GELS1_LUMTE
ID GELS1_LUMTE Reviewed; 367 AA.
AC Q7JQD3; A8I4V6; Q25418; Q27410;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Gelsolin-like protein 1;
DE AltName: Full=Actin-modulator {ECO:0000303|PubMed:7957213, ECO:0000312|EMBL:BAA06219.2};
DE Short=EWAM {ECO:0000303|PubMed:7957213};
DE Short=EWAM-P1 {ECO:0000303|PubMed:18197420};
GN Name=AM {ECO:0000303|PubMed:7957213};
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:BAA06219.2}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle {ECO:0000312|EMBL:CAA83537.1};
RX PubMed=7957213; DOI=10.1111/j.1432-1033.1994.0773b.x;
RA Giebing T., D'Haese J., Hinssen H.;
RT "The complete sequence of a 40-kDa actin-modulating protein from the
RT earthworm Lumbricus terrestris.";
RL Eur. J. Biochem. 225:773-779(1994).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABV82435.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-168, FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Seminal vesicle {ECO:0000312|EMBL:ABV82435.1};
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 [3] {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 [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH ACTIN.
RX PubMed=9395293; DOI=10.1016/s0014-5793(97)01230-1;
RA Giebing T., Obermann W.M., Furst D., D'Haese J.;
RT "C-terminally deleted fragments of 40-kDa earthworm actin modulator still
RT show gelsolin activities.";
RL FEBS Lett. 417:191-195(1997).
RN [5] {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|PubMed:18197420, ECO:0000269|PubMed:9395293,
CC ECO:0000269|Ref.3}.
CC -!- SUBUNIT: Interacts with actin monomers and filaments.
CC {ECO:0000269|PubMed:9395293, ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P06396}.
CC -!- TISSUE SPECIFICITY: Expressed in circular and longitudinal muscle,
CC pseudohearts, pharynx and gizzard. Also expressed in male germ cells at
CC the proximal pole of primary spermatocytes in 16 cell-stage morulae,
CC and in the distal parts of the spermatocytes in 32 and 64 cell-stage
CC morulae. In the spermatids of the 128 cell-stage morulae it is
CC expressed at the proximal pole of the elongated nucleus and the distal
CC pole near the base of the flagellae. {ECO:0000269|PubMed:18197420,
CC ECO:0000269|Ref.5}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the cytophore, spermatocytes and
CC young spermatids during spermatogenesis. Not expressed in mature sperm.
CC {ECO:0000269|PubMed:18197420}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000255}.
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DR EMBL; D29920; BAA06219.2; -; mRNA.
DR EMBL; Z32528; CAA83537.1; -; mRNA.
DR EMBL; EU155485; ABV82435.1; -; mRNA.
DR PIR; S51363; S51363.
DR AlphaFoldDB; Q7JQD3; -.
DR SMR; Q7JQD3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0051693; P:actin filament capping; IDA:UniProtKB.
DR GO; GO:0030043; P:actin filament fragmentation; IDA:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; IDA:UniProtKB.
DR GO; GO:0045010; P:actin nucleation; IDA:UniProtKB.
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;
KW Developmental protein; Repeat.
FT CHAIN 1..367
FT /note="Gelsolin-like protein 1"
FT /id="PRO_0000390385"
FT REPEAT 56..141
FT /note="Gelsolin-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 179..225
FT /note="Gelsolin-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 287..322
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REGION 1..185
FT /note="Actin binding"
FT /evidence="ECO:0000269|PubMed:7957213,
FT ECO:0000269|PubMed:9395293"
FT REGION 106..109
FT /note="Actin-actin interfilament contact point"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT REGION 186..295
FT /note="Actin binding, Actin-severing"
FT /evidence="ECO:0000269|PubMed:9395293"
FT REGION 235..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..366
FT /note="Actin-severing, Ca-sensitive"
FT /evidence="ECO:0000269|PubMed:9395293"
FT COMPBIAS 235..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 69..73
FT /note="KFYNG -> SSTR (in Ref. 1; CAA83537)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 41636 MW; 7A18DED824553ADE CRC64;
MATGLIKAKE YDWKDSNLAL FGSDTEKQVK KDSAATEPAW KGAGQKEGLK IWRIVNFKVT
EWPQNQHGKF YNGDSYIILN TYKPDPKSNE LAYDVHFWIG SQSSQDEYGT AAYKTVELDT
FLDDKPVQHR EVQGYESELF RNYFKQGLTI LEGGAETGFH HVKPTEYKPR LLHFSGQKQQ
IYVHEVPLVK ERLDHKDVFI LDLGLTLYQW NGKESSKEEG FKAMQYLGLM RSERPKAEAE
TLEDESTPES HKFYTSLTGT DEPNLVKPLV KEENQLLKVS DAGGHLKTTE VKRGAVNSKD
FSSNDVFILD TGDQCFVWVG KGRFAVGEAE WTRISHAHLM KTCHPLAPIH VIKEGQLCKA
FNVAIAA
