GELS_HUMAN
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 03-AUG-2022, entry version 249.
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 AMYL5 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 AMYL5 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]
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]
RP STRUCTURE BY NMR OF 177-196.
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]
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 [20]
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 [21]
RP VARIANT AMYL5 ASN-214.
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 [22]
RP VARIANTS AMYL5 ASN-214 AND TYR-214.
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 [23]
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. Plays a role in ciliogenesis.
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). {ECO:0000250}.
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; D3DTF8: APLN; NbExp=3; IntAct=EBI-351506, EBI-22002556;
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: CCDC141; NbExp=3; IntAct=EBI-351506, EBI-928795;
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; A0A0C4DGV4: LAMTOR5; NbExp=3; IntAct=EBI-351506, EBI-10173304;
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; Q9H8H3: METTL7A; NbExp=3; IntAct=EBI-351506, EBI-1390168;
CC P06396; D3DX41: MGC16703; NbExp=3; IntAct=EBI-351506, EBI-25850974;
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; 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; Q9P2T0: THEG; NbExp=3; IntAct=EBI-351506, EBI-751020;
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; 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-742638;
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 -!- 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 5 (AMYL5) [MIM:105120]: A hereditary generalized
CC amyloidosis due to gelsolin amyloid deposition. It is typically
CC characterized by cranial neuropathy and lattice corneal dystrophy. Most
CC patients have modest involvement of internal organs, but severe
CC systemic disease can develop in some individuals causing peripheral
CC polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading
CC to renal failure. {ECO:0000269|PubMed:1338910,
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";
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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. [P06396-2]
DR RefSeq; XP_016870135.1; XM_017014646.1.
DR RefSeq; XP_016870136.1; XM_017014647.1.
DR RefSeq; XP_016870137.1; XM_017014648.1. [P06396-3]
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; 5DD2; X-ray; 2.60 A; A/G=55-188.
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 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; 5DD2; -.
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 AlphaFoldDB; P06396; -.
DR SMR; P06396; -.
DR BioGRID; 109189; 172.
DR CORUM; P06396; -.
DR DIP; DIP-2196N; -.
DR IntAct; P06396; 296.
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 GlyGen; P06396; 9 sites, 4 O-linked glycans (9 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 EPD; P06396; -.
DR jPOST; P06396; -.
DR MassIVE; P06396; -.
DR MaxQB; P06396; -.
DR PaxDb; P06396; -.
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 ABCD; P06396; 5 sequenced antibodies.
DR Antibodypedia; 3387; 770 antibodies from 47 providers.
DR CPTC; P06396; 4 antibodies.
DR DNASU; 2934; -.
DR Ensembl; ENST00000373808.8; ENSP00000362914.3; ENSG00000148180.21. [P06396-3]
DR Ensembl; ENST00000373818.8; ENSP00000362924.4; ENSG00000148180.21. [P06396-1]
DR Ensembl; ENST00000373823.7; ENSP00000362929.2; ENSG00000148180.21. [P06396-2]
DR Ensembl; ENST00000432226.7; ENSP00000404226.2; ENSG00000148180.21. [P06396-2]
DR Ensembl; ENST00000545652.6; ENSP00000445823.1; ENSG00000148180.21. [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 CTD; 2934; -.
DR DisGeNET; 2934; -.
DR GeneCards; GSN; -.
DR HGNC; HGNC:4620; GSN.
DR HPA; ENSG00000148180; Low tissue specificity.
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; 1376537at2759; -.
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; 9 hits in 1073 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 209 other tissues.
DR ExpressionAtlas; P06396; baseline and differential.
DR Genevisible; P06396; HS.
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:0030041; P:actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0090527; P:actin filament reorganization; IGI:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; IDA:UniProtKB.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
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 interferon-gamma; 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 Gene3D; 3.40.20.10; -; 6.
DR IDEAL; IID00265; -.
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;
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; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..27
FT CHAIN 28..782
FT /note="Gelsolin"
FT /id="PRO_0000036385"
FT REPEAT 76..126
FT /note="Gelsolin-like 1"
FT REPEAT 198..238
FT /note="Gelsolin-like 2"
FT REPEAT 314..356
FT /note="Gelsolin-like 3"
FT REPEAT 453..504
FT /note="Gelsolin-like 4"
FT REPEAT 576..616
FT /note="Gelsolin-like 5"
FT REPEAT 679..721
FT /note="Gelsolin-like 6"
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 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 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 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 551
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 591
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 592
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 614
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 696
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 697
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 719
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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:8703941,
FT 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 AMYL5; dbSNP:rs121909715)"
FT /evidence="ECO:0000269|PubMed:1338910,
FT ECO:0000269|PubMed:2176481"
FT /id="VAR_007718"
FT VARIANT 214
FT /note="D -> Y (in AMYL5; 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 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
