ID   GELS2_LUMTE             Reviewed;         366 AA.
AC   Q8MPM1;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Gelsolin-like protein 2;
DE   AltName: Full=Actin-modulator {ECO:0000303|PubMed:18197420, ECO:0000303|Ref.2};
DE            Short=EWAM-P2 {ECO:0000303|PubMed:18197420, ECO:0000303|Ref.2};
GN   Name=gelsolin {ECO:0000312|EMBL:CAD43405.1};
OS   Lumbricus terrestris (Common earthworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Oligochaeta; Crassiclitellata; Lumbricina; Lumbricidae; Lumbricinae;
OC   Lumbricus.
OX   NCBI_TaxID=6398;
RN   [1] {ECO:0000312|EMBL:CAD43405.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle {ECO:0000312|EMBL:CAD43405.1};
RA   Krueger E.M.I.;
RT   "Isoforms of the gelsolin-related protein of the earthworm Lumbricus
RT   terrestris.";
RL   Thesis (2001), Heinrich-Heine Universitaet Duesseldorf, Germany.
RN   [2] {ECO:0000305}
RP   FUNCTION, AND INTERACTION WITH ACTIN.
RX   DOI=10.1007/BF00700982;
RA   D'Haese J., Hinssen H.;
RT   "Isolation and characterization of a Ca(2+)-activated actin-modulating
RT   protein from obliquely striated muscle.";
RL   J. Comp. Physiol. B 157:615-623(1987).
RN   [3] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=18197420; DOI=10.1007/s00441-007-0561-9;
RA   Kruger E., Hinssen H., D'Haese J.;
RT   "Involvement of a gelsolin-related protein in spermatogenesis of the
RT   earthworm Lumbricus terrestris.";
RL   Cell Tissue Res. 332:141-150(2008).
RN   [4] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   DOI=10.1023/A:1017120917085;
RA   Kruger E., Giebing T., Hinssen H., Fey M., D'Haese J.;
RT   "Two distinct isoforms of the gelsolin-related protein of the annelid
RT   Lumbricus terrestris: characterization by sequence analysis and
RT   localization in various muscle tissues.";
RL   (In) Abstracts of the XXVI European Muscle Conference,
RL   J. Muscle Res. Cell Motil., pp.522-522, Berlin (2001).
CC   -!- FUNCTION: Calcium-regulated protein that binds to the plus (or barbed)
CC       ends of actin monomers or filaments, preventing monomer exchange (end-
CC       blocking or capping). Can promote the assembly of monomers into
CC       filaments (nucleation) as well as sever existing filaments.
CC       {ECO:0000269|Ref.2}.
CC   -!- SUBUNIT: Interacts with actin monomers and filaments.
CC       {ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P06396}.
CC   -!- TISSUE SPECIFICITY: Expressed in circular and longitudinal muscle,
CC       pseudohearts, pharynx and gizzard. Not expressed in seminal vesicles.
CC       {ECO:0000269|PubMed:18197420, ECO:0000269|Ref.4}.
CC   -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000255}.
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DR   EMBL; AJ504727; CAD43405.1; -; mRNA.
DR   AlphaFoldDB; Q8MPM1; -.
DR   SMR; Q8MPM1; -.
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:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.20.10; -; 3.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR036180; Gelsolin-like_dom_sf.
DR   InterPro; IPR007122; Villin/Gelsolin.
DR   PANTHER; PTHR11977; PTHR11977; 1.
DR   Pfam; PF00626; Gelsolin; 3.
DR   PRINTS; PR00597; GELSOLIN.
DR   SMART; SM00262; GEL; 3.
DR   SUPFAM; SSF82754; SSF82754; 1.
PE   1: Evidence at protein level;
KW   Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton; Repeat.
FT   CHAIN           1..366
FT                   /note="Gelsolin-like protein 2"
FT                   /id="PRO_0000390386"
FT   REPEAT          55..139
FT                   /note="Gelsolin-like 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          177..252
FT                   /note="Gelsolin-like 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          286..327
FT                   /note="Gelsolin-like 3"
FT                   /evidence="ECO:0000255"
FT   REGION          100..116
FT                   /note="Actin binding"
FT                   /evidence="ECO:0000250|UniProtKB:P06396"
FT   REGION          104..107
FT                   /note="Actin-actin interfilament contact point"
FT                   /evidence="ECO:0000250|UniProtKB:P06396"
SQ   SEQUENCE   366 AA;  40968 MW;  14A8E80533B540BD CRC64;
     MSGLVKAKRY DWKDSNLAMF GSALDKSVKK ESALKEAAWK GVGEKVGLKI WRIVNFKVTE
     WPEKDYGSFF SGDSYIILNT YKLKGREELA YDVHFWIGSK STQDEYCVAA YKTVELDAYL
     DDAAIQHRDA EGNESDLFLS YFENGLTIME GGAEMGFNNV KPEEYKARLL HFSGLKKHIV
     VKEVPLCPQR LKSDDVFILD LGRTLYQWNG TGSNKDERFK AMQYLQNLKA ERGAATSKTL
     EEEHIDKSHE FYTSLTGEDE DLPEDQTDSA AVKTLLRVSD AAGHFKSTVV KTGHIAASDL
     DSKDVFILDN GSTCFVWVGN GASAQEKRNG LGYAHSHLMK TPHPLIPILR HQRGQASKCF
     NAALAA