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Gelsolin

 GELS_DROME              Reviewed;         798 AA.
Q07171; A4V2C8; A9UNC4; Q0KIE3; Q0KIE4; Q8MRF9; Q9VMZ1; Q9VMZ2;
28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2000, sequence version 2.
22-NOV-2017, entry version 147.
RecName: Full=Gelsolin;
Flags: Precursor;
Name=Gel; ORFNames=CG1106;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|EMBL:AAF52163.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8386771; DOI=10.1006/jmbi.1993.1191;
Heintzelman M.B., Frankel S.A., Artavanis-Tsakonas S., Mooseker M.S.;
"Cloning of a secretory gelsolin from Drosophila melanogaster.";
J. Mol. Biol. 230:709-716(1993).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8175883; DOI=10.1083/jcb.125.3.607;
Stella M.C., Schauerte H., Straub K.L., Leptin M.;
"Identification of secreted and cytosolic gelsolin in Drosophila.";
J. Cell Biol. 125:607-616(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H.,
Yu C., Celniker S.E.;
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Calcium-regulated, actin-modulating protein that binds
to the plus (or barbed) ends of actin monomers or filaments,
preventing monomer exchange (end-blocking or capping). It can
promote the assembly of monomers into filaments (nucleation) as
well as sever filaments already formed.
{ECO:0000269|PubMed:8175883}.
-!- SUBUNIT: Binds to actin and to fibronectin.
{ECO:0000269|PubMed:8175883}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton.
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1 {ECO:0000269|PubMed:8175883, ECO:0000305}; Synonyms=B
{ECO:0000269|PubMed:8175883, ECO:0000305}, D
{ECO:0000312|FlyBase:FBgn0010225}, F
{ECO:0000312|FlyBase:FBgn0010225}, Secreted
{ECO:0000269|PubMed:8175883, ECO:0000305};
IsoId=Q07171-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:8175883, ECO:0000305}; Synonyms=A
{ECO:0000269|PubMed:8175883, ECO:0000305}, Cytoplasmic
{ECO:0000269|PubMed:8175883, ECO:0000305};
IsoId=Q07171-2; Sequence=VSP_007010;
Name=K {ECO:0000312|FlyBase:FBgn0010225};
IsoId=Q07171-6; Sequence=VSP_058364;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are ubiquitously
expressed in early embryo. Isoform 1 is expressed in the fat body,
and is abundant in hemolymph. Isoform 2 is expressed in parts of
the gut. {ECO:0000269|PubMed:8175883}.
-!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
-!- CAUTION: Lacks one of the cysteines to make the disulfide bridge
in isoform 1. It is replaced by Val-233. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA28568.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAM50316.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAM50316.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAM50316.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=ABY20529.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA53295.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; L08794; AAA28568.1; ALT_INIT; mRNA.
EMBL; X75629; CAA53294.1; -; mRNA.
EMBL; X75630; CAA53295.1; ALT_INIT; mRNA.
EMBL; AE014297; AAF52162.2; -; Genomic_DNA.
EMBL; AE014297; AAF52163.1; -; Genomic_DNA.
EMBL; AE014297; AAF52164.3; -; Genomic_DNA.
EMBL; AE014297; AAN13333.3; -; Genomic_DNA.
EMBL; AE014297; AAO41510.1; -; Genomic_DNA.
EMBL; AY119662; AAM50316.1; ALT_SEQ; mRNA.
EMBL; BT031288; ABY20529.1; ALT_INIT; mRNA.
PIR; A53909; A53909.
RefSeq; NP_001036657.2; NM_001043192.3. [Q07171-2]
RefSeq; NP_524865.2; NM_080126.4. [Q07171-1]
RefSeq; NP_730788.1; NM_164319.4. [Q07171-2]
RefSeq; NP_730790.2; NM_164321.5. [Q07171-1]
RefSeq; NP_788571.1; NM_176394.3. [Q07171-1]
RefSeq; NP_996148.2; NM_206426.4. [Q07171-6]
RefSeq; NP_996149.3; NM_206427.4.
ProteinModelPortal; Q07171; -.
SMR; Q07171; -.
BioGrid; 70060; 5.
IntAct; Q07171; 4.
MINT; MINT-4080740; -.
STRING; 7227.FBpp0078607; -.
PaxDb; Q07171; -.
PRIDE; Q07171; -.
EnsemblMetazoa; FBtr0078968; FBpp0078607; FBgn0010225. [Q07171-1]
EnsemblMetazoa; FBtr0078969; FBpp0078608; FBgn0010225. [Q07171-1]
EnsemblMetazoa; FBtr0078971; FBpp0078610; FBgn0010225. [Q07171-2]
EnsemblMetazoa; FBtr0078973; FBpp0078612; FBgn0010225. [Q07171-1]
EnsemblMetazoa; FBtr0309256; FBpp0301195; FBgn0010225. [Q07171-1]
EnsemblMetazoa; FBtr0309257; FBpp0301196; FBgn0010225. [Q07171-6]
EnsemblMetazoa; FBtr0336707; FBpp0307688; FBgn0010225. [Q07171-2]
GeneID; 46008; -.
KEGG; dme:Dmel_CG1106; -.
CTD; 46008; -.
FlyBase; FBgn0010225; Gel.
eggNOG; KOG0443; Eukaryota.
eggNOG; ENOG410XR0A; LUCA.
GeneTree; ENSGT00760000119111; -.
InParanoid; Q07171; -.
KO; K05768; -.
OMA; GTGFKHV; -.
OrthoDB; EOG091G05SC; -.
PhylomeDB; Q07171; -.
ChiTaRS; Bsg; fly.
GenomeRNAi; 46008; -.
PRO; PR:Q07171; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0010225; -.
ExpressionAtlas; Q07171; differential.
Genevisible; Q07171; DM.
GO; GO:0005884; C:actin filament; IDA:FlyBase.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; ISS:FlyBase.
GO; GO:0051015; F:actin filament binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
GO; GO:0006909; P:phagocytosis; IMP:FlyBase.
Gene3D; 3.40.20.10; -; 6.
InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
InterPro; IPR007123; Gelsolin-like_dom.
InterPro; IPR007122; Villin/Gelsolin.
PANTHER; PTHR11977; PTHR11977; 1.
Pfam; PF00626; Gelsolin; 5.
PRINTS; PR00597; GELSOLIN.
SMART; SM00262; GEL; 6.
1: Evidence at protein level;
Actin-binding; Alternative splicing; Calcium; Complete proteome;
Cytoplasm; Cytoskeleton; Metal-binding; Phosphoprotein;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 798 Gelsolin.
/FTId=PRO_0000036393.
REPEAT 78 131 Gelsolin-like 1.
REPEAT 203 243 Gelsolin-like 2.
REPEAT 322 365 Gelsolin-like 3.
REPEAT 474 524 Gelsolin-like 4.
REPEAT 583 625 Gelsolin-like 5.
REPEAT 689 730 Gelsolin-like 6.
REGION 57 181 Actin-severing. {ECO:0000255}.
REGION 128 131 Actin-actin interfilament contact point.
{ECO:0000250}.
REGION 167 174 Polyphosphoinositide binding.
{ECO:0000250}.
REGION 193 201 Polyphosphoinositide binding.
{ECO:0000250}.
REGION 451 792 Actin-binding, Ca-sensitive.
{ECO:0000255}.
METAL 599 599 Calcium 1. {ECO:0000250}.
METAL 623 623 Calcium 1. {ECO:0000250}.
METAL 705 705 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 706 706 Calcium 2. {ECO:0000250}.
METAL 728 728 Calcium 2. {ECO:0000250}.
MOD_RES 90 90 Phosphotyrosine; by SRC. {ECO:0000305}.
MOD_RES 612 612 Phosphotyrosine; by SRC. {ECO:0000305}.
MOD_RES 662 662 Phosphotyrosine; by SRC. {ECO:0000305}.
VAR_SEQ 1 58 Missing (in isoform 2).
{ECO:0000303|PubMed:8175883}.
/FTId=VSP_007010.
VAR_SEQ 1 14 MDASGAATMAVLSS -> MF (in isoform K).
/FTId=VSP_058364.
CONFLICT 498 498 N -> S (in Ref. 2; CAA53294/CAA53295).
{ECO:0000305}.
CONFLICT 646 646 G -> S (in Ref. 2; CAA53294/CAA53295).
{ECO:0000305}.
SEQUENCE 798 AA; 88375 MW; 79828666DC0965CC CRC64;
MDASGAATMA VLSSLLVFLA LSSSLCSAGT LNARPAFPVQ SGEIQPSGQN SKQAARRVMH
PSFANAGRTP GLEIWRIENF EPVIYPKTNY GKFYTGDSFI VLNTIENKKD KKLSWDVHFW
LGLETSTDEA GAAAILTVQL DDLLNGGPVQ HREVQDHESQ LFLSYFKNGI RYEQGGVGTG
FKHVETNAQG ETRLFQVKGK RNVRVRQVNL SVSSMNTGDC FILDAGSDIY VYVGSQAKRV
EKLKAISAAN QIRDQDHNGR ARVQIVDDFS TDADKQHFFD VLGSGSADQV PDESTADEDS
AFERTDAAAV SLYKVSDASG KLKVDIIGQK PLTQAMLDTR ECFILDTGSG IFVWVGKGAT
QKEKTDAMAK AQEFLRTKKY PAWTQIHRIV EGSESAPFKQ YFDTWRDAGM SHSRLIRSAL
GIGSDELLND DEIDSVVTQL KKSGGRAFGF MPDHGQNVIE TITQYVAKPG SDEIVVSTVP
FDEKLPLLGF ASYVLTYNYE ANNGDTGSLT YVWHGVKASA AARKRAFEEG LVGSKDGLLV
QTNQGHEPRH FYKIFKGKLL TSFTALPVTA QLFRIRGTVE SDVHASEVAA DSSSLASSDA
FVLHSGKSHK IYIWNGLGAS AFEKQAAVDR FSDYWDDVEL EQVEEGAEPD EFWEELNGEG
QYDRSLGDDG APLLESRLFH CHLSSGGFLK VEEVAQYEQE DLDSDDIMLL DAGDEIYLWV
GYGVSEEENG KLLDTAKLYF NLEPTARSFD TVSIIRVPQG KEPRVFKRMF PNWDDNYWQN
QPSYEDMKQL VIDANNEV


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