ID U3JGR5_FICAL Unreviewed; 869 AA.
AC U3JGR5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Gelsolin {ECO:0000256|ARBA:ARBA00018797, ECO:0000256|RuleBase:RU367130};
DE Short=ADF {ECO:0000256|RuleBase:RU367130};
DE AltName: Full=Actin-depolymerizing factor {ECO:0000256|RuleBase:RU367130};
GN Name=GSN {ECO:0000313|Ensembl:ENSFALP00000001969.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000001969.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000001969.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000001969.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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.
CC {ECO:0000256|RuleBase:RU367130}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|RuleBase:RU367130}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family.
CC {ECO:0000256|RuleBase:RU367130}.
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DR AlphaFoldDB; U3JGR5; -.
DR STRING; 59894.ENSFALP00000001969; -.
DR Ensembl; ENSFALT00000001981.2; ENSFALP00000001969.1; ENSFALG00000001837.2.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000155591; -.
DR HOGENOM; CLU_002568_3_1_1; -.
DR OMA; HYWDDAE; -.
DR Proteomes; UP000016665; Chromosome 17.
DR GO; GO:0030478; C:actin cap; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0002102; C:podosome; IEA:Ensembl.
DR GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0045159; F:myosin II binding; IEA:Ensembl.
DR GO; GO:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; IEA:Ensembl.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:Ensembl.
DR GO; GO:0030041; P:actin filament polymerization; IEA:Ensembl.
DR GO; GO:0051014; P:actin filament severing; IEA:UniProtKB-UniRule.
DR GO; GO:1990000; P:amyloid fibril formation; IEA:Ensembl.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:UniProtKB-UniRule.
DR GO; GO:0086003; P:cardiac muscle cell contraction; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0006911; P:phagocytosis, engulfment; IEA:Ensembl.
DR GO; GO:0051127; P:positive regulation of actin nucleation; IEA:Ensembl.
DR GO; GO:1902174; P:positive regulation of keratinocyte apoptotic process; IEA:Ensembl.
DR GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:1903903; P:regulation of establishment of T cell polarity; IEA:Ensembl.
DR GO; GO:1903906; P:regulation of plasma membrane raft polarization; IEA:Ensembl.
DR GO; GO:0071801; P:regulation of podosome assembly; IEA:Ensembl.
DR GO; GO:1903909; P:regulation of receptor clustering; IEA:Ensembl.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
DR GO; GO:0097017; P:renal protein absorption; IEA:Ensembl.
DR GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
DR GO; GO:0042989; P:sequestering of actin monomers; IEA:Ensembl.
DR GO; GO:0014891; P:striated muscle atrophy; IEA:Ensembl.
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 3: Inferred from homology;
KW Actin capping {ECO:0000256|RuleBase:RU367130};
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW ECO:0000256|RuleBase:RU367130};
KW Cilium biogenesis/degradation {ECO:0000256|ARBA:ARBA00022794};
KW Cytoplasm {ECO:0000256|RuleBase:RU367130};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT DOMAIN 162..245
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 284..357
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 403..476
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 542..623
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 664..729
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 767..843
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 348..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 95303 MW; CF4BEC24B727A7FB CRC64;
MSLNLCPCDP VANGSHIVCS ECCWARGSEE PLGFQQDCLH KAFRPCAAEG VGVFVPDKRL
ASALHPPQQP EEQGAATPHS SAGEGAHLLL GMGRKDFNFL FLAILCTMAL KLSCVSSMSV
AGLGYVVTAA LVLSAVPVSM VEHAEFLKAG KEPGLQIWRV EKFDLVPVPK NLYGDFFTGD
SYLVLNTIKQ RSGNLQYDLH FWLGDESSQD ERGAAAIFTV QMDEHLQGKA VQHREVQGHE
SPTFLGYFKS GIKYKAGGVA SGFRHVVPNE VTVQRLLQVK GRRTVRATEV PVSWDSFNTG
DCFILDLGSN IFQWCGSKSN RQERLKATVL AKGIRDNERN GRAKVYVSEE GSEREEMLQV
LGPKPSLPEG ASDETKTDTA NRKLAKLYKV SNGAGNMAVS LVADENPFSQ AALSTDDCFI
LDHGTDGKIF VWKGRGANSE EKKAALKTAS EFIDKMGYPK HTQIQVLPES GETPLFKQFF
KNWRDKDQTE GLGQPHVSGH VAKIEQVPFD AATLHSSKAM AAQHGMEDDG SGKKQIWRIE
GSEKVPVDPA TYGQFYGGDS YIILYDYQHD GKRGQIIYTW QGADSTQDEI TTSAFLTVQL
DEELGGSPVQ KRVVQGKEPP HLMSMFGGKP LIVYKGGTSR EGGQTAPAAT RLFQVRSSTS
GATRAVELDP TASQLNSNDA FVLKTPSAAY LWVGQGASNA EKSGAQELLK ILGARPVQVA
EGKEPENFWA ALGGKAPYRT SPRLKDKKMD THPPRLFACS NKSGRFTIEE VPGDLTQDDL
ATDDVMLLDT WDQVFVWIGK DAQEEEKTEA LKSAKRYIDT DPSTRDKRTP VTIVKQGFEP
PTFSGWFLGW DDDYWAVDPL QRAMADVDV
//