GELS_HORSE
ID GELS_HORSE Reviewed; 731 AA.
AC Q28372; Q95180;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Gelsolin;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
DE AltName: Full=Brevin;
GN Name=GSN;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Smooth muscle;
RX PubMed=9490033; DOI=10.1046/j.1432-1327.1998.2510613.x;
RA Koepf E.K., Hewitt J., Vo H., Macgillivray R.T.A., Burtnick L.D.;
RT "Equus caballus gelsolin -- cDNA sequence and protein structural
RT implications.";
RL Eur. J. Biochem. 251:613-621(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9288746; DOI=10.1016/s0092-8674(00)80527-9;
RA Burtnick L.D., Koepf E.K., Grimes J., Jones E.Y., Stuart D.I.,
RA McLaughlin P.J., Robinson R.C.;
RT "The crystal structure of plasma gelsolin: implications for actin severing,
RT capping, and nucleation.";
RL Cell 90:661-670(1997).
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. Plays a role in ciliogenesis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds to actin and to fibronectin. Identified in a complex
CC composed of ACTA1, COBL, GSN AND TMSB4X (By similarity). Interacts with
CC the inactive form of EIF2AK2/PKR (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; U31699; AAC13353.1; -; mRNA.
DR RefSeq; NP_001075422.1; NM_001081953.1.
DR PDB; 1D0N; X-ray; 2.50 A; A/B=3-731.
DR PDB; 1RGI; X-ray; 3.00 A; G=2-347.
DR PDB; 2FGH; X-ray; 2.80 A; A/B=2-731.
DR PDBsum; 1D0N; -.
DR PDBsum; 1RGI; -.
DR PDBsum; 2FGH; -.
DR AlphaFoldDB; Q28372; -.
DR SMR; Q28372; -.
DR STRING; 9796.ENSECAP00000026815; -.
DR PeptideAtlas; Q28372; -.
DR PRIDE; Q28372; -.
DR GeneID; 100034186; -.
DR KEGG; ecb:100034186; -.
DR CTD; 2934; -.
DR InParanoid; Q28372; -.
DR OrthoDB; 1376537at2759; -.
DR EvolutionaryTrace; Q28372; -.
DR PRO; PR:Q28372; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin capping; Actin-binding; Calcium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Disulfide bond;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..731
FT /note="Gelsolin"
FT /id="PRO_0000367500"
FT REPEAT 25..75
FT /note="Gelsolin-like 1"
FT REPEAT 147..187
FT /note="Gelsolin-like 2"
FT REPEAT 263..305
FT /note="Gelsolin-like 3"
FT REPEAT 402..453
FT /note="Gelsolin-like 4"
FT REPEAT 525..565
FT /note="Gelsolin-like 5"
FT REPEAT 628..670
FT /note="Gelsolin-like 6"
FT REGION 2..125
FT /note="Actin-severing"
FT /evidence="ECO:0000255"
FT REGION 72..75
FT /note="Actin-actin interfilament contact point"
FT REGION 383..731
FT /note="Actin-binding, Ca-sensitive"
FT /evidence="ECO:0000255"
FT BINDING 111..118
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:0000250"
FT BINDING 137..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 /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 541
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 563
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 358
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 414
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 533
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13020"
FT MOD_RES 552
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 600
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT MOD_RES 691
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06396"
FT DISULFID 164..177
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:1D0N"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2FGH"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:1D0N"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 217..223
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:1RGI"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 260..270
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:2FGH"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2FGH"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:1D0N"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 380..386
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 421..431
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 434..443
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 449..464
FT /evidence="ECO:0007829|PDB:1D0N"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:1D0N"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:2FGH"
FT STRAND 511..519
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 539..546
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 551..555
FT /evidence="ECO:0007829|PDB:2FGH"
FT HELIX 561..574
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:2FGH"
FT HELIX 588..592
FT /evidence="ECO:0007829|PDB:1D0N"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 610..613
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 617..622
FT /evidence="ECO:0007829|PDB:1D0N"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 646..651
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 666..669
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 672..682
FT /evidence="ECO:0007829|PDB:1D0N"
FT STRAND 693..697
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 703..706
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 714..717
FT /evidence="ECO:0007829|PDB:1D0N"
FT HELIX 721..729
FT /evidence="ECO:0007829|PDB:1D0N"
SQ SEQUENCE 731 AA; 80827 MW; A72ABEC8015145A5 CRC64;
MVVEHPEFLK AGKEPGLQIW RVEKFDLVPV PPNLYGDFFT GDAYVILKTV QLRNGILQYD
LHYWLGNECS QDESGAAAIF TVQLDDYLNG RAVQHREVQG FESATFLGYF KSGLKYKKGG
VASGFKHVVP NEVVVQRLLQ VKGRRVVRAT EVPVSWESFN NGDCFILDLG NNIYQWCGSK
SNRFERLKAT QVSKGIRDNE RSGRAQVSVF EEGAEPEAML QVLGPKPTLP EATEDTVKED
AANRKLAKLY KVSNGAGPMV VSLVADENPF AQGALRSEDC FILDHGKDGK IFVWKGKQAN
MEERKAALKT ASDFISKMDY PKQTQVSVLP EGGETPLFRQ FFKNWRDPDQ TEGLGLAYLS
SHIAHVERVP FDAATLHTST AMAAQHGMDD DGTGQKQIWR VEGSNKVPVD PATYGQFYGG
DSYIILYNYR HGSRQGQIIY NWQGAQSTQD EVAASAILTA QLDEELGGTP VQSRVVQGKE
PAHLMSLFGG KPMIVYKGGT SREGGQTAPA STRLFQVRAS SSGATRAVEI IPKAGALNSN
DAFVLKTPSA AYLWVGAGAS EAEKTGAQEL LRVLRAQPVQ VAEGSEPDSF WEALGGKATY
RTSPRLKDKK MDAHPPRLFA CSNKIGRFVI EEVPGEFMQE DLATDDVMLL DTWDQVFVWV
GKDSQDEEKT EALTSAKRYI DTDPAHRDRR TPITVVKQGF EPPSFVGWFL GWDDSYWSVD
PLDRALAELA A
