GELS_BOVIN
ID GELS_BOVIN Reviewed; 731 AA.
AC Q3SX14;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Gelsolin;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
DE AltName: Full=Brevin;
GN Name=GSN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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. 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: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; BC104560; AAI04561.1; -; mRNA.
DR RefSeq; NP_001029799.1; NM_001034627.1.
DR AlphaFoldDB; Q3SX14; -.
DR SMR; Q3SX14; -.
DR STRING; 9913.ENSBTAP00000026534; -.
DR PaxDb; Q3SX14; -.
DR PeptideAtlas; Q3SX14; -.
DR PRIDE; Q3SX14; -.
DR GeneID; 535077; -.
DR KEGG; bta:535077; -.
DR CTD; 2934; -.
DR eggNOG; KOG0443; Eukaryota.
DR InParanoid; Q3SX14; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0051014; P:actin filament severing; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Actin capping; Actin-binding; Calcium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Disulfide bond;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..731
FT /note="Gelsolin"
FT /id="PRO_0000367499"
FT REPEAT 25..75
FT /note="Gelsolin-like 1"
FT REPEAT 147..187
FT /note="Gelsolin-like 2"
FT REPEAT 263..305
FT /note="Gelsolin-like 3"
FT REPEAT 402..453
FT /note="Gelsolin-like 4"
FT REPEAT 525..565
FT /note="Gelsolin-like 5"
FT REPEAT 628..670
FT /note="Gelsolin-like 6"
FT REGION 2..125
FT /note="Actin-severing"
FT /evidence="ECO:0000255"
FT REGION 72..75
FT /note="Actin-actin interfilament contact point"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..731
FT /note="Actin-binding, Ca-sensitive"
FT /evidence="ECO:0000255"
FT COMPBIAS 197..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111..118
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 137..145
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 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 451
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 540
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 541
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 563
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 358
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 414
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 533
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13020"
FT MOD_RES 552
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 600
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 691
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT DISULFID 164..177
FT /evidence="ECO:0000250"
SQ SEQUENCE 731 AA; 80731 MW; 2418C22B9B598E1E CRC64;
MVVEHPEFLK AGKEPGLQIW RVEKFDLVPV PPNLYGDFFT GDAYVILKTV QLRNGNLQYD
LHYWLGNECS QDESGAAAIF TVQLDDYLNG RAVQHREVQG FESATFLGYF KSGLKYKKGG
VASGFKHVVP NEVVVQRLFQ VKGRRVVRAT EVPVSWESFN NGDCFILDLG NDIYQWCGSS
SNRFERLKAT QVSKGIRDNE RSGRARVHVS EEGAEPEAML EVLGPKPALP AGTEDTAKED
AANRKLAKLY KVSNGAGTMS VSLVADENPF AQGALRSEDC FILDHGKDGK IFVWKGRQAN
TEERKAALKT ASDFISKMDY PRQTQVSVLP EGGETPLFKQ FFKNWRDPDQ TDGPGLSYLS
SHIANVERVP FDAATLHTST AMAAQHGMDD DGRGQKQIWR IEGSDKVPVD PATYGQFYGG
DSYIILYNYR HGGRQGQIIY NWQGAQSTQD EVAASAILTA QLDEELGGTP VRSRVVQGKE
PAHLMSLFGG KPMIIYRGGT SREGGQTAPA STRLFQVRAS SSGATRAVEV MPKAGALNSN
DAFVLKTPSA AYLWVGAGAS EAEKTGALEL LRVLRAQPVQ VAEGSEPDSF WEALGGKAAY
RTSPRLKDKK MDAHPPRLFA CSNKIGRFVI EEVPGELMQE DLATDDVMLL DTWDQVFVWV
GKDSQEEEKT EALTSAKRYI ETDPANRDRR TPITVVKQGF EPPSFVGWFL GWDDNYWSVD
PLDRALAELA A
