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 24-JAN-2024, entry version 120. 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 (By similarity). Plays a role in ciliogenesis (By CC similarity). {ECO:0000250|UniProtKB:P06396}. 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 gelsolin-like (G1-G6) CC domains, that, in a calcium-free environment, are packed together to CC form a compact globular structure in which the putative actin-binding CC sequences are not sufficiently exposed to enable binding to occur. CC Binding calcium may release the connections that join the N- and C- CC terminal halves of gelsolin, enabling each half to bind actin CC relatively independently. G1 and G4 bind two Ca(2+) in a type I and in CC a type II manner. G2, G3, G5 and G6 bind only one Ca(2+) in a type II CC manner. Type I Ca(2+) binding sites are shared between actin and CC gelsolin-like repeats G1 and G4. Type I binding governs the strength of CC interactions between gelsolin and actin by direct participation at the CC binding interface. Ca(2+) binding to G2 and G6 disrupts the CC interactions between G2 and G6, releases the C-terminal tail, and CC induces large interdomain rearrangements that result in the exposure of CC the F-actin-binding site on G2 and contributes to the activation of CC gelsolin. Binding to phosphoinositides may inhibit the severing and CC capping properties of gelsolin. {ECO:0000250|UniProtKB:P06396}. 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; 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.ENSGALP00000054518; -. DR PaxDb; 9031-ENSGALP00000002197; -. DR GeneID; 395774; -. DR KEGG; gga:395774; -. DR CTD; 2934; -. DR VEuPathDB; HostDB:geneid_395774; -. DR eggNOG; KOG0443; Eukaryota. DR InParanoid; O93510; -. DR PhylomeDB; O93510; -. DR PRO; PR:O93510; -. DR Proteomes; UP000000539; Unassembled WGS sequence. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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: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 CDD; cd11290; gelsolin_S1_like; 1. DR CDD; cd11289; gelsolin_S2_like; 1. DR CDD; cd11292; gelsolin_S3_like; 1. DR CDD; cd11293; gelsolin_S4_like; 1. DR CDD; cd11288; gelsolin_S5_like; 1. DR CDD; cd11291; gelsolin_S6_like; 1. DR Gene3D; 3.40.20.10; Severin; 6. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf. DR InterPro; IPR007123; Gelsolin-like_dom. DR InterPro; IPR007122; Villin/Gelsolin. DR PANTHER; PTHR11977:SF29; GELSOLIN; 1. DR PANTHER; PTHR11977; VILLIN; 1. DR Pfam; PF00626; Gelsolin; 6. DR PRINTS; PR00597; GELSOLIN. DR SMART; SM00262; GEL; 6. DR SUPFAM; SSF55753; Actin depolymerizing proteins; 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..154 FT /note="Gelsolin-like 1" FT /evidence="ECO:0000255" FT REPEAT 193..266 FT /note="Gelsolin-like 2" FT /evidence="ECO:0000255" FT REPEAT 313..385 FT /note="Gelsolin-like 3" FT /evidence="ECO:0000255" FT REPEAT 451..532 FT /note="Gelsolin-like 4" FT /evidence="ECO:0000255" FT REPEAT 574..638 FT /note="Gelsolin-like 5" FT /evidence="ECO:0000255" FT REPEAT 677..752 FT /note="Gelsolin-like 6" FT /evidence="ECO:0000255" 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 88 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 89 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 120 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 132 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="type I" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 137 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="type I" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 139 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="type I" FT /evidence="ECO:0000250|UniProtKB:P06396" 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 168 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" 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 209 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 210 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 232 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 282 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 325 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 326 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 350 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 467 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 468 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 498 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 510 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /ligand_note="type I" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 515 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /ligand_note="type I" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 517 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /ligand_note="type I" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 547 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 587 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 588 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 610 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 692 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 693 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT BINDING 715 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /ligand_note="type II" FT /evidence="ECO:0000250|UniProtKB:P06396" FT DISULFID 211..224 FT /evidence="ECO:0000250|UniProtKB:P06396" 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 //