ID A0A093SM70_9PASS Unreviewed; 710 AA.
AC A0A093SM70;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=N305_12860 {ECO:0000313|EMBL:KFW83739.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW83739.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW83739.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW83739.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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; KL671828; KFW83739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093SM70; -.
DR STRING; 328815.ENSMVIP00005014832; -.
DR Proteomes; UP000053258; 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:UP000053258}.
FT DOMAIN 17..100
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 139..212
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 258..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:KFW83739.1"
FT NON_TER 710
FT /evidence="ECO:0000313|EMBL:KFW83739.1"
SQ SEQUENCE 710 AA; 78706 MW; 9338D471D263BA4C CRC64;
FLKAGKEPGL QIWRVEKFDL VPVPKNLYGD FFTGDSYLVL NTIKQRSGNL QYDLHFWLGD
ESSQDERGAA AIFTVQMDDH LQGRAVQHRE VQGHESPTFL GYFKSGIKYK AGGVASGFRH
VVPNEVTVQR LLQVKGRRTV RATEVPVSWD SFNTGDCFIL DLGSNIFQWC GSNSNRQERL
KATVLAKGIR DNERNGRAKV YVSEEGSERE EMLQVLGPKP TLPPGVSDET KTDTANRKLA
KLYKVSNGAG NMAVSLVADE NPFSQAALST DDCFILDHGT DGKIFVWKGK GANSEEKKAA
LKTASEFIDK MGYPKHTQIQ VLPESGETPL FKQFFKNWRD KDQTEGLGQA HVSGHIAKIE
QVPFDAATLH SSRAMAAQHG MEDDGSGKKQ IWRIEGSEKV PVNPATYGQF YGGDSYIILY
DYQHDGRKGQ IIYTWQGADS TQDEIATSAF LTVQLDEELG GSPVQKRVVQ GKEPPHLMSM
FGGKPLIVYK GGTSREGGQT APAETRLFQV RSSTSGATRA VELDPTASQL NSNDAFVLKT
PSAAYLWVGQ GASNAEKSGA QELLKILGAR PVQVSEGREP DNFWAALGGK APYRTSPRLK
DKKMDTHPPR LFACSNKSGH FTIEEVPGDL TQDDLATDDV MILDTWDQVF VWIGQDAQEE
EKTEALKSAK RYIDTDPSNR DKRTPVTIIK QGFEPPTFSG WFLGWDDQYW
//
