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Database: UniProt
Entry: U6DZB1_NEOVI
LinkDB: U6DZB1_NEOVI
Original site: U6DZB1_NEOVI 
ID   U6DZB1_NEOVI            Unreviewed;       139 AA.
AC   U6DZB1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
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   Name=GELS {ECO:0000313|EMBL:CCP87283.1};
OS   Neovison vison (American mink) (Mustela vison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Neogale.
OX   NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP87283.1};
RN   [1] {ECO:0000313|EMBL:CCP87283.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pool of brain {ECO:0000313|EMBL:CCP87283.1};
RA   Anistoroaei R., Christensen K.;
RT   "An American mink transcriptome.";
RL   Submitted (NOV-2012) 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   -!- SUBUNIT: Binds to actin and to fibronectin. Identified in a complex
CC       composed of ACTA1, COBL, GSN and TMSB4X. Interacts with the inactive
CC       form of EIF2AK2/PKR. {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; HAAF01015463; CCP87283.1; -; mRNA.
DR   AlphaFoldDB; U6DZB1; -.
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; cd11288; gelsolin_S5_like; 1.
DR   Gene3D; 3.40.20.10; Severin; 2.
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; 2.
DR   SMART; SM00262; GEL; 1.
DR   SUPFAM; SSF55753; Actin depolymerizing proteins; 2.
PE   2: Evidence at transcript level;
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}.
FT   DOMAIN          2..56
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   DOMAIN          95..134
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CCP87283.1"
FT   NON_TER         139
FT                   /evidence="ECO:0000313|EMBL:CCP87283.1"
SQ   SEQUENCE   139 AA;  15447 MW;  79FC75EEED1A09A2 CRC64;
     ALNSNDAFVL KTPSAAYLWV GIGAREAEKT GAQELLRVLR AQPVQVAEGS EPDSFWVALG
     GKAAYRTSPR LKDKKMDAHP PRLFACSNKI GRFVIEEVPG ELMQEDLATD DVMLLDTWDQ
     VFVWVGKGFP RRGEDRSIE
//
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