKI FVWKGKQANM DERKAALKTA
SDFISKMQYP RQTQVSVLPE GGETPLFKQF FKNWRDPDQT DGPGLSYLSS HIANVERVPF
DAATLHTSTA MAAQHGMDDD GTGQKQIWRI EGSNKVLVDP ATYGQFYGGD SYIILYNYRH
GGRQGQIIYN WQGAQSTQDE VAASAILTAQ LDEELGGTPV QSRVVQGKEP AHLMSLFGGK
PMIIYKGGTS RDGGQTTPAS TRLFQVRASS SGATRAVEVM PKAGALNSND AFVLKTPSAA
YLWVGTGASD AEKTGALELL KVLRAQHVQV EEGSEPDGFW EALGGKTAYR TSPRLKDKKM
DAHPPRLFAC SNRIGRFVIE EVPGELMQED LATDDVMLLD TWDQVFVWVG KDSQEEEKTE
ALTSAKRYIE TDPANRDRRT PITVVRQGFE PPSFVGWFLG WDDDYWSVDP LDRALAELAA
