ID GELS_HUMAN Reviewed; 782 AA. AC P06396; A2A418; A8MUD1; A8MYN7; B7Z373; B7Z5V1; F5H1A8; Q5T0I2; Q8WVV7; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 02-OCT-2024, entry version 261. DE RecName: Full=Gelsolin; DE AltName: Full=AGEL; DE AltName: Full=Actin-depolymerizing factor; DE Short=ADF; DE AltName: Full=Brevin; DE Flags: Precursor; GN Name=GSN; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE INITIATION. RX PubMed=3020431; DOI=10.1038/323455a0; RA Kwiatkowski D.J., Stossel T.P., Orkin S.H., Mole J.E., Colten H.R., RA Yin H.L.; RT "Plasma and cytoplasmic gelsolins are encoded by a single gene and contain RT a duplicated actin-binding domain."; RL Nature 323:455-458(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC TISSUE=Hippocampus, Testis, and Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, and Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 53-72 (ISOFORM 2). RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP INTERACTION WITH FIBRONECTIN. RX PubMed=6092370; DOI=10.1016/s0021-9258(18)90687-3; RA Lind S.E., Janmey P.A.; RT "Human plasma gelsolin binds to fibronectin."; RL J. Biol. Chem. 259:13262-13266(1984). RN [8] RP IDENTITY OF AMYLD4 AMYLOID PROTEIN WITH GELSOLIN. RX PubMed=2157434; DOI=10.1016/0006-291x(90)90612-q; RA Haltia M., Prelli F., Ghiso J., Kiuru S., Sommer H., Palo J., Frangione B.; RT "Amyloid protein in familial amyloidosis (Finnish type) is homologous to RT gelsolin, an actin-binding protein."; RL Biochem. Biophys. Res. Commun. 167:927-932(1990). RN [9] RP IDENTITY OF AMYLD4 AMYLOID PROTEIN WITH GELSOLIN. RX PubMed=2153578; DOI=10.1016/0014-5793(90)80072-q; RA Maury C.P.J., Alli K., Baumann M.; RT "Finnish hereditary amyloidosis. Amino acid sequence homology between the RT amyloid fibril protein and human plasma gelsoline."; RL FEBS Lett. 260:85-87(1990). RN [10] RP DISULFIDE BOND. RX PubMed=8703941; DOI=10.1021/bi960920n; RA Wen D., Corina K., Chow E.P., Miller S., Janmey P.A., Pepinsky R.B.; RT "The plasma and cytoplasmic forms of human gelsolin differ in disulfide RT structure."; RL Biochemistry 35:9700-9709(1996). RN [11] RP DISULFIDE BOND. RX PubMed=9003812; DOI=10.1016/s0014-5793(96)01439-1; RA Allen P.G.; RT "Functional consequences of disulfide bond formation in gelsolin."; RL FEBS Lett. 401:89-94(1997). RN [12] RP PHOSPHORYLATION AT TYR-86; TYR-409; TYR-465; TYR-603 AND TYR-651. RX PubMed=10210201; DOI=10.1110/ps.8.1.234; RA De Corte V., Demol H., Goethals M., Van Damme J., Gettemans J., RA Vandekerckhove J.; RT "Identification of Tyr438 as the major in vitro c-Src phosphorylation site RT in human gelsolin: a mass spectrometric approach."; RL Protein Sci. 8:234-241(1999). RN [13] RP FUNCTION. RX PubMed=20393563; DOI=10.1038/nature08895; RA Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., RA Aza-Blanc P., Gleeson J.G.; RT "Functional genomic screen for modulators of ciliogenesis and cilium RT length."; RL Nature 464:1048-1051(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-742, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] {ECO:0007744|PDB:1EQY} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-503. RX PubMed=8395021; DOI=10.1038/364685a0; RA McLaughlin P.J., Gooch J.T., Mannherz H.-G., Weeds A.G.; RT "Structure of gelsolin segment 1-actin complex and the mechanism of RT filament severing."; RL Nature 364:685-692(1993). RN [18] {ECO:0007744|PDB:1SOL} RP STRUCTURE BY NMR OF 177-196, AND DOMAIN. RX PubMed=8599675; DOI=10.1016/s0006-3495(95)80140-2; RA Xian W., Vegners R., Janmey P.A., Braunlin W.H.; RT "Spectroscopic studies of a phosphoinositide-binding peptide from gelsolin: RT behavior in solutions of mixed solvent and anionic micelles."; RL Biophys. J. 69:2695-2702(1995). RN [19] {ECO:0007744|PDB:1H1V} RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 439-769 IN COMPLEX WITH ACTIN AND RP CALCIUM, AND DOMAIN. RX PubMed=12460571; DOI=10.1016/s0022-2836(02)01131-2; RA Choe H., Burtnick L.D., Mejillano M., Yin H.L., Robinson R.C., Choe S.; RT "The calcium activation of gelsolin: insights from the 3A structure of the RT G4-G6/actin complex."; RL J. Mol. Biol. 324:691-702(2002). RN [20] {ECO:0007744|PDB:2FH1, ECO:0007744|PDB:2FH2, ECO:0007744|PDB:2FH3, ECO:0007744|PDB:2FH4} RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 439-782, AND CALCIUM-BINDING RP SITES. RX PubMed=16466744; DOI=10.1016/j.jmb.2006.01.026; RA Chumnarnsilpa S., Loonchanta A., Xue B., Choe H., Urosev D., Wang H., RA Lindberg U., Burtnick L.D., Robinson R.C.; RT "Calcium ion exchange in crystalline gelsolin."; RL J. Mol. Biol. 357:773-782(2006). RN [21] {ECO:0007744|PDB:3FFK, ECO:0007744|PDB:3FFN} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH ACTIN AND CALCIUM, RP FUNCTION, DOMAIN, DISULFIDE BOND, CHARACTERIZATION OF VARIANT AMYLD4 RP ASN-214, AND MUTAGENESIS OF GLU-236; ASP-697 AND GLU-719. RX PubMed=19666512; DOI=10.1073/pnas.0812374106; RA Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee W.L., Larsson M., Kannan B., RA Hernandez-Valladares M., Burtnick L.D., Robinson R.C.; RT "Ca2+ binding by domain 2 plays a critical role in the activation and RT stabilization of gelsolin."; RL Proc. Natl. Acad. Sci. U.S.A. 106:13713-13718(2009). RN [22] {ECO:0007744|PDB:3TU5} RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 53-174 IN COMPLEX WITH ACTA1; COBL RP AND TMSB4X, AND SUBUNIT. RX PubMed=23009842; DOI=10.1016/j.bpj.2012.07.030; RA Durer Z.A., Kudryashov D.S., Sawaya M.R., Altenbach C., Hubbell W., RA Reisler E.; RT "Structural states and dynamics of the D-loop in actin."; RL Biophys. J. 103:930-939(2012). RN [23] RP VARIANT AMYLD4 ASN-214, AND INVOLVEMENT IN AMYLD4. RX PubMed=2176481; DOI=10.1042/bj2720827; RA Ghiso J., Haltia M., Prelli F., Novello J., Frangione B.; RT "Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type."; RL Biochem. J. 272:827-830(1990). RN [24] RP VARIANTS AMYLD4 ASN-214 AND TYR-214, AND INVOLVEMENT IN AMYLD4. RX PubMed=1338910; DOI=10.1038/ng1092-157; RA de la Chapelle A., Tolvanen R., Boysen G., Santavy J., RA Bleeker-Wagemakers L., Maury C.P.J., Kere J.; RT "Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine RT substitution for aspartic acid at residue 187."; RL Nat. Genet. 2:157-160(1992). RN [25] RP VARIANTS [LARGE SCALE ANALYSIS] LEU-22; ILE-201 AND ASN-611. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). 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 (PubMed:19666512). Plays a role in ciliogenesis CC (PubMed:20393563). {ECO:0000269|PubMed:19666512, CC ECO:0000269|PubMed:20393563}. 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 (By similarity). Interacts with FLII (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P13020}. CC -!- INTERACTION: CC P06396; Q8NC06-3: ACBD4; NbExp=3; IntAct=EBI-351506, EBI-12811089; CC P06396; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-351506, EBI-10173507; CC P06396; Q8N302-2: AGGF1; NbExp=3; IntAct=EBI-351506, EBI-25838028; CC P06396; P55008: AIF1; NbExp=3; IntAct=EBI-351506, EBI-9031341; CC P06396; Q99996-3: AKAP9; NbExp=3; IntAct=EBI-351506, EBI-11022349; CC P06396; Q9NQ31: AKIP1; NbExp=3; IntAct=EBI-351506, EBI-517035; CC P06396; P10275: AR; NbExp=2; IntAct=EBI-351506, EBI-608057; CC P06396; Q9NXL2-1: ARHGEF38; NbExp=3; IntAct=EBI-351506, EBI-18172597; CC P06396; Q9Y2Y0: ARL2BP; NbExp=3; IntAct=EBI-351506, EBI-3449344; CC P06396; P49407: ARRB1; NbExp=3; IntAct=EBI-351506, EBI-743313; CC P06396; P32121: ARRB2; NbExp=3; IntAct=EBI-351506, EBI-714559; CC P06396; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-351506, EBI-9089489; CC P06396; Q9UII2: ATP5IF1; NbExp=3; IntAct=EBI-351506, EBI-718459; CC P06396; Q9ULK2-2: ATXN7L1; NbExp=3; IntAct=EBI-351506, EBI-21568482; CC P06396; Q9H7T9: AUNIP; NbExp=3; IntAct=EBI-351506, EBI-10693257; CC P06396; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-351506, EBI-742750; CC P06396; Q16520: BATF; NbExp=3; IntAct=EBI-351506, EBI-749503; CC P06396; P54687-4: BCAT1; NbExp=3; IntAct=EBI-351506, EBI-25834445; CC P06396; Q5H9J7: BEX5; NbExp=3; IntAct=EBI-351506, EBI-10243741; CC P06396; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-351506, EBI-2548012; CC P06396; Q9ULD4-2: BRPF3; NbExp=3; IntAct=EBI-351506, EBI-23662416; CC P06396; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-351506, EBI-18036948; CC P06396; P20807-4: CAPN3; NbExp=3; IntAct=EBI-351506, EBI-11532021; CC P06396; O00257-3: CBX4; NbExp=3; IntAct=EBI-351506, EBI-4392727; CC P06396; Q49A88-3: CCDC14; NbExp=3; IntAct=EBI-351506, EBI-12105646; CC P06396; Q6ZP82-1: CCDC141; NbExp=3; IntAct=EBI-351506, EBI-49119542; CC P06396; O95388-2: CCN4; NbExp=3; IntAct=EBI-351506, EBI-25863768; CC P06396; P24941: CDK2; NbExp=3; IntAct=EBI-351506, EBI-375096; CC P06396; P38936: CDKN1A; NbExp=3; IntAct=EBI-351506, EBI-375077; CC P06396; O95674: CDS2; NbExp=3; IntAct=EBI-351506, EBI-3913685; CC P06396; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-351506, EBI-749253; CC P06396; Q9H2A9: CHST8; NbExp=3; IntAct=EBI-351506, EBI-21642354; CC P06396; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-351506, EBI-744045; CC P06396; Q96NS8: CLUHP3; NbExp=3; IntAct=EBI-351506, EBI-25864451; CC P06396; Q96BR5: COA7; NbExp=3; IntAct=EBI-351506, EBI-6269632; CC P06396; P02458-1: COL2A1; NbExp=3; IntAct=EBI-351506, EBI-12375799; CC P06396; P21964-2: COMT; NbExp=3; IntAct=EBI-351506, EBI-10200977; CC P06396; Q9UJU6: DBNL; NbExp=3; IntAct=EBI-351506, EBI-751783; CC P06396; Q9NRI5: DISC1; NbExp=2; IntAct=EBI-351506, EBI-529989; CC P06396; Q8NDP9: DKFZp547K2416; NbExp=3; IntAct=EBI-351506, EBI-25842538; CC P06396; Q96EY1-3: DNAJA3; NbExp=3; IntAct=EBI-351506, EBI-11526226; CC P06396; Q92782-2: DPF1; NbExp=3; IntAct=EBI-351506, EBI-23669343; CC P06396; Q7Z7J5: DPPA2; NbExp=3; IntAct=EBI-351506, EBI-741400; CC P06396; Q14117: DPYS; NbExp=3; IntAct=EBI-351506, EBI-12275416; CC P06396; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-351506, EBI-724653; CC P06396; Q9Y6W6: DUSP10; NbExp=3; IntAct=EBI-351506, EBI-3443946; CC P06396; A0AVK6: E2F8; NbExp=3; IntAct=EBI-351506, EBI-7779316; CC P06396; O00472: ELL2; NbExp=3; IntAct=EBI-351506, EBI-395274; CC P06396; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-351506, EBI-11793142; CC P06396; Q8NB25: FAM184A; NbExp=3; IntAct=EBI-351506, EBI-9917523; CC P06396; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-351506, EBI-1384254; CC P06396; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-351506, EBI-11958845; CC P06396; P15407: FOSL1; NbExp=3; IntAct=EBI-351506, EBI-744510; CC P06396; P15408: FOSL2; NbExp=3; IntAct=EBI-351506, EBI-3893419; CC P06396; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-351506, EBI-9088619; CC P06396; P15976-2: GATA1; NbExp=3; IntAct=EBI-351506, EBI-9090198; CC P06396; Q15486: GUSBP1; NbExp=3; IntAct=EBI-351506, EBI-712457; CC P06396; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-351506, EBI-2514791; CC P06396; Q99075: HBEGF; NbExp=3; IntAct=EBI-351506, EBI-7211558; CC P06396; A8K0U2: hCG_2001421; NbExp=3; IntAct=EBI-351506, EBI-25843825; CC P06396; Q5T447-2: HECTD3; NbExp=3; IntAct=EBI-351506, EBI-25854793; CC P06396; Q53T59: HS1BP3; NbExp=3; IntAct=EBI-351506, EBI-11335623; CC P06396; Q53GQ0: HSD17B12; NbExp=3; IntAct=EBI-351506, EBI-2963255; CC P06396; P14060: HSD3B1; NbExp=3; IntAct=EBI-351506, EBI-17426018; CC P06396; Q96EW2-2: HSPBAP1; NbExp=3; IntAct=EBI-351506, EBI-25835621; CC P06396; P41134: ID1; NbExp=3; IntAct=EBI-351506, EBI-1215527; CC P06396; Q8IY31-2: IFT20; NbExp=3; IntAct=EBI-351506, EBI-11742277; CC P06396; P22692: IGFBP4; NbExp=3; IntAct=EBI-351506, EBI-2831948; CC P06396; Q9NZH6: IL37; NbExp=3; IntAct=EBI-351506, EBI-3862125; CC P06396; Q9NXX0: ILF3; NbExp=3; IntAct=EBI-351506, EBI-743980; CC P06396; Q86VI3: IQGAP3; NbExp=3; IntAct=EBI-351506, EBI-1237354; CC P06396; Q8NA54: IQUB; NbExp=3; IntAct=EBI-351506, EBI-10220600; CC P06396; Q86U28: ISCA2; NbExp=3; IntAct=EBI-351506, EBI-10258659; CC P06396; P28290-2: ITPRID2; NbExp=3; IntAct=EBI-351506, EBI-25863618; CC P06396; P05412: JUN; NbExp=3; IntAct=EBI-351506, EBI-852823; CC P06396; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-351506, EBI-743960; CC P06396; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-351506, EBI-9089060; CC P06396; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-351506, EBI-714379; CC P06396; Q9UH77: KLHL3; NbExp=3; IntAct=EBI-351506, EBI-8524663; CC P06396; P08727: KRT19; NbExp=3; IntAct=EBI-351506, EBI-742756; CC P06396; Q14525: KRT33B; NbExp=3; IntAct=EBI-351506, EBI-1049638; CC P06396; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-351506, EBI-1048945; CC P06396; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-351506, EBI-10241353; CC P06396; Q6IAA8: LAMTOR1; NbExp=3; IntAct=EBI-351506, EBI-715385; CC P06396; O43504: LAMTOR5; NbExp=3; IntAct=EBI-351506, EBI-713382; CC P06396; Q14847-2: LASP1; NbExp=3; IntAct=EBI-351506, EBI-9088686; CC P06396; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-351506, EBI-25835523; CC P06396; Q8N0U6: LINC00518; NbExp=3; IntAct=EBI-351506, EBI-10264791; CC P06396; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-351506, EBI-2510853; CC P06396; Q96JB6: LOXL4; NbExp=3; IntAct=EBI-351506, EBI-749562; CC P06396; Q96LR2: LURAP1; NbExp=3; IntAct=EBI-351506, EBI-741355; CC P06396; P0DP58-2: LYNX1; NbExp=3; IntAct=EBI-351506, EBI-21916939; CC P06396; P27338: MAOB; NbExp=3; IntAct=EBI-351506, EBI-3911344; CC P06396; P33993-2: MCM7; NbExp=3; IntAct=EBI-351506, EBI-11741465; CC P06396; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-351506, EBI-348259; CC P06396; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-351506, EBI-2801965; CC P06396; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-351506, EBI-25835557; CC P06396; Q00013: MPP1; NbExp=3; IntAct=EBI-351506, EBI-711788; CC P06396; Q6IN84-2: MRM1; NbExp=3; IntAct=EBI-351506, EBI-25835707; CC P06396; O60783: MRPS14; NbExp=3; IntAct=EBI-351506, EBI-1045956; CC P06396; Q96H12: MSANTD3; NbExp=3; IntAct=EBI-351506, EBI-8466227; CC P06396; P01106: MYC; NbExp=3; IntAct=EBI-351506, EBI-447544; CC P06396; Q9NPC6: MYOZ2; NbExp=3; IntAct=EBI-351506, EBI-746712; CC P06396; P14598: NCF1; NbExp=3; IntAct=EBI-351506, EBI-395044; CC P06396; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-351506, EBI-928842; CC P06396; Q15843: NEDD8; NbExp=3; IntAct=EBI-351506, EBI-716247; CC P06396; Q8NC67-2: NETO2; NbExp=3; IntAct=EBI-351506, EBI-25852289; CC P06396; Q16621: NFE2; NbExp=3; IntAct=EBI-351506, EBI-726369; CC P06396; Q8N5V2: NGEF; NbExp=3; IntAct=EBI-351506, EBI-718372; CC P06396; Q14995: NR1D2; NbExp=3; IntAct=EBI-351506, EBI-6144053; CC P06396; F1D8P7: NR1H2; NbExp=3; IntAct=EBI-351506, EBI-10177172; CC P06396; Q6PHZ7: NR2C2; NbExp=3; IntAct=EBI-351506, EBI-2802743; CC P06396; Q96MF7: NSMCE2; NbExp=3; IntAct=EBI-351506, EBI-2557388; CC P06396; Q4KMX9: OBSCN; NbExp=3; IntAct=EBI-351506, EBI-10490715; CC P06396; A5D8V7: ODAD3; NbExp=3; IntAct=EBI-351506, EBI-8466445; CC P06396; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-351506, EBI-25830200; CC P06396; Q9H8K7: PAAT; NbExp=3; IntAct=EBI-351506, EBI-714785; CC P06396; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-351506, EBI-2513978; CC P06396; Q495U3: PANX2; NbExp=3; IntAct=EBI-351506, EBI-17242559; CC P06396; Q9NR21-5: PARP11; NbExp=3; IntAct=EBI-351506, EBI-17159452; CC P06396; O15534: PER1; NbExp=3; IntAct=EBI-351506, EBI-2557276; CC P06396; Q9BUL5: PHF23; NbExp=3; IntAct=EBI-351506, EBI-722852; CC P06396; Q03405-2: PLAUR; NbExp=3; IntAct=EBI-351506, EBI-11028203; CC P06396; Q9UPR0: PLCL2; NbExp=3; IntAct=EBI-351506, EBI-311059; CC P06396; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-351506, EBI-12891828; CC P06396; Q5SXH7-1: PLEKHS1; NbExp=3; IntAct=EBI-351506, EBI-26412802; CC P06396; P0DPB6: POLR1D; NbExp=3; IntAct=EBI-351506, EBI-359498; CC P06396; Q9P1U0: POLR1H; NbExp=3; IntAct=EBI-351506, EBI-355434; CC P06396; Q07869: PPARA; NbExp=3; IntAct=EBI-351506, EBI-78615; CC P06396; Q9UNP9: PPIE; NbExp=3; IntAct=EBI-351506, EBI-591818; CC P06396; O60237-2: PPP1R12B; NbExp=3; IntAct=EBI-351506, EBI-10700351; CC P06396; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-351506, EBI-710402; CC P06396; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-351506, EBI-25835994; CC P06396; O43741: PRKAB2; NbExp=3; IntAct=EBI-351506, EBI-1053424; CC P06396; O60260-5: PRKN; NbExp=3; IntAct=EBI-351506, EBI-21251460; CC P06396; Q06323: PSME1; NbExp=3; IntAct=EBI-351506, EBI-712149; CC P06396; Q8WUD1-2: RAB2B; NbExp=3; IntAct=EBI-351506, EBI-25835884; CC P06396; Q9UNT1-2: RABL2B; NbExp=3; IntAct=EBI-351506, EBI-12256104; CC P06396; Q15311: RALBP1; NbExp=3; IntAct=EBI-351506, EBI-749285; CC P06396; Q9HD47-3: RANGRF; NbExp=3; IntAct=EBI-351506, EBI-9089733; CC P06396; Q8TBY0: RBM46; NbExp=3; IntAct=EBI-351506, EBI-12068216; CC P06396; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-351506, EBI-1504830; CC P06396; Q04206: RELA; NbExp=3; IntAct=EBI-351506, EBI-73886; CC P06396; P47804-3: RGR; NbExp=3; IntAct=EBI-351506, EBI-25834767; CC P06396; Q8IXN7: RIMKLA; NbExp=3; IntAct=EBI-351506, EBI-21890191; CC P06396; Q8WVD3: RNF138; NbExp=3; IntAct=EBI-351506, EBI-749039; CC P06396; P62899: RPL31; NbExp=3; IntAct=EBI-351506, EBI-1053664; CC P06396; P62244: RPS15A; NbExp=3; IntAct=EBI-351506, EBI-347895; CC P06396; P62701: RPS4X; NbExp=3; IntAct=EBI-351506, EBI-354303; CC P06396; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-351506, EBI-10248967; CC P06396; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-351506, EBI-9089805; CC P06396; Q9UHI5: SLC7A8; NbExp=3; IntAct=EBI-351506, EBI-13292283; CC P06396; Q12824: SMARCB1; NbExp=3; IntAct=EBI-351506, EBI-358419; CC P06396; O14544: SOCS6; NbExp=3; IntAct=EBI-351506, EBI-3929549; CC P06396; Q02086-2: SP2; NbExp=3; IntAct=EBI-351506, EBI-9088579; CC P06396; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-351506, EBI-10696971; CC P06396; Q86W54-2: SPATA24; NbExp=3; IntAct=EBI-351506, EBI-12041693; CC P06396; Q496A3: SPATS1; NbExp=3; IntAct=EBI-351506, EBI-3923692; CC P06396; Q9P2T0: SPMAP2; NbExp=3; IntAct=EBI-351506, EBI-751020; CC P06396; Q9C004: SPRY4; NbExp=3; IntAct=EBI-351506, EBI-354861; CC P06396; Q5W111-2: SPRYD7; NbExp=3; IntAct=EBI-351506, EBI-12408727; CC P06396; Q8N4C7: STX19; NbExp=3; IntAct=EBI-351506, EBI-8484990; CC P06396; Q15814: TBCC; NbExp=3; IntAct=EBI-351506, EBI-15695297; CC P06396; O15273: TCAP; NbExp=3; IntAct=EBI-351506, EBI-954089; CC P06396; Q96A09: TENT5B; NbExp=3; IntAct=EBI-351506, EBI-752030; CC P06396; P54274-2: TERF1; NbExp=3; IntAct=EBI-351506, EBI-711018; CC P06396; Q6N021: TET2; NbExp=3; IntAct=EBI-351506, EBI-310727; CC P06396; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-351506, EBI-12833746; CC P06396; O60830: TIMM17B; NbExp=3; IntAct=EBI-351506, EBI-2372529; CC P06396; Q9BZW5-2: TM6SF1; NbExp=3; IntAct=EBI-351506, EBI-25852210; CC P06396; Q8N0U2: TMEM61; NbExp=3; IntAct=EBI-351506, EBI-25830583; CC P06396; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-351506, EBI-10242677; CC P06396; Q9H8H3: TMT1A; NbExp=3; IntAct=EBI-351506, EBI-1390168; CC P06396; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-351506, EBI-9089156; CC P06396; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-351506, EBI-25831574; CC P06396; P50616: TOB1; NbExp=3; IntAct=EBI-351506, EBI-723281; CC P06396; Q9H496: TOR1AIP2; NbExp=3; IntAct=EBI-351506, EBI-2510146; CC P06396; P36406: TRIM23; NbExp=3; IntAct=EBI-351506, EBI-740098; CC P06396; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-351506, EBI-11525489; CC P06396; Q99598: TSNAX; NbExp=3; IntAct=EBI-351506, EBI-21353855; CC P06396; O60636: TSPAN2; NbExp=3; IntAct=EBI-351506, EBI-3914288; CC P06396; P49459: UBE2A; NbExp=3; IntAct=EBI-351506, EBI-2339348; CC P06396; Q13404: UBE2V1; NbExp=3; IntAct=EBI-351506, EBI-1050671; CC P06396; Q9HA47-2: UCK1; NbExp=3; IntAct=EBI-351506, EBI-16434682; CC P06396; Q9H270: VPS11; NbExp=3; IntAct=EBI-351506, EBI-373380; CC P06396; Q8NEZ2: VPS37A; NbExp=3; IntAct=EBI-351506, EBI-2850578; CC P06396; Q9P1Q0-4: VPS54; NbExp=3; IntAct=EBI-351506, EBI-25835297; CC P06396; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-351506, EBI-10316321; CC P06396; Q8TBZ3-3: WDR20; NbExp=3; IntAct=EBI-351506, EBI-9089370; CC P06396; O00755: WNT7A; NbExp=3; IntAct=EBI-351506, EBI-727198; CC P06396; O43829: ZBTB14; NbExp=3; IntAct=EBI-351506, EBI-10176632; CC P06396; Q9NP64: ZCCHC17; NbExp=3; IntAct=EBI-351506, EBI-746345; CC P06396; Q96JL9-2: ZNF333; NbExp=3; IntAct=EBI-351506, EBI-25835852; CC P06396; Q9C0F3: ZNF436; NbExp=3; IntAct=EBI-351506, EBI-8489702; CC P06396; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-351506, EBI-745520; CC P06396; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-351506, EBI-18036029; CC P06396; B7ZVW5; NbExp=3; IntAct=EBI-351506, EBI-25863917; CC P06396; Q7L8T7; NbExp=3; IntAct=EBI-351506, EBI-25831943; CC P06396; P07830: act21; Xeno; NbExp=4; IntAct=EBI-351506, EBI-7195234; CC P06396; P68135: ACTA1; Xeno; NbExp=10; IntAct=EBI-351506, EBI-367540; CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=4; CC Name=1; Synonyms=Secreted, Plasma; CC IsoId=P06396-1; Sequence=Displayed; CC Name=2; Synonyms=Cytoplasmic; CC IsoId=P06396-2; Sequence=VSP_018959; CC Name=3; CC IsoId=P06396-3; Sequence=VSP_042879; CC Name=4; CC IsoId=P06396-4; Sequence=VSP_054791; CC -!- TISSUE SPECIFICITY: Phagocytic cells, platelets, fibroblasts, nonmuscle CC cells, smooth and skeletal muscle cells. CC -!- DOMAIN: Comprises six structurally related gelsolin-like (G1-G6) CC domains, that, in a calcium-free environment, are packed together to CC form a compact globular structure in which the putative actin-binding CC sequences are not sufficiently exposed to enable binding to occur CC (PubMed:19666512). Binding calcium may release the connections that CC join the N- and C-terminal halves of gelsolin, enabling each half to CC bind actin relatively independently (PubMed:12460571, PubMed:19666512). CC G1 and G4 bind two Ca(2+) in a type I and in a type II manner CC (PubMed:12460571, PubMed:19666512). G2, G3, G5 and G6 bind only one CC Ca(2+) in a type II manner (PubMed:12460571, PubMed:19666512). Type I CC Ca(2+) binding sites are shared between actin and gelsolin-like repeats CC G1 and G4 (PubMed:12460571, PubMed:19666512). Type I binding governs CC the strength of interactions between gelsolin and actin by direct CC participation at the binding interface (PubMed:12460571, CC PubMed:19666512). Ca(2+) binding to G2 and G6 disrupts the interactions CC between G2 and G6, releases the C-terminal tail, and induces large CC interdomain rearrangements that result in the exposure of the F-actin- CC binding site on G2 and contributes to the activation of gelsolin CC (PubMed:12460571, PubMed:19666512). Binding to phosphoinositides may CC inhibit the severing and capping properties of gelsolin (Probable). CC {ECO:0000269|PubMed:12460571, ECO:0000269|PubMed:19666512, CC ECO:0000305|PubMed:8599675}. CC -!- PTM: Phosphorylation on Tyr-86, Tyr-409, Tyr-465, Tyr-603 and Tyr-651 CC in vitro is induced in presence of phospholipids. CC {ECO:0000269|PubMed:10210201}. CC -!- DISEASE: Amyloidosis, hereditary systemic 4, Finnish type (AMYLD4) CC [MIM:105120]: A form of hereditary systemic amyloidosis, a disorder CC characterized by amyloid deposition in multiple tissues resulting in a CC wide clinical spectrum. AMYLD4 is due to gelsolin amyloid deposition CC and is typically characterized by cranial neuropathy and lattice CC corneal dystrophy. Most patients have modest involvement of internal CC organs, but severe systemic disease can develop in some individuals CC causing peripheral polyneuropathy, amyloid cardiomyopathy, and CC nephrotic syndrome leading to renal failure. AMYLD4 is usually CC inherited in an autosomal dominant pattern. However, homozygotes with a CC more severe phenotype have also been reported. CC {ECO:0000269|PubMed:1338910, ECO:0000269|PubMed:19666512, CC ECO:0000269|PubMed:2176481}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Gelsolin entry; CC URL="https://en.wikipedia.org/wiki/Gelsolin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04412; CAA28000.1; -; mRNA. DR EMBL; AK096280; BAG53247.1; -; mRNA. DR EMBL; AK125819; BAG54252.1; -; mRNA. DR EMBL; AK295572; BAH12109.1; -; mRNA. DR EMBL; AK299453; BAH13037.1; -; mRNA. DR EMBL; AK315494; BAG37878.1; -; mRNA. DR EMBL; AL137068; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL513122; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87489.1; -; Genomic_DNA. DR EMBL; CH471090; EAW87490.1; -; Genomic_DNA. DR EMBL; CH471090; EAW87491.1; -; Genomic_DNA. DR EMBL; BC017491; AAH17491.1; -; mRNA. DR EMBL; BC026033; AAH26033.1; -; mRNA. DR CCDS; CCDS48011.1; -. [P06396-3] DR CCDS; CCDS65118.1; -. [P06396-4] DR CCDS; CCDS6828.1; -. [P06396-1] DR CCDS; CCDS6829.1; -. [P06396-2] DR PIR; A03011; FAHUP. DR RefSeq; NP_000168.1; NM_000177.4. [P06396-1] DR RefSeq; NP_001121134.1; NM_001127662.1. [P06396-2] DR RefSeq; NP_001121135.2; NM_001127663.1. DR RefSeq; NP_001121136.1; NM_001127664.1. [P06396-2] DR RefSeq; NP_001121137.1; NM_001127665.1. [P06396-2] DR RefSeq; NP_001121138.1; NM_001127666.1. [P06396-3] DR RefSeq; NP_001121139.1; NM_001127667.1. [P06396-3] DR RefSeq; NP_001244958.1; NM_001258029.1. DR RefSeq; NP_001244959.1; NM_001258030.1. [P06396-4] DR RefSeq; NP_937895.1; NM_198252.2. [P06396-2] DR RefSeq; XP_005252000.1; XM_005251943.1. DR RefSeq; XP_005252001.1; XM_005251944.1. [P06396-3] DR RefSeq; XP_005252002.1; XM_005251945.3. DR RefSeq; XP_006717142.1; XM_006717079.1. DR RefSeq; XP_011516888.1; XM_011518586.1. DR RefSeq; XP_011516889.1; XM_011518587.2. DR RefSeq; XP_011516890.1; XM_011518588.2. DR RefSeq; XP_011516891.1; XM_011518589.2. DR RefSeq; XP_011516892.1; XM_011518590.2. DR RefSeq; XP_011516893.1; XM_011518591.2. DR RefSeq; XP_011516894.1; XM_011518592.1. DR RefSeq; XP_011516895.1; XM_011518593.1. DR RefSeq; XP_016870135.1; XM_017014646.1. DR RefSeq; XP_016870136.1; XM_017014647.1. DR RefSeq; XP_016870137.1; XM_017014648.1. DR PDB; 1C0F; X-ray; 2.40 A; S=53-176. DR PDB; 1C0G; X-ray; 2.00 A; S=53-176. DR PDB; 1D4X; X-ray; 1.75 A; G=52-177. DR PDB; 1DEJ; X-ray; 2.40 A; S=53-176. DR PDB; 1EQY; X-ray; 2.30 A; S=52-176. DR PDB; 1ESV; X-ray; 2.00 A; S=52-176. DR PDB; 1H1V; X-ray; 3.00 A; G=439-769. DR PDB; 1KCQ; X-ray; 1.65 A; A=185-288. DR PDB; 1MDU; X-ray; 2.20 A; A/D=52-176. DR PDB; 1NLV; X-ray; 1.80 A; G=52-176. DR PDB; 1NM1; X-ray; 1.80 A; G=52-176. DR PDB; 1NMD; X-ray; 1.90 A; G=52-176. DR PDB; 1P8X; X-ray; 2.00 A; A/B/C=439-782. DR PDB; 1P8Z; X-ray; 2.60 A; G=52-187. DR PDB; 1SOL; NMR; -; A=177-196. DR PDB; 1T44; X-ray; 2.00 A; G=55-179. DR PDB; 1YAG; X-ray; 1.90 A; G=52-176. DR PDB; 1YVN; X-ray; 2.10 A; G=52-176. DR PDB; 2FF3; X-ray; 2.00 A; A=52-179. DR PDB; 2FF6; X-ray; 2.05 A; G=52-179. DR PDB; 2FH1; X-ray; 1.55 A; A/B/C=439-782. DR PDB; 2FH2; X-ray; 2.50 A; A/B/C=439-782. DR PDB; 2FH3; X-ray; 2.87 A; A/B/C=439-782. DR PDB; 2FH4; X-ray; 3.00 A; A/B/C=439-782. DR PDB; 3A5L; X-ray; 2.40 A; S=53-176. DR PDB; 3A5M; X-ray; 2.40 A; S=53-176. DR PDB; 3A5N; X-ray; 2.36 A; S=53-176. DR PDB; 3A5O; X-ray; 2.40 A; S=53-176. DR PDB; 3CI5; X-ray; 1.70 A; G=52-176. DR PDB; 3CIP; X-ray; 1.60 A; G=52-176. DR PDB; 3CJB; X-ray; 3.21 A; G=52-176. DR PDB; 3CJC; X-ray; 3.90 A; G=52-176. DR PDB; 3FFK; X-ray; 3.00 A; A/D=52-426. DR PDB; 3FFN; X-ray; 3.00 A; A/B=1-782. DR PDB; 3TU5; X-ray; 3.00 A; B=53-174. DR PDB; 4PKG; X-ray; 1.80 A; G=52-176. DR PDB; 4PKH; X-ray; 2.15 A; B/E/G/J=52-176, B/E/G/J=196-260. DR PDB; 4PKI; X-ray; 2.30 A; G=52-176. DR PDB; 4S10; X-ray; 2.61 A; C/D=186-288. DR PDB; 4Z94; X-ray; 2.40 A; G=52-176. DR PDB; 5FAE; X-ray; 1.70 A; A=178-293. DR PDB; 5FAF; X-ray; 1.05 A; A=178-293. DR PDB; 5H3M; NMR; -; A=55-187. DR PDB; 5H3N; NMR; -; A=55-187. DR PDB; 5O2Z; X-ray; 1.70 A; A/B=178-293. DR PDB; 5UBO; X-ray; 2.39 A; S=52-178. DR PDB; 5ZZ0; X-ray; 2.63 A; A/G=55-188. DR PDB; 6H1F; X-ray; 1.90 A; B=178-293. DR PDB; 6JCO; X-ray; 2.88 A; A/B=56-782. DR PDB; 6JEG; X-ray; 2.98 A; A/B=54-782. DR PDB; 6JEH; X-ray; 2.95 A; A/B=56-782. DR PDB; 6LJE; X-ray; 1.40 A; A/B=297-397. DR PDB; 6LJF; X-ray; 1.50 A; A/B=297-397. DR PDB; 6Q9R; X-ray; 2.73 A; A/B=28-782. DR PDB; 6Q9Z; X-ray; 3.80 A; A/B=28-782. DR PDB; 6QBF; X-ray; 3.50 A; A/B=28-782. DR PDB; 6QW3; X-ray; 1.30 A; A=178-293. DR PDB; 7P2B; X-ray; 3.00 A; A/B=28-782. DR PDBsum; 1C0F; -. DR PDBsum; 1C0G; -. DR PDBsum; 1D4X; -. DR PDBsum; 1DEJ; -. DR PDBsum; 1EQY; -. DR PDBsum; 1ESV; -. DR PDBsum; 1H1V; -. DR PDBsum; 1KCQ; -. DR PDBsum; 1MDU; -. DR PDBsum; 1NLV; -. DR PDBsum; 1NM1; -. DR PDBsum; 1NMD; -. DR PDBsum; 1P8X; -. DR PDBsum; 1P8Z; -. DR PDBsum; 1SOL; -. DR PDBsum; 1T44; -. DR PDBsum; 1YAG; -. DR PDBsum; 1YVN; -. DR PDBsum; 2FF3; -. DR PDBsum; 2FF6; -. DR PDBsum; 2FH1; -. DR PDBsum; 2FH2; -. DR PDBsum; 2FH3; -. DR PDBsum; 2FH4; -. DR PDBsum; 3A5L; -. DR PDBsum; 3A5M; -. DR PDBsum; 3A5N; -. DR PDBsum; 3A5O; -. DR PDBsum; 3CI5; -. DR PDBsum; 3CIP; -. DR PDBsum; 3CJB; -. DR PDBsum; 3CJC; -. DR PDBsum; 3FFK; -. DR PDBsum; 3FFN; -. DR PDBsum; 3TU5; -. DR PDBsum; 4PKG; -. DR PDBsum; 4PKH; -. DR PDBsum; 4PKI; -. DR PDBsum; 4S10; -. DR PDBsum; 4Z94; -. DR PDBsum; 5FAE; -. DR PDBsum; 5FAF; -. DR PDBsum; 5H3M; -. DR PDBsum; 5H3N; -. DR PDBsum; 5O2Z; -. DR PDBsum; 5UBO; -. DR PDBsum; 5ZZ0; -. DR PDBsum; 6H1F; -. DR PDBsum; 6JCO; -. DR PDBsum; 6JEG; -. DR PDBsum; 6JEH; -. DR PDBsum; 6LJE; -. DR PDBsum; 6LJF; -. DR PDBsum; 6Q9R; -. DR PDBsum; 6Q9Z; -. DR PDBsum; 6QBF; -. DR PDBsum; 6QW3; -. DR PDBsum; 7P2B; -. DR AlphaFoldDB; P06396; -. DR SASBDB; P06396; -. DR SMR; P06396; -. DR BioGRID; 109189; 209. DR CORUM; P06396; -. DR DIP; DIP-2196N; -. DR IntAct; P06396; 322. DR MINT; P06396; -. DR STRING; 9606.ENSP00000362924; -. DR ChEMBL; CHEMBL4295700; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB02621; Latrunculin A. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR GlyCosmos; P06396; 8 sites, 3 glycans. DR GlyGen; P06396; 10 sites, 5 O-linked glycans (10 sites). DR iPTMnet; P06396; -. DR MetOSite; P06396; -. DR PhosphoSitePlus; P06396; -. DR SwissPalm; P06396; -. DR BioMuta; GSN; -. DR DMDM; 121116; -. DR OGP; P06396; -. DR CPTAC; non-CPTAC-1126; -. DR CPTAC; non-CPTAC-1127; -. DR jPOST; P06396; -. DR MassIVE; P06396; -. DR PaxDb; 9606-ENSP00000362924; -. DR PeptideAtlas; P06396; -. DR PRIDE; P06396; -. DR ProteomicsDB; 25596; -. DR ProteomicsDB; 51897; -. [P06396-1] DR ProteomicsDB; 51898; -. [P06396-2] DR ProteomicsDB; 51899; -. [P06396-3] DR Pumba; P06396; -. DR ABCD; P06396; 5 sequenced antibodies. DR Antibodypedia; 3387; 840 antibodies from 48 providers. DR CPTC; P06396; 4 antibodies. DR DNASU; 2934; -. DR Ensembl; ENST00000373808.8; ENSP00000362914.3; ENSG00000148180.22. [P06396-3] DR Ensembl; ENST00000373818.8; ENSP00000362924.4; ENSG00000148180.22. [P06396-1] DR Ensembl; ENST00000373823.7; ENSP00000362929.2; ENSG00000148180.22. [P06396-2] DR Ensembl; ENST00000432226.7; ENSP00000404226.2; ENSG00000148180.22. [P06396-2] DR Ensembl; ENST00000545652.6; ENSP00000445823.1; ENSG00000148180.22. [P06396-4] DR GeneID; 2934; -. DR KEGG; hsa:2934; -. DR MANE-Select; ENST00000432226.7; ENSP00000404226.2; NM_198252.3; NP_937895.1. [P06396-2] DR UCSC; uc004ble.1; human. [P06396-1] DR AGR; HGNC:4620; -. DR CTD; 2934; -. DR DisGeNET; 2934; -. DR GeneCards; GSN; -. DR HGNC; HGNC:4620; GSN. DR HPA; ENSG00000148180; Tissue enhanced (heart). DR MalaCards; GSN; -. DR MIM; 105120; phenotype. DR MIM; 137350; gene. DR neXtProt; NX_P06396; -. DR OpenTargets; ENSG00000148180; -. DR Orphanet; 85448; AGel amyloidosis. DR PharmGKB; PA29011; -. DR VEuPathDB; HostDB:ENSG00000148180; -. DR eggNOG; KOG0443; Eukaryota. DR GeneTree; ENSGT00940000155591; -. DR HOGENOM; CLU_002568_3_2_1; -. DR InParanoid; P06396; -. DR OrthoDB; 25995at2759; -. DR PhylomeDB; P06396; -. DR TreeFam; TF313468; -. DR PathwayCommons; P06396; -. DR Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea. DR Reactome; R-HSA-977225; Amyloid fiber formation. DR SABIO-RK; P06396; -. DR SignaLink; P06396; -. DR SIGNOR; P06396; -. DR BioGRID-ORCS; 2934; 11 hits in 1153 CRISPR screens. DR ChiTaRS; GSN; human. DR EvolutionaryTrace; P06396; -. DR GeneWiki; Gelsolin; -. DR GenomeRNAi; 2934; -. DR Pharos; P06396; Tbio. DR PRO; PR:P06396; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P06396; protein. DR Bgee; ENSG00000148180; Expressed in synovial joint and 211 other cell types or tissues. DR ExpressionAtlas; P06396; baseline and differential. DR GO; GO:0030478; C:actin cap; IDA:UniProtKB. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl. DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0002102; C:podosome; IDA:UniProtKB. DR GO; GO:0016528; C:sarcoplasm; IDA:UniProtKB. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IMP:UniProtKB. DR GO; GO:0045159; F:myosin II binding; IPI:UniProtKB. DR GO; GO:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; IPI:BHF-UCL. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central. DR GO; GO:0051693; P:actin filament capping; IMP:UniProtKB. DR GO; GO:0030042; P:actin filament depolymerization; IDA:BHF-UCL. DR GO; GO:0007015; P:actin filament organization; IGI:UniProtKB. DR GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB. DR GO; GO:0051014; P:actin filament severing; IDA:UniProtKB. DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central. DR GO; GO:1990000; P:amyloid fibril formation; IMP:UniProtKB. DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central. DR GO; GO:0086003; P:cardiac muscle cell contraction; ISS:BHF-UCL. 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; IMP:UniProtKB. DR GO; GO:0097284; P:hepatocyte apoptotic process; IMP:UniProtKB. DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IMP:UniProtKB. DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB. DR GO; GO:0051127; P:positive regulation of actin nucleation; IMP:UniProtKB. DR GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:1902174; P:positive regulation of keratinocyte apoptotic process; IMP:UniProtKB. DR GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; ISS:UniProtKB. DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB. DR GO; GO:1903903; P:regulation of establishment of T cell polarity; IMP:UniProtKB. DR GO; GO:1903906; P:regulation of plasma membrane raft polarization; IMP:UniProtKB. DR GO; GO:0071801; P:regulation of podosome assembly; IMP:UniProtKB. DR GO; GO:1903909; P:regulation of receptor clustering; IMP:UniProtKB. DR GO; GO:0055119; P:relaxation of cardiac muscle; ISS:BHF-UCL. DR GO; GO:0097017; P:renal protein absorption; IMP:UniProtKB. DR GO; GO:0035994; P:response to muscle stretch; ISS:BHF-UCL. DR GO; GO:0042989; P:sequestering of actin monomers; IMP:UniProtKB. DR GO; GO:0014891; P:striated muscle atrophy; IMP:UniProtKB. 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 IDEAL; IID00265; -. 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 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin capping; Actin-binding; KW Alternative initiation; Alternative splicing; Amyloid; Amyloidosis; KW Calcium; Cilium biogenesis/degradation; Corneal dystrophy; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Disease variant; Disulfide bond; KW Metal-binding; Phosphoprotein; Proteomics identification; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..27 FT CHAIN 28..782 FT /note="Gelsolin" FT /id="PRO_0000036385" FT REPEAT 76..158 FT /note="Gelsolin-like 1" FT /evidence="ECO:0000255" FT REPEAT 198..270 FT /note="Gelsolin-like 2" FT /evidence="ECO:0000255" FT REPEAT 317..389 FT /note="Gelsolin-like 3" FT /evidence="ECO:0000255" FT REPEAT 455..536 FT /note="Gelsolin-like 4" FT /evidence="ECO:0000255" FT REPEAT 576..642 FT /note="Gelsolin-like 5" FT /evidence="ECO:0000255" FT REPEAT 681..756 FT /note="Gelsolin-like 6" FT /evidence="ECO:0000255" FT REGION 53..176 FT /note="Actin-severing" FT /evidence="ECO:0000255" FT REGION 123..126 FT /note="Actin-actin interfilament contact point" FT REGION 247..285 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 434..782 FT /note="Actin-binding, Ca-sensitive" FT /evidence="ECO:0000255" FT COMPBIAS 247..264 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 92 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 93 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 124 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 136 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="type I" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 141 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="type I" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 143 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="type I" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 162..169 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 172 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 188..196 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 213 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 214 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 236 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 286 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 329 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 330 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 354 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0007744|PDB:3FFK" FT BINDING 471 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, FT ECO:0007744|PDB:2FH2, ECO:0007744|PDB:2FH3" FT BINDING 472 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, FT ECO:0007744|PDB:2FH1, ECO:0007744|PDB:2FH2, FT ECO:0007744|PDB:2FH3" FT BINDING 502 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, FT ECO:0007744|PDB:2FH1, ECO:0007744|PDB:2FH2, FT ECO:0007744|PDB:2FH3" FT BINDING 514 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /ligand_note="type I" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0007744|PDB:1H1V" FT BINDING 519 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /ligand_note="type I" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0007744|PDB:1H1V" FT BINDING 521 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /ligand_note="type I" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0007744|PDB:1H1V" FT BINDING 551 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, FT ECO:0007744|PDB:2FH1, ECO:0007744|PDB:2FH2, FT ECO:0007744|PDB:2FH3" FT BINDING 591 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, FT ECO:0007744|PDB:2FH1, ECO:0007744|PDB:2FH2, FT ECO:0007744|PDB:2FH3" FT BINDING 592 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, FT ECO:0007744|PDB:2FH1, ECO:0007744|PDB:2FH2, FT ECO:0007744|PDB:2FH3" FT BINDING 614 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, FT ECO:0007744|PDB:2FH2, ECO:0007744|PDB:2FH3" FT BINDING 696 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, FT ECO:0007744|PDB:2FH1, ECO:0007744|PDB:2FH2, FT ECO:0007744|PDB:2FH3" FT BINDING 697 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, FT ECO:0007744|PDB:2FH3" FT BINDING 719 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /ligand_note="type II" FT /evidence="ECO:0000269|PubMed:12460571, FT ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, FT ECO:0007744|PDB:2FH1, ECO:0007744|PDB:2FH2, FT ECO:0007744|PDB:2FH3" FT MOD_RES 86 FT /note="Phosphotyrosine; by SRC; in vitro" FT /evidence="ECO:0000269|PubMed:10210201" FT MOD_RES 409 FT /note="Phosphotyrosine; by SRC; in vitro" FT /evidence="ECO:0000269|PubMed:10210201" FT MOD_RES 465 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000269|PubMed:10210201" FT MOD_RES 584 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13020" FT MOD_RES 603 FT /note="Phosphotyrosine; by SRC; in vitro" FT /evidence="ECO:0000269|PubMed:10210201" FT MOD_RES 651 FT /note="Phosphotyrosine; by SRC; in vitro" FT /evidence="ECO:0000269|PubMed:10210201" FT MOD_RES 742 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT DISULFID 215..228 FT /note="In isoform 1" FT /evidence="ECO:0000269|PubMed:19666512, FT ECO:0000269|PubMed:8703941, ECO:0000269|PubMed:9003812" FT VAR_SEQ 1..51 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:3020431" FT /id="VSP_018959" FT VAR_SEQ 1..48 FT /note="MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEAR -> FT MEKLFCCF (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042879" FT VAR_SEQ 1..48 FT /note="MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEAR -> FT MPLCT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054791" FT VARIANT 22 FT /note="S -> L (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036337" FT VARIANT 129 FT /note="A -> T (in dbSNP:rs2230287)" FT /id="VAR_024690" FT VARIANT 201 FT /note="T -> I (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036338" FT VARIANT 214 FT /note="D -> N (in AMYLD4; does not result in actin FT depolymerization in absence of calcium; dbSNP:rs121909715)" FT /evidence="ECO:0000269|PubMed:1338910, FT ECO:0000269|PubMed:19666512, ECO:0000269|PubMed:2176481" FT /id="VAR_007718" FT VARIANT 214 FT /note="D -> Y (in AMYLD4; dbSNP:rs121909715)" FT /evidence="ECO:0000269|PubMed:1338910" FT /id="VAR_007719" FT VARIANT 231 FT /note="N -> D (in dbSNP:rs11550199)" FT /id="VAR_061982" FT VARIANT 611 FT /note="S -> N (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036339" FT VARIANT 668 FT /note="R -> L (in dbSNP:rs9696578)" FT /id="VAR_033958" FT MUTAGEN 236 FT /note="E->Q: Does not result in actin depolymerization FT activity in absence of calcium. Has actin depolymerization FT activity in absence of calcium; when associated with N-214 FT and N-697 or N-214, N-697 and Q-719." FT /evidence="ECO:0000269|PubMed:19666512" FT MUTAGEN 697 FT /note="D->N: Does not result in actin depolymerization FT activity in absence of calcium. Has actin depolymerization FT activity in absence of calcium; when associated with N-214 FT and Q-236, N-214 and Q-719 or N-214, Q-236 and Q-719." FT /evidence="ECO:0000269|PubMed:19666512" FT MUTAGEN 719 FT /note="E->Q: Does not result in actin depolymerization FT activity in absence of calcium. Has actin depolymerization FT activity in absence of calcium; when associated with N-214 FT and N-697 or N-214, Q-236 and N-697." FT /evidence="ECO:0000269|PubMed:19666512" FT CONFLICT 294 FT /note="N -> D (in Ref. 2; BAH13037)" FT /evidence="ECO:0000305" FT CONFLICT 419 FT /note="R -> W (in Ref. 2; BAH13037)" FT /evidence="ECO:0000305" FT CONFLICT 603 FT /note="Y -> H (in Ref. 2; BAH13037)" FT /evidence="ECO:0000305" FT STRAND 52..55 FT /evidence="ECO:0007829|PDB:3FFN" FT HELIX 57..61 FT /evidence="ECO:0007829|PDB:3CIP" FT STRAND 64..74 FT /evidence="ECO:0007829|PDB:3CIP" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:3CIP" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:3CIP" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:3CIP" FT STRAND 94..102 FT /evidence="ECO:0007829|PDB:3CIP" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:1P8Z" FT STRAND 108..116 FT /evidence="ECO:0007829|PDB:3CIP" FT HELIX 122..138 FT /evidence="ECO:0007829|PDB:3CIP" FT TURN 139..141 FT /evidence="ECO:0007829|PDB:3CIP" FT STRAND 143..149 FT /evidence="ECO:0007829|PDB:3CIP" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:5H3M" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:3CIP" FT STRAND 166..169 FT /evidence="ECO:0007829|PDB:3CIP" FT TURN 172..175 FT /evidence="ECO:0007829|PDB:6Q9R" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:5H3M" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:1SOL" FT HELIX 183..186 FT /evidence="ECO:0007829|PDB:5H3M" FT STRAND 188..193 FT /evidence="ECO:0007829|PDB:5FAF" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:5FAF" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:5FAF" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:5FAF" FT STRAND 214..219 FT /evidence="ECO:0007829|PDB:5FAF" FT STRAND 221..228 FT /evidence="ECO:0007829|PDB:5FAF" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:6JCO" FT HELIX 234..251 FT /evidence="ECO:0007829|PDB:5FAF" FT STRAND 256..262 FT /evidence="ECO:0007829|PDB:5FAF" FT TURN 263..265 FT /evidence="ECO:0007829|PDB:3FFK" FT HELIX 268..274 FT /evidence="ECO:0007829|PDB:5FAF" FT HELIX 292..294 FT /evidence="ECO:0007829|PDB:6Q9R" FT STRAND 299..304 FT /evidence="ECO:0007829|PDB:6LJE" FT STRAND 306..309 FT /evidence="ECO:0007829|PDB:3FFN" FT STRAND 311..316 FT /evidence="ECO:0007829|PDB:6LJE" FT STRAND 318..321 FT /evidence="ECO:0007829|PDB:6LJE" FT HELIX 323..325 FT /evidence="ECO:0007829|PDB:6LJE" FT STRAND 330..336 FT /evidence="ECO:0007829|PDB:6LJE" FT HELIX 337..339 FT /evidence="ECO:0007829|PDB:6LJE" FT STRAND 341..346 FT /evidence="ECO:0007829|PDB:6LJE" FT HELIX 352..368 FT /evidence="ECO:0007829|PDB:6LJE" FT STRAND 377..381 FT /evidence="ECO:0007829|PDB:6LJE" FT HELIX 387..390 FT /evidence="ECO:0007829|PDB:6LJE" FT STRAND 393..395 FT /evidence="ECO:0007829|PDB:6JEH" FT STRAND 401..406 FT /evidence="ECO:0007829|PDB:6Q9R" FT HELIX 412..414 FT /evidence="ECO:0007829|PDB:6Q9R" FT HELIX 424..429 FT /evidence="ECO:0007829|PDB:6Q9R" FT HELIX 431..437 FT /evidence="ECO:0007829|PDB:6Q9R" FT STRAND 445..453 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 456..459 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 462..464 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 467..469 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 472..482 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 485..494 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 500..516 FT /evidence="ECO:0007829|PDB:2FH1" FT TURN 517..519 FT /evidence="ECO:0007829|PDB:1P8X" FT STRAND 521..527 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 533..536 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 537..539 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 544..548 FT /evidence="ECO:0007829|PDB:2FH1" FT TURN 553..555 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 562..570 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 576..581 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 585..587 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 592..597 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 602..606 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 612..624 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 630..633 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 639..644 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 645..647 FT /evidence="ECO:0007829|PDB:2FH4" FT HELIX 655..658 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 661..664 FT /evidence="ECO:0007829|PDB:6Q9R" FT STRAND 668..673 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 676..678 FT /evidence="ECO:0007829|PDB:6JEH" FT STRAND 680..684 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 690..692 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 697..702 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 707..711 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 717..732 FT /evidence="ECO:0007829|PDB:2FH1" FT TURN 735..737 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 744..748 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 754..757 FT /evidence="ECO:0007829|PDB:2FH1" FT STRAND 760..762 FT /evidence="ECO:0007829|PDB:2FH1" FT HELIX 767..769 FT /evidence="ECO:0007829|PDB:6Q9R" FT HELIX 772..778 FT /evidence="ECO:0007829|PDB:6Q9R" SQ SEQUENCE 782 AA; 85698 MW; 8CEBC52257A160F7 CRC64; MAPHRPAPAL LCALSLALCA LSLPVRAATA SRGASQAGAP QGRVPEARPN SMVVEHPEFL KAGKEPGLQI WRVEKFDLVP VPTNLYGDFF TGDAYVILKT VQLRNGNLQY DLHYWLGNEC SQDESGAAAI FTVQLDDYLN GRAVQHREVQ GFESATFLGY FKSGLKYKKG GVASGFKHVV PNEVVVQRLF QVKGRRVVRA TEVPVSWESF NNGDCFILDL GNNIHQWCGS NSNRYERLKA TQVSKGIRDN ERSGRARVHV SEEGTEPEAM LQVLGPKPAL PAGTEDTAKE DAANRKLAKL YKVSNGAGTM SVSLVADENP FAQGALKSED CFILDHGKDG KIFVWKGKQA NTEERKAALK TASDFITKMD YPKQTQVSVL PEGGETPLFK QFFKNWRDPD QTDGLGLSYL SSHIANVERV PFDAATLHTS TAMAAQHGMD DDGTGQKQIW RIEGSNKVPV DPATYGQFYG GDSYIILYNY RHGGRQGQII YNWQGAQSTQ DEVAASAILT AQLDEELGGT PVQSRVVQGK EPAHLMSLFG GKPMIIYKGG TSREGGQTAP ASTRLFQVRA NSAGATRAVE VLPKAGALNS NDAFVLKTPS AAYLWVGTGA SEAEKTGAQE LLRVLRAQPV QVAEGSEPDG FWEALGGKAA YRTSPRLKDK KMDAHPPRLF ACSNKIGRFV IEEVPGELMQ EDLATDDVML LDTWDQVFVW VGKDSQEEEK TEALTSAKRY IETDPANRDR RTPITVVKQG FEPPSFVGWF LGWDDDYWSV DPLDRAMAEL AA //