GELS_CHICK
ID GELS_CHICK Reviewed; 778 AA.
AC O93510;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Gelsolin;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
DE AltName: Full=Brevin;
DE AltName: Full=Homogenin;
DE Flags: Precursor;
GN Name=GSN;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=White leghorn; TISSUE=Basilar papilla;
RX PubMed=9736748; DOI=10.1073/pnas.95.19.11400;
RA Heller S., Sheane C.A., Javed Z., Hudspeth A.J.;
RT "Molecular markers for cell types of the inner ear and candidate genes for
RT hearing disorders.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11400-11405(1998).
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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=A cytoplasmic form may also exist. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in homogene cells of the basilar
CC papilla. Also detected in subcutaneous layer of the skin.
CC {ECO:0000269|PubMed:9736748}.
CC -!- DOMAIN: Comprises six structurally related domains, in a calcium-free
CC environment, pack together to form a compact globular structure in
CC which the putative actin-binding sequences are not sufficiently exposed
CC to enable binding to occur. Binding calcium may release the connections
CC that join the N- and C-terminal halves of gelsolin, enabling each half
CC to bind actin relatively independently. The severing and capping
CC properties of gelsolin are inhibited by binding polyphosphoinositides.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; AF042795; AAC62928.1; -; mRNA.
DR RefSeq; NP_990265.1; NM_204934.1.
DR AlphaFoldDB; O93510; -.
DR SMR; O93510; -.
DR BioGRID; 676048; 1.
DR IntAct; O93510; 1.
DR STRING; 9031.ENSGALP00000002197; -.
DR PaxDb; O93510; -.
DR PRIDE; O93510; -.
DR GeneID; 395774; -.
DR KEGG; gga:395774; -.
DR CTD; 2934; -.
DR VEuPathDB; HostDB:geneid_395774; -.
DR eggNOG; KOG0443; Eukaryota.
DR InParanoid; O93510; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; O93510; -.
DR PRO; PR:O93510; -.
DR Proteomes; UP000000539; 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 Actin capping; Actin-binding; Calcium; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Disulfide bond; Metal-binding; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..778
FT /note="Gelsolin"
FT /id="PRO_0000036392"
FT REPEAT 72..122
FT /note="Gelsolin-like 1"
FT REPEAT 194..234
FT /note="Gelsolin-like 2"
FT REPEAT 310..352
FT /note="Gelsolin-like 3"
FT REPEAT 449..500
FT /note="Gelsolin-like 4"
FT REPEAT 572..612
FT /note="Gelsolin-like 5"
FT REPEAT 675..717
FT /note="Gelsolin-like 6"
FT REGION 49..172
FT /note="Actin-severing"
FT /evidence="ECO:0000255"
FT REGION 119..122
FT /note="Actin-actin interfilament contact point"
FT REGION 430..778
FT /note="Actin-binding, Ca-sensitive"
FT /evidence="ECO:0000255"
FT BINDING 158..165
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 184..192
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 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 588
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 610
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 692
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 693
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 715
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT DISULFID 211..224
FT /evidence="ECO:0000250"
SQ SEQUENCE 778 AA; 85832 MW; 7C8DFB0336B068FD CRC64;
MGKQGFGYIF LTIFCTMALK LNCVSSVSVA GLGYVVTAAV VLSAVPVSMV EHAEFSKAGK
EPGLQIWRIE KFDLVPVPKN LYGDFFTGDS YLVLNTIRQR SGNLQYDLHF WLGDESSQDE
RGAAAIFTVQ MDDYLQGKAV QHREVQGHES STFLGYFKSG IKYKAGGVAS GFRHVVPNEV
TVQRLLQVKG RRTVRATEVP VSWESFNTGD CFILDLGSNI YQWCGSNSNR QERLKATVLA
KGIRDNEKNG RAKVFVSEEG AEREEMLQVL GPKPSLPQGA SDDTKTDTAN RKLAKLYKVS
NGAGNMAVSL VADENPFSQA ALNTEDCFIL DHGTDGKIFV WKGRSANSDE RKAALKTATD
FIDKMGYPKH TQVQVLPESG ETPLFKQFFK NWRDKDQTEG LGEAYISGHV AKIEKVPFDA
ATLHTSRAMA AQHGMEDDGS GKKQIWRIEG SEKVPVDPAT YGQFYGGDSY IILYDYRHAG
KQGQIIYTWQ GAHSTQDEIA TSAFLTVQLD EELGGSPVQK RVVQGKEPPH LMSMFGGKPL
IVYKGGTSRE GGQTTPAQTR LFQVRSSTSG ATRAVELDPA ASQLNSNDAF VLKTPSAAYL
WVGRGSNSAE LSGAQELLKV LGARPVQVSE GREPDNFWVA LGGKAPYRTS PRLKDKKMDA
YPPRLFACSN KSGRFTIEEV PGDLTQDDLA TDDVMILDTW DQVFVWIGKD AQEEEKTEAL
KSAKRYIETD PASRDKRTPV TLVKQGLEPP TFSGWFLGWD DDYWSVDPLQ RAMADVDV
