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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8VIZ

Structure of full-length gelsolin bound to the barbed end of F-actin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0001725cellular_componentstress fiber
A0003785molecular_functionactin monomer binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005523molecular_functiontropomyosin binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0010628biological_processpositive regulation of gene expression
A0016787molecular_functionhydrolase activity
A0019904molecular_functionprotein domain specific binding
A0030027cellular_componentlamellipodium
A0030041biological_processactin filament polymerization
A0030175cellular_componentfilopodium
A0030240biological_processskeletal muscle thin filament assembly
A0031013molecular_functiontroponin I binding
A0031432molecular_functiontitin binding
A0031941cellular_componentfilamentous actin
A0032036molecular_functionmyosin heavy chain binding
A0032432cellular_componentactin filament bundle
A0042802molecular_functionidentical protein binding
A0044297cellular_componentcell body
A0048306molecular_functioncalcium-dependent protein binding
A0048741biological_processskeletal muscle fiber development
A0051017biological_processactin filament bundle assembly
A0090131biological_processmesenchyme migration
A0098723cellular_componentskeletal muscle myofibril
A0140660molecular_functioncytoskeletal motor activator activity
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0001725cellular_componentstress fiber
B0003785molecular_functionactin monomer binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005523molecular_functiontropomyosin binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005865cellular_componentstriated muscle thin filament
B0005884cellular_componentactin filament
B0010628biological_processpositive regulation of gene expression
B0016787molecular_functionhydrolase activity
B0019904molecular_functionprotein domain specific binding
B0030027cellular_componentlamellipodium
B0030041biological_processactin filament polymerization
B0030175cellular_componentfilopodium
B0030240biological_processskeletal muscle thin filament assembly
B0031013molecular_functiontroponin I binding
B0031432molecular_functiontitin binding
B0031941cellular_componentfilamentous actin
B0032036molecular_functionmyosin heavy chain binding
B0032432cellular_componentactin filament bundle
B0042802molecular_functionidentical protein binding
B0044297cellular_componentcell body
B0048306molecular_functioncalcium-dependent protein binding
B0048741biological_processskeletal muscle fiber development
B0051017biological_processactin filament bundle assembly
B0090131biological_processmesenchyme migration
B0098723cellular_componentskeletal muscle myofibril
B0140660molecular_functioncytoskeletal motor activator activity
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0001725cellular_componentstress fiber
C0003785molecular_functionactin monomer binding
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005523molecular_functiontropomyosin binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005865cellular_componentstriated muscle thin filament
C0005884cellular_componentactin filament
C0010628biological_processpositive regulation of gene expression
C0016787molecular_functionhydrolase activity
C0019904molecular_functionprotein domain specific binding
C0030027cellular_componentlamellipodium
C0030041biological_processactin filament polymerization
C0030175cellular_componentfilopodium
C0030240biological_processskeletal muscle thin filament assembly
C0031013molecular_functiontroponin I binding
C0031432molecular_functiontitin binding
C0031941cellular_componentfilamentous actin
C0032036molecular_functionmyosin heavy chain binding
C0032432cellular_componentactin filament bundle
C0042802molecular_functionidentical protein binding
C0044297cellular_componentcell body
C0048306molecular_functioncalcium-dependent protein binding
C0048741biological_processskeletal muscle fiber development
C0051017biological_processactin filament bundle assembly
C0090131biological_processmesenchyme migration
C0098723cellular_componentskeletal muscle myofibril
C0140660molecular_functioncytoskeletal motor activator activity
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0001725cellular_componentstress fiber
D0003785molecular_functionactin monomer binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005523molecular_functiontropomyosin binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005865cellular_componentstriated muscle thin filament
D0005884cellular_componentactin filament
D0010628biological_processpositive regulation of gene expression
D0016787molecular_functionhydrolase activity
D0019904molecular_functionprotein domain specific binding
D0030027cellular_componentlamellipodium
D0030041biological_processactin filament polymerization
D0030175cellular_componentfilopodium
D0030240biological_processskeletal muscle thin filament assembly
D0031013molecular_functiontroponin I binding
D0031432molecular_functiontitin binding
D0031941cellular_componentfilamentous actin
D0032036molecular_functionmyosin heavy chain binding
D0032432cellular_componentactin filament bundle
D0042802molecular_functionidentical protein binding
D0044297cellular_componentcell body
D0048306molecular_functioncalcium-dependent protein binding
D0048741biological_processskeletal muscle fiber development
D0051017biological_processactin filament bundle assembly
D0090131biological_processmesenchyme migration
D0098723cellular_componentskeletal muscle myofibril
D0140660molecular_functioncytoskeletal motor activator activity
E0000166molecular_functionnucleotide binding
E0000287molecular_functionmagnesium ion binding
E0001725cellular_componentstress fiber
E0003785molecular_functionactin monomer binding
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0005523molecular_functiontropomyosin binding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005865cellular_componentstriated muscle thin filament
E0005884cellular_componentactin filament
E0010628biological_processpositive regulation of gene expression
E0016787molecular_functionhydrolase activity
E0019904molecular_functionprotein domain specific binding
E0030027cellular_componentlamellipodium
E0030041biological_processactin filament polymerization
E0030175cellular_componentfilopodium
E0030240biological_processskeletal muscle thin filament assembly
E0031013molecular_functiontroponin I binding
E0031432molecular_functiontitin binding
E0031941cellular_componentfilamentous actin
E0032036molecular_functionmyosin heavy chain binding
E0032432cellular_componentactin filament bundle
E0042802molecular_functionidentical protein binding
E0044297cellular_componentcell body
E0048306molecular_functioncalcium-dependent protein binding
E0048741biological_processskeletal muscle fiber development
E0051017biological_processactin filament bundle assembly
E0090131biological_processmesenchyme migration
E0098723cellular_componentskeletal muscle myofibril
E0140660molecular_functioncytoskeletal motor activator activity
F0000166molecular_functionnucleotide binding
F0000287molecular_functionmagnesium ion binding
F0001725cellular_componentstress fiber
F0003785molecular_functionactin monomer binding
F0005509molecular_functioncalcium ion binding
F0005515molecular_functionprotein binding
F0005523molecular_functiontropomyosin binding
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005856cellular_componentcytoskeleton
F0005865cellular_componentstriated muscle thin filament
F0005884cellular_componentactin filament
F0010628biological_processpositive regulation of gene expression
F0016787molecular_functionhydrolase activity
F0019904molecular_functionprotein domain specific binding
F0030027cellular_componentlamellipodium
F0030041biological_processactin filament polymerization
F0030175cellular_componentfilopodium
F0030240biological_processskeletal muscle thin filament assembly
F0031013molecular_functiontroponin I binding
F0031432molecular_functiontitin binding
F0031941cellular_componentfilamentous actin
F0032036molecular_functionmyosin heavy chain binding
F0032432cellular_componentactin filament bundle
F0042802molecular_functionidentical protein binding
F0044297cellular_componentcell body
F0048306molecular_functioncalcium-dependent protein binding
F0048741biological_processskeletal muscle fiber development
F0051017biological_processactin filament bundle assembly
F0090131biological_processmesenchyme migration
F0098723cellular_componentskeletal muscle myofibril
F0140660molecular_functioncytoskeletal motor activator activity
G0003779molecular_functionactin binding
G0005509molecular_functioncalcium ion binding
G0005515molecular_functionprotein binding
G0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
G0005576cellular_componentextracellular region
G0005615cellular_componentextracellular space
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0005856cellular_componentcytoskeleton
G0005886cellular_componentplasma membrane
G0005925cellular_componentfocal adhesion
G0006911biological_processphagocytosis, engulfment
G0007015biological_processactin filament organization
G0007417biological_processcentral nervous system development
G0008154biological_processactin polymerization or depolymerization
G0010628biological_processpositive regulation of gene expression
G0014891biological_processstriated muscle atrophy
G0015629cellular_componentactin cytoskeleton
G0016528cellular_componentsarcoplasm
G0030027cellular_componentlamellipodium
G0030030biological_processcell projection organization
G0030031biological_processcell projection assembly
G0030036biological_processactin cytoskeleton organization
G0030041biological_processactin filament polymerization
G0030042biological_processactin filament depolymerization
G0030478cellular_componentactin cap
G0030864cellular_componentcortical actin cytoskeleton
G0031648biological_processprotein destabilization
G0034774cellular_componentsecretory granule lumen
G0035994biological_processresponse to muscle stretch
G0036313molecular_functionphosphatidylinositol 3-kinase catalytic subunit binding
G0043065biological_processpositive regulation of apoptotic process
G0045159molecular_functionmyosin II binding
G0045335cellular_componentphagocytic vesicle
G0046597biological_processhost-mediated suppression of symbiont invasion
G0046872molecular_functionmetal ion binding
G0051014biological_processactin filament severing
G0051015molecular_functionactin filament binding
G0051016biological_processbarbed-end actin filament capping
G0051127biological_processpositive regulation of actin nucleation
G0051693biological_processactin filament capping
G0055119biological_processrelaxation of cardiac muscle
G0060271biological_processcilium assembly
G0070062cellular_componentextracellular exosome
G0072562cellular_componentblood microparticle
G0086003biological_processcardiac muscle cell contraction
G0097017biological_processrenal protein absorption
G0097284biological_processhepatocyte apoptotic process
G1902174biological_processpositive regulation of keratinocyte apoptotic process
G1903903biological_processregulation of establishment of T cell polarity
G1903906biological_processregulation of plasma membrane raft polarization
G1903909biological_processregulation of receptor clustering
G1903923biological_processpositive regulation of protein processing in phagocytic vesicle
G1904813cellular_componentficolin-1-rich granule lumen
G1990000biological_processamyloid fibril formation
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63
site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
ATRP356-GLU364
site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues150
DetailsRegion: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues12
DetailsModified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues6
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N-acetylaspartate; in Actin, alpha skeletal muscle","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues82
DetailsRepeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues72
DetailsRepeat: {"description":"Gelsolin-like 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues72
DetailsRepeat: {"description":"Gelsolin-like 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues81
DetailsRepeat: {"description":"Gelsolin-like 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues66
DetailsRepeat: {"description":"Gelsolin-like 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues75
DetailsRepeat: {"description":"Gelsolin-like 6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues123
DetailsRegion: {"description":"Actin-severing","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues3
DetailsRegion: {"description":"Actin-actin interfilament contact point"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues38
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues15
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19666512","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FFK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues15
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16466744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16466744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16466744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine; by SRC; in vitro","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P13020","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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