GELS_HALRO
ID GELS_HALRO Reviewed; 715 AA.
AC O61270;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Gelsolin, cytoplasmic;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
DE AltName: Full=Ascidian gelsolin;
OS Halocynthia roretzi (Sea squirt) (Cynthia roretzi).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC Pyuridae; Halocynthia.
OX NCBI_TaxID=7729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND FUNCTION.
RC TISSUE=Body wall muscle;
RX PubMed=9602133; DOI=10.1016/s0167-4838(97)00211-2;
RA Ohtsuka Y., Nakae H., Abe H., Obinata T.;
RT "Functional characteristics and the complete primary structure of ascidian
RT gelsolin.";
RL Biochim. Biophys. Acta 1383:219-231(1998).
RN [2]
RP IDENTIFICATION OF PROTEIN.
RC TISSUE=Body wall muscle;
RA Ohtsuka Y., Nakae H., Abe H., Obinata T.;
RT "Immunochemical studies of an actin-binding protein in ascidian body wall
RT smooth muscle.";
RL Zool. Sci. 11:407-412(1994).
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. {ECO:0000269|PubMed:9602133}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Predominantly in the body wall muscle, but
CC expression is not restricted to muscle cells.
CC -!- INDUCTION: Interaction with actin is suppressed by PIP2.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; AB009981; BAA28674.1; -; mRNA.
DR AlphaFoldDB; O61270; -.
DR SMR; O61270; -.
DR PRIDE; O61270; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051014; P:actin filament severing; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:InterPro.
DR Gene3D; 3.40.20.10; -; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR030004; Gelsolin.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF27; PTHR11977:SF27; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SUPFAM; SSF82754; SSF82754; 1.
PE 1: Evidence at protein level;
KW Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW Metal-binding; Repeat.
FT CHAIN 1..715
FT /note="Gelsolin, cytoplasmic"
FT /id="PRO_0000218725"
FT REPEAT 24..75
FT /note="Gelsolin-like 1"
FT REPEAT 147..187
FT /note="Gelsolin-like 2"
FT REPEAT 260..306
FT /note="Gelsolin-like 3"
FT REPEAT 405..451
FT /note="Gelsolin-like 4"
FT REPEAT 524..564
FT /note="Gelsolin-like 5"
FT REPEAT 625..667
FT /note="Gelsolin-like 6"
FT REGION 1..124
FT /note="Actin-severing"
FT /evidence="ECO:0000255"
FT REGION 72..75
FT /note="Actin-actin interfilament contact point"
FT REGION 384..715
FT /note="Actin-binding, Ca-sensitive"
FT /evidence="ECO:0000255"
FT BINDING 136..145
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 562
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 665
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 715 AA; 79866 MW; 63AFCC6541255136 CRC64;
MTTELEIQKA GKETGIQIWR IEDFELVPVP KTNHGKFYTG DSYIILKTTA LESGRGFEWN
LHYWQGKESS QDERGAVAIL AVKMDDHLNG GPVEHREVQG NESAAFKGLF PTITYLIGGV
ASGFTHVEIN EVEDRKVLTR VKGKRPVRAT QVPIKWTSLT DSDSYVFDIG KEIYVWSGPK
ASHFEKNKAI QYADGLKNER QGRAELHHID SLDDKESRTM LKDFFGEAFP GSIPSGESDT
VQQVGTTIKL FRISDDSGTL KITLVSENSP FNQGDLSSGD TFVLANARTN HIFVWKGKDS
SRTERASAAN PDNSFFNKIE MPLTSKLTVL PEGGETANFK SLFTNWKSSR DQRGLGQVHS
INKTAKVAKE TFDASVLHSN PKKAAESKMI DDGSGKTQIW RVASLRKEPV PKELYGQFYG
GDCYIIMYTP QRGANVLYYW QGNKASINER TALPIQTKNT HETECDGNAS QIRVVQGTEP
PHMMMLFGGK PLIVHLGDTI SPTGKSKAAS TRLYQVQSFF AGRCRAVEVP AKSSHLNSND
AFLLITPSGS YIWVGKGAVE SEIQGAKDTA GILKISKYEI INENQEPNEF WTALGGQSDY
WRDEREEGVP VEPRLFEMSN ATGNFIAEEI NSNYVQSDLN PDSIMMLDAW NYIYVWIGKE
ANQEEKMSFK SLVDNYVKTD GSGRSKDIPR EVFDQGKEPL SFTGHFLGWD KTLWD
