ID G1NSG7_MYOLU Unreviewed; 782 AA.
AC G1NSG7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Gelsolin {ECO:0000256|ARBA:ARBA00018797, ECO:0000256|RuleBase:RU367130};
DE Short=ADF {ECO:0000256|RuleBase:RU367130};
DE AltName: Full=Actin-depolymerizing factor {ECO:0000256|RuleBase:RU367130};
GN Name=GSN {ECO:0000313|Ensembl:ENSMLUP00000000071.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000000071.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000000071.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000000071.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|RuleBase:RU367130}.
CC -!- SUBUNIT: Binds to actin and to fibronectin. Identified in a complex
CC composed of ACTA1, COBL, GSN and TMSB4X. Interacts with the inactive
CC form of EIF2AK2/PKR. {ECO:0000256|RuleBase:RU367130}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|RuleBase:RU367130}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family.
CC {ECO:0000256|RuleBase:RU367130}.
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DR EMBL; AAPE02022954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1NSG7; -.
DR STRING; 59463.ENSMLUP00000000071; -.
DR Ensembl; ENSMLUT00000000076.2; ENSMLUP00000000071.2; ENSMLUG00000000076.2.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000155591; -.
DR HOGENOM; CLU_002568_3_2_1; -.
DR InParanoid; G1NSG7; -.
DR OMA; NRVVHVK; -.
DR TreeFam; TF313468; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0030478; C:actin cap; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0002102; C:podosome; IEA:Ensembl.
DR GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0045159; F:myosin II binding; IEA:Ensembl.
DR GO; GO:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; IEA:Ensembl.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:Ensembl.
DR GO; GO:0030041; P:actin filament polymerization; IEA:Ensembl.
DR GO; GO:0051014; P:actin filament severing; IEA:UniProtKB-UniRule.
DR GO; GO:1990000; P:amyloid fibril formation; IEA:Ensembl.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:UniProtKB-UniRule.
DR GO; GO:0086003; P:cardiac muscle cell contraction; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0006911; P:phagocytosis, engulfment; IEA:Ensembl.
DR GO; GO:0051127; P:positive regulation of actin nucleation; IEA:Ensembl.
DR GO; GO:1902174; P:positive regulation of keratinocyte apoptotic process; IEA:Ensembl.
DR GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:1903903; P:regulation of establishment of T cell polarity; IEA:Ensembl.
DR GO; GO:1903906; P:regulation of plasma membrane raft polarization; IEA:Ensembl.
DR GO; GO:0071801; P:regulation of podosome assembly; IEA:Ensembl.
DR GO; GO:1903909; P:regulation of receptor clustering; IEA:Ensembl.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
DR GO; GO:0097017; P:renal protein absorption; IEA:Ensembl.
DR GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
DR GO; GO:0042989; P:sequestering of actin monomers; IEA:Ensembl.
DR GO; GO:0014891; P:striated muscle atrophy; IEA:Ensembl.
DR CDD; cd11290; gelsolin_S1_like; 1.
DR CDD; cd11289; gelsolin_S2_like; 1.
DR CDD; cd11292; gelsolin_S3_like; 1.
DR CDD; cd11293; gelsolin_S4_like; 1.
DR CDD; cd11288; gelsolin_S5_like; 1.
DR CDD; cd11291; gelsolin_S6_like; 1.
DR Gene3D; 3.40.20.10; Severin; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977:SF29; GELSOLIN; 1.
DR PANTHER; PTHR11977; VILLIN; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SUPFAM; SSF55753; Actin depolymerizing proteins; 6.
PE 3: Inferred from homology;
KW Actin capping {ECO:0000256|RuleBase:RU367130};
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW ECO:0000256|RuleBase:RU367130};
KW Cilium biogenesis/degradation {ECO:0000256|ARBA:ARBA00022794};
KW Cytoplasm {ECO:0000256|RuleBase:RU367130};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..782
FT /note="Gelsolin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003417502"
FT DOMAIN 75..158
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 197..270
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 317..389
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 455..536
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 584..642
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 681..757
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 246..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 85702 MW; 9ED5DC9B32A28064 CRC64;
MAPQSSVPAM LAALVLALCA LSSPAGAATA SRRATQAPAT QGRVSLTSPI SMAAEHPEFL
KAGKEPGLQI WRVEKFDLVP VPPNLYGDFF TGDAYVILKT VQLRNGNLQY DLHYWLGNEC
SQDESGAAAI FTVQLDDYLN GRAVQHREVQ GFESATFLSY FKSGLKYKKG GVASGFKHVV
PNEVVVQRLF QVKGRRTVRA TEVPVSWESF NNGDCFILDL GNDIYQWCGS NSNRFERLKA
TQVSKGIRDN ERHGRARVHV SEEGAEPEAM LQVLGSKPTL PEGTEDTAKE DAANRKLAKL
YKVSNGAGTM SVLLVADENP FAQGALKSED CFILDHGKNG KIFVWKGRGA NTEERKAALK
TATDFISKMD YPRQTQVAVL PEGGETPLFK QFFKNWRDPD QTDGLGLTYL SSHIANVERV
PFDAATLHTS TAMAAQHGMD DDGTGQKQIW RIEGSNKVPV DPASYGQFYG GDSYIILYNY
RHGGRQGQII YNWQGAQSTQ DEVAASAILT AQLDEELGGT PVQSRVVQGK EPAHLMSLFG
GKPMIIYKGG TSREGGQTAP ASTRLFQVRA SSSGATRAVE IMPKAGALNS NDAFVLKTPS
AAYLWVGTGA SDAEKTGAQE LLRVLQAQPV QVAEGSEPDS FWEALGGKAA YRTSPRLKDK
KMDAHPPRLF ACSNKIGRFV IEEVPGELMQ EDLATDDVML LDTWDQVFVW VGKDSQEEEK
TEALNSAKRY IETDPANRDR RTPITMVKQG FEPPSFVGWF LGWDDDYWSM DPLDRALADL
AA
//
