ID F6UAI3_MONDO Unreviewed; 776 AA.
AC F6UAI3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 74.
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:ENSMODP00000024516.3};
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000024516.3, ECO:0000313|Proteomes:UP000002280};
RN [1] {ECO:0000313|Ensembl:ENSMODP00000024516.3, ECO:0000313|Proteomes:UP000002280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17495919; DOI=10.1038/nature05805;
RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT coding sequences.";
RL Nature 447:167-177(2007).
RN [2] {ECO:0000313|Ensembl:ENSMODP00000024516.3}
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 RefSeq; XP_001369795.1; XM_001369758.4.
DR AlphaFoldDB; F6UAI3; -.
DR STRING; 13616.ENSMODP00000024516; -.
DR Ensembl; ENSMODT00000024952.4; ENSMODP00000024516.3; ENSMODG00000019652.4.
DR GeneID; 100015804; -.
DR KEGG; mdo:100015804; -.
DR CTD; 2934; -.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000155591; -.
DR HOGENOM; CLU_002568_3_2_1; -.
DR InParanoid; F6UAI3; -.
DR OMA; NRVVHVK; -.
DR OrthoDB; 25995at2759; -.
DR TreeFam; TF313468; -.
DR Proteomes; UP000002280; Chromosome 1.
DR Bgee; ENSMODG00000019652; Expressed in liver and 18 other cell types or tissues.
DR GO; GO:0030478; C:actin cap; IEA:Ensembl.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IBA:GO_Central.
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:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:1990000; P:amyloid fibril formation; IEA:Ensembl.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0086003; P:cardiac muscle cell contraction; IEA:Ensembl.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
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:UP000002280};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..776
FT /note="Gelsolin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003343871"
FT DOMAIN 71..153
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 192..265
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 311..384
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 451..531
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 571..637
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 676..751
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
SQ SEQUENCE 776 AA; 85765 MW; A49284A6A066C839 CRC64;
MARGSLVLAA LGCLLLRAGC GHAAVTPGSL VSLLTATVAL SAGPVSMVVE HAEFLKAGKE
PGLQIWRVEQ FDLVPVPKNL YGDFFSGDAY LILNTIKRRD GSLQYDLHFW LGNECTQDES
GAAAIFTVQM DDYLHGKAVQ HREVQGFESP TFLGYFRSGI KYKKGGVASG FKHVVPNEVS
VQRLFKVKGR RTTRATEVPV TWDSFNNGDC FILDLGNDIY QWCGSKSNRF ERLRATQVSK
GIRDNERSGR AKVHVSEEGA EPEKMLQVLG PKPTLPDSPD DTIVEDTVNR RLAKLYKVSN
GAGTMTVSLV ADENPFSQAA LSSDDCFILD HGTNGKIYVW KGKQANMEER KAALKSASDF
ISKMNYRRET QIEVLPEEGE TPLFKQFFKN WRERDQTQGL GVAYISSHIA NVERVPFDAA
TLHNSTAMAA QHGMEDDGTG QKQIWRIEGA DKVPVNPSTY GQFYGGDCYI ILYNYQHAGR
QGQIIYYWQG ADSSQEERAT AAILTIQLDE ELGGTPVQSR VVQGKEPAHL MSLFGGKPMI
IYKGGTSREG GQTAPASTRL FQVRSSSAGA TRAVEVNPTA GELNSNDAFV LKTPTSTYLW
VGEGASDSEK SGAQELLKVL GARPVQVAEG KEPDSFWEVL GGKTTYRTSP RLKDKKMDAH
PPRLFACSNK IGRFVIEEVP GEFMQEDLAT DDVMLLDTWD QVYVWVGKDS QEEEKTEALT
SAKRYIDTDP ANRRGTPITM VKQGSEPPSF MGWFLGWDNS YWDVDPLDRA MAELDV
//
