GELS_HOMAM
ID GELS_HOMAM Reviewed; 754 AA.
AC Q27319;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Gelsolin, cytoplasmic;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
OS Homarus americanus (American lobster).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Nephropoidea; Nephropidae; Homarus.
OX NCBI_TaxID=6706;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 360-395 AND 514-544.
RC TISSUE=Tail muscle;
RX PubMed=7848275; DOI=10.1042/bj3050767;
RA Lueck A., D'Haese J., Hinssen H.;
RT "A gelsolin-related protein from lobster muscle: cloning, sequence analysis
RT and expression.";
RL Biochem. J. 305:767-775(1995).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Tail muscle.
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; Z29534; CAA82650.1; -; mRNA.
DR PIR; S41391; S41391.
DR PIR; S53373; S53373.
DR AlphaFoldDB; Q27319; -.
DR SMR; Q27319; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR Gene3D; 3.40.20.10; -; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
PE 1: Evidence at protein level;
KW Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Metal-binding; Repeat.
FT CHAIN 1..754
FT /note="Gelsolin, cytoplasmic"
FT /id="PRO_0000218726"
FT REPEAT 22..71
FT /note="Gelsolin-like 1"
FT REPEAT 143..183
FT /note="Gelsolin-like 2"
FT REPEAT 266..306
FT /note="Gelsolin-like 3"
FT REPEAT 414..463
FT /note="Gelsolin-like 4"
FT REPEAT 538..580
FT /note="Gelsolin-like 5"
FT REPEAT 643..684
FT /note="Gelsolin-like 6"
FT REGION 1..120
FT /note="Actin-severing"
FT /evidence="ECO:0000255"
FT REGION 68..71
FT /note="Actin-actin interfilament contact point"
FT REGION 209..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..751
FT /note="Actin-binding, Ca-sensitive"
FT /evidence="ECO:0000255"
FT BINDING 101..108
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000255"
FT BINDING 133..141
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000255"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 556
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 578
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 659
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 660
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 682
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 754 AA; 83522 MW; CBD2D158CCB980E8 CRC64;
MVPAFEGAGA VEGLTIWRIE NFEVVPYPKE KYGQFYQGDS YIVLYTRDVN GNLSWDLHFW
LGSETSQDEA GTAAIKTVEL DDQLGGVPVQ HREVEGHETS LFLSRFKKGV RYLKGGVASG
FHHVDPDAPY PARLFHVKGR RNIRIRQVEV GVGSMNKGDC FILDCGSQVY AYMGPSSRKM
DRLKAIQAAN PVRADDHAGK AKVIVIDETA SGSEAGESSP GLGGGSPDDV ADEDTGVDDS
AFERSEVNVV TLHHIFEDGD GVIQTNMIGE KPLLQSMLDS GDCFLLDTGV GVYVWIGSGS
SKKEKVKSME LAAGYMEKKG YPTYTNVQRV VEKAEPAVFK AYFKTWREPQ EQIGLGRVFT
QRQMSAVSAT ETDFDVSSLH AEKRRLLQKN AGPAFALCPI MVLARRNLGP LRTLKLEPVD
ESTHGFFFGG DSYVLKYIYE VNGNERYILY FWQGCASSQD EKASSAIHTV RLDNELCGKA
VQVRVVQGYE PAHFLRIFKG RMVIFLGGKA SGFKNVHDHD TYDVDGTRLF RVRGTCDFDT
RAIQQTEVAG SLNSDDVFVL ETPGKTYLWI GKGASEEEKA MGEKVVELVS PGRDMVTVAE
GEEDDDFWGG LGGKGDYQTA RDLDRPLLYP RLFHCTISPA GCLRVNEMSD FAQEDLNEDD
VMVLDSGDEV YVWVGQGSDD QEKEKAFTMA ENYIKTDPTE RTLDATVILR INQGEEPAAF
TSIFPAWNPD MWQKGLVSYD DMKAQVPETN AAVE
