ID A0A091NUR4_HALAL Unreviewed; 710 AA.
AC A0A091NUR4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
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};
DE Flags: Fragment;
GN ORFNames=N329_11717 {ECO:0000313|EMBL:KFP97309.1};
OS Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Haliaeetus.
OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFP97309.1, ECO:0000313|Proteomes:UP000054379};
RN [1] {ECO:0000313|EMBL:KFP97309.1, ECO:0000313|Proteomes:UP000054379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFP97309.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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.
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 EMBL; KK643296; KFP97309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091NUR4; -.
DR Proteomes; UP000054379; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051014; P:actin filament severing; IEA:UniProtKB-UniRule.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:UniProtKB-UniRule.
DR GO; GO:0060271; P:cilium assembly; IEA:UniProtKB-UniRule.
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:UP000054379}.
FT DOMAIN 17..100
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 140..212
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 261..331
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 397..478
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 519..584
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 622..698
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP97309.1"
FT NON_TER 710
FT /evidence="ECO:0000313|EMBL:KFP97309.1"
SQ SEQUENCE 710 AA; 78656 MW; BAD62BD952FD1109 CRC64;
FLKAGKEPGL QIWRIEKFDL VPVPKNLYGD FFSGDSYLVL NTIKQRSGNF QYDLHFWLGD
QSSQDERGAA AIFTVQMDDY LQGKAVQHRE VQGHESSTFL GYFKSGIKYK AGGVASGFRH
VVPNEVTVQR LLQVKGRRTV RAMEVPVTWE SFNTGDCFIL DLGSNIFQWC GSNSNRQERL
KATVLAKGIR DNERNGRAKV YVSEEGSERE EMLQVLGPKP SLPPGASDDT KTDTANRRLA
KLYKVSNGAG NMAVSLVADD NPFSQAALNT DDCFILDHGT DGKIFVWKGK GANSDEKKAA
LKTASEFIDK MGYPKHTQVQ VLPESGETPL FKQFFKNWRD KDQTEGLGQA YISGHVAKIE
KVPFDAATLH TSKAMAAQHG MEDDGSGRKQ IWRIEGSEKV PVDPSTYGQF YGGDSYIILY
NYQHGGKQGQ IIYTWQGADS TQDEIATSAF LTVQLDEELG GSPVQKRVVQ GKEPPHLMSM
FGGKPLIVYK GGTSREGGQT APAEMRLFQV RSSTSGATRA VELDPTASQL NSNDAFVLKT
PSAAYLWVGQ GASDAEKSGA QELLKLLGAR PVQVSEGREP DNFWAALGGK APYRTSPRLK
DKKMDAHPPR LFACSNKSGR FTIEEVPGDL TQEDLATDDV MLLDTWDQVF VWIGKDAQEE
EKTEALKSAK RYIETDPASR DKRTPITVVK QGLEPPTFSG WFLGWDDDYW
//
