GELS_PIG
ID GELS_PIG Reviewed; 772 AA.
AC P20305;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Gelsolin;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
DE AltName: Full=Brevin;
DE Flags: Precursor; Fragment;
GN Name=GSN;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE INITIATION.
RX PubMed=2850369; DOI=10.1016/0022-2836(88)90132-5;
RA Way M., Weeds A.G.;
RT "Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence
RT with human gelsolin and other actin-severing proteins shows strong
RT homologies and evidence for large internal repeats.";
RL J. Mol. Biol. 203:1127-1133(1988).
RN [2]
RP PROTEIN SEQUENCE OF 34-72.
RX PubMed=3023087; DOI=10.1111/j.1432-1033.1986.tb10125.x;
RA Weeds A.G., Gooch J., Pope B., Harris H.E.;
RT "Preparation and characterization of pig plasma and platelet gelsolins.";
RL Eur. J. Biochem. 161:69-76(1986).
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 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=P20305-1; Sequence=Displayed;
CC Name=2; Synonyms=Cytoplasmic;
CC IsoId=P20305-2; Sequence=VSP_018961;
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; M36927; AAA31042.1; -; mRNA.
DR EMBL; X13871; CAA32077.1; -; mRNA.
DR PIR; S02665; S02665.
DR AlphaFoldDB; P20305; -.
DR SMR; P20305; -.
DR PeptideAtlas; P20305; -.
DR PRIDE; P20305; -.
DR Ensembl; ENSSSCT00035110269; ENSSSCP00035048068; ENSSSCG00035079388. [P20305-2]
DR Ensembl; ENSSSCT00035110331; ENSSSCP00035048108; ENSSSCG00035079388. [P20305-2]
DR Ensembl; ENSSSCT00065004313; ENSSSCP00065001769; ENSSSCG00065003179. [P20305-2]
DR InParanoid; P20305; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
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:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:BHF-UCL.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; ISS:UniProtKB.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
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:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
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..17
FT /evidence="ECO:0000255"
FT PROPEP 18..33
FT /evidence="ECO:0000269|PubMed:3023087"
FT /id="PRO_0000036389"
FT CHAIN 34..772
FT /note="Gelsolin"
FT /id="PRO_0000036390"
FT REPEAT 66..116
FT /note="Gelsolin-like 1"
FT REPEAT 188..228
FT /note="Gelsolin-like 2"
FT REPEAT 304..346
FT /note="Gelsolin-like 3"
FT REPEAT 443..494
FT /note="Gelsolin-like 4"
FT REPEAT 566..606
FT /note="Gelsolin-like 5"
FT REPEAT 669..711
FT /note="Gelsolin-like 6"
FT REGION 19..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..166
FT /note="Actin-severing"
FT /evidence="ECO:0000255"
FT REGION 113..116
FT /note="Actin-actin interfilament contact point"
FT REGION 424..772
FT /note="Actin-binding, Ca-sensitive"
FT /evidence="ECO:0000255"
FT BINDING 152..159
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 178..186
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 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 541
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 582
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 604
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 686
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 687
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 709
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 399
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 455
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 574
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13020"
FT MOD_RES 593
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 641
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 732
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT DISULFID 205..218
FT /note="In isoform 1"
FT /evidence="ECO:0000250"
FT VAR_SEQ <1..41
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018961"
FT CONFLICT 38
FT /note="R -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 772 AA; 84775 MW; E56111DB9D541BF9 CRC64;
LGALVVALCA LSPPARAATA SRGAPQARAP QGRVSPMRPS TMVVEHPEFL KAGKEPGLQI
WRVEKFDLVP VPPNLYGDFF TGDAYVILKT VQLRNGNLQY DLHYWLGNEC SQDESGAAAI
FTVQLDDYLN GRAVQHREVQ GFESATFLGY FKSGLKYKKG GVASGFKHVV PNEVAVQRLF
QVKGRRVVRA TEVPVSWESF NRGDCFILDL GNDIYQWCGS NSNRYERLKA TQVSKGIRDN
ERSGRAHVHV SEEDAEPAGM LQVLGPKPTL PEGTEDTVKE DAANRKLAKL YKVSNGAGTM
TVSLVADENP FAQGALKSED CFILDHGKDG KIFVWKGKQA NTEERKAALK TASDFISKMN
YPKQTQVSVL PEGGETPLFK QFFKNWRDPD QVDGPGLSYL SSHIANVERV PFDAATLHTS
TAMAAQHGMD DDGTGQKQIW RIEGSNKVPV DPATYGQFYG GDSYIILYNY RHGGRQGQII
YNWQGAQSTQ DEVAASAILT AQLDEELGGT PVQSRVVQGK EPAHLMSLFG GKPMIIYRGG
TSREGGQTAP ASTRLFQVRA SSSGATRAVE VIPKAGALNS NDAFVLKTPS AAYLWVGTGA
SEAEKTGAQE LLRVLRAQPV QVAEGSEPDS FWEALGGKAA YRTSPRLKDK KMDAHPPRLF
ACSNKIGRFV VEEVPGELMQ EDLATDDVML LDTWDQVFVW VGKDSQEEEK TEALTSAKRY
IETDPANRDR RTPINVVKQG FEPPSFVGWF LGWDDNYWSV DPLDRAIAEL AA
