FSCN1_HUMAN
ID FSCN1_HUMAN Reviewed; 493 AA.
AC Q16658; A6NI89; B2RE97; Q96IC5; Q96IH1; Q9BRF1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Fascin;
DE AltName: Full=55 kDa actin-bundling protein;
DE AltName: Full=Singed-like protein;
DE AltName: Full=p55;
GN Name=FSCN1; Synonyms=FAN1, HSN, SNL;
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].
RC TISSUE=Teratocarcinoma;
RX PubMed=8068206; DOI=10.1089/dna.1994.13.821;
RA Duh F.-M., Latif F., Weng Y., Geil L., Modi W., Stackhouse T.,
RA Matsumura F., Duan D.R., Linehan W.M., Lerman M.I., Gnarra J.R.;
RT "cDNA cloning and expression of the human homolog of the sea urchin fascin
RT and Drosophila singed genes which encodes an actin-bundling protein.";
RL DNA Cell Biol. 13:821-827(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7933116; DOI=10.1128/jvi.68.11.7320-7328.1994;
RA Mosialos G., Yamashiro S., Baughman R.W., Matsudaira P., Vara L.,
RA Matsumura F., Kieff E., Birkenbach M.;
RT "Epstein-Barr virus infection induces expression in B lymphocytes of a
RT novel gene encoding an evolutionarily conserved 55-kilodalton actin-
RT bundling protein.";
RL J. Virol. 68:7320-7328(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bros M., Ross X.L., Reske-Kunz A.B., Ross R.;
RT "Human fascin gene sequence.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Eye, Lung, and Muscle;
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 [9]
RP PROTEIN SEQUENCE OF 2-32; 44-63; 69-82; 111-149; 159-185; 202-217; 230-241;
RP 248-271; 314-341; 409-426 AND 469-493, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2010) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 119-149; 202-217; 230-241; 314-330 AND 380-389, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=3525578; DOI=10.1083/jcb.103.2.631;
RA Yamashiro-Matsumura S., Matsumura F.;
RT "Intracellular localization of the 55-kD actin-bundling protein in cultured
RT cells: spatial relationships with actin, alpha-actinin, tropomyosin, and
RT fimbrin.";
RL J. Cell Biol. 103:631-640(1986).
RN [12]
RP PHOSPHORYLATION.
RX PubMed=8647875; DOI=10.1074/jbc.271.21.12632;
RA Yamakita Y., Ono S., Matsumura F., Yamashiro S.;
RT "Phosphorylation of human fascin inhibits its actin binding and bundling
RT activities.";
RL J. Biol. Chem. 271:12632-12638(1996).
RN [13]
RP FUNCTION.
RX PubMed=9362073; DOI=10.1091/mbc.8.11.2345;
RA Adams J.C.;
RT "Characterization of cell-matrix adhesion requirements for the formation of
RT fascin microspikes.";
RL Mol. Biol. Cell 8:2345-2363(1997).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9571235; DOI=10.1091/mbc.9.5.993;
RA Yamashiro S., Yamakita Y., Ono S., Matsumura F.;
RT "Fascin, an actin-bundling protein, induces membrane protrusions and
RT increases cell motility of epithelial cells.";
RL Mol. Biol. Cell 9:993-1006(1998).
RN [15]
RP PHOSPHORYLATION AT SER-39, AND MUTAGENESIS OF SER-39.
RX PubMed=8999969; DOI=10.1074/jbc.272.4.2527;
RA Ono S., Yamakita Y., Yamashiro S., Matsudaira P.T., Gnarra J.R.,
RA Obinata T., Matsumura F.;
RT "Identification of an actin binding region and a protein kinase C
RT phosphorylation site on human fascin.";
RL J. Biol. Chem. 272:2527-2533(1997).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20137952; DOI=10.1016/j.cub.2009.12.035;
RA Li A., Dawson J.C., Forero-Vargas M., Spence H.J., Yu X., Konig I.,
RA Anderson K., Machesky L.M.;
RT "The actin-bundling protein fascin stabilizes actin in invadopodia and
RT potentiates protrusive invasion.";
RL Curr. Biol. 20:339-345(2010).
RN [18]
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 [19]
RP FUNCTION, MUTAGENESIS OF 36-SER--SER-39, AND PHOSPHORYLATION.
RX PubMed=22155786; DOI=10.1126/scisignal.2002060;
RA Deinhardt K., Kim T., Spellman D.S., Mains R.E., Eipper B.A., Neubert T.A.,
RA Chao M.V., Hempstead B.L.;
RT "Neuronal growth cone retraction relies on proneurotrophin receptor
RT signaling through Rac.";
RL Sci. Signal. 4:RA82-RA82(2011).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [22]
RP INTERACTION WITH PLXNB3, AND SUBCELLULAR LOCATION.
RX PubMed=21706053; DOI=10.1038/onc.2011.256;
RA Li X., Law J.W., Lee A.Y.;
RT "Semaphorin 5A and plexin-B3 regulate human glioma cell motility and
RT morphology through Rac1 and the actin cytoskeleton.";
RL Oncogene 31:595-610(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-234 AND THR-239, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [24]
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 [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-399, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), AND DOMAIN.
RX PubMed=20434460; DOI=10.1016/j.jmb.2010.04.043;
RA Sedeh R.S., Fedorov A.A., Fedorov E.V., Ono S., Matsumura F., Almo S.C.,
RA Bathe M.;
RT "Structure, evolutionary conservation, and conformational dynamics of Homo
RT sapiens fascin-1, an F-actin crosslinking protein.";
RL J. Mol. Biol. 400:589-604(2010).
RN [27] {ECO:0007744|PDB:3LLP}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, DOMAIN, AND MUTAGENESIS
RP OF HIS-392; LYS-471 AND ALA-488.
RX PubMed=20393565; DOI=10.1038/nature08978;
RA Chen L., Yang S., Jakoncic J., Zhang J.J., Huang X.Y.;
RT "Migrastatin analogues target fascin to block tumour metastasis.";
RL Nature 464:1062-1066(2010).
RN [28]
RP ERRATUM OF PUBMED:20393565, AND RETRACTION NOTICE OF PUBMED:20393565 OF TWO
RP 3D-STRUCTURES.
RX DOI=10.1038/nature10281;
RA Chen L., Yang S., Jakoncic J., Zhang J.J., Huang X.Y.;
RL Nature 476:0-0(2011).
RN [29] {ECO:0007744|PDB:3P53}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, DOMAIN, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-22; LYS-43; ARG-100; ARG-109;
RP 150-LYS-LYS-151; LYS-247; ARG-271; LYS-313; ARG-341; ARG-348; LYS-353;
RP LYS-358; ARG-398 AND LYS-464.
RX PubMed=21685497; DOI=10.1074/jbc.m111.251439;
RA Jansen S., Collins A., Yang C., Rebowski G., Svitkina T., Dominguez R.;
RT "Mechanism of actin filament bundling by fascin.";
RL J. Biol. Chem. 286:30087-30096(2011).
RN [30] {ECO:0007744|PDB:4GOV, ECO:0007744|PDB:4GOY, ECO:0007744|PDB:4GP0, ECO:0007744|PDB:4GP3}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), FUNCTION, AND MUTAGENESIS OF
RP PHE-29; SER-39; 149-ARG--ARG-151; 247-LYS--LYS-250 AND LYS-358.
RX PubMed=23184945; DOI=10.1074/jbc.m112.427971;
RA Yang S., Huang F.K., Huang J., Chen S., Jakoncic J., Leo-Macias A.,
RA Diaz-Avalos R., Chen L., Zhang J.J., Huang X.Y.;
RT "Molecular mechanism of fascin function in filopodial formation.";
RL J. Biol. Chem. 288:274-284(2013).
CC -!- FUNCTION: Actin-binding protein that contains 2 major actin binding
CC sites (PubMed:21685497, PubMed:23184945). Organizes filamentous actin
CC into parallel bundles (PubMed:20393565, PubMed:21685497,
CC PubMed:23184945). Plays a role in the organization of actin filament
CC bundles and the formation of microspikes, membrane ruffles, and stress
CC fibers (PubMed:22155786). Important for the formation of a diverse set
CC of cell protrusions, such as filopodia, and for cell motility and
CC migration (PubMed:20393565, PubMed:21685497, PubMed:23184945). Mediates
CC reorganization of the actin cytoskeleton and axon growth cone collapse
CC in response to NGF (PubMed:22155786). {ECO:0000269|PubMed:20137952,
CC ECO:0000269|PubMed:20393565, ECO:0000269|PubMed:21685497,
CC ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:23184945,
CC ECO:0000269|PubMed:9362073, ECO:0000269|PubMed:9571235}.
CC -!- SUBUNIT: Interacts with RUFY3 (via N-terminus); the interaction induces
CC neuron axon development (By similarity). Interacts with NGFR (By
CC similarity). Associates with CTNNB1 (By similarity). Interacts with
CC PLXNB3 (PubMed:21706053). {ECO:0000250|UniProtKB:P85845,
CC ECO:0000250|UniProtKB:Q61553, ECO:0000269|PubMed:21706053}.
CC -!- INTERACTION:
CC Q16658; Q9BXW9: FANCD2; NbExp=6; IntAct=EBI-351076, EBI-359343;
CC Q16658; P40692: MLH1; NbExp=7; IntAct=EBI-351076, EBI-744248;
CC Q16658; Q9ULL4: PLXNB3; NbExp=2; IntAct=EBI-351076, EBI-311073;
CC Q16658; P63104: YWHAZ; NbExp=3; IntAct=EBI-351076, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21706053,
CC ECO:0000269|PubMed:9571235}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:21685497}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21685497, ECO:0000269|PubMed:3525578,
CC ECO:0000269|PubMed:9571235}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:21706053}. Cell projection, filopodium
CC {ECO:0000269|PubMed:20137952, ECO:0000269|PubMed:21685497,
CC ECO:0000269|PubMed:3525578}. Cell projection, invadopodium
CC {ECO:0000269|PubMed:20137952}. Cell projection, microvillus
CC {ECO:0000269|PubMed:9571235}. Cell junction
CC {ECO:0000269|PubMed:9571235}. Note=Colocalized with RUFY3 and F-actin
CC at filipodia of the axonal growth cone. Colocalized with DBN1 and F-
CC actin at the transitional domain of the axonal growth cone (By
CC similarity). {ECO:0000250|UniProtKB:Q61553,
CC ECO:0000269|PubMed:21706053}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: Composed of four fascin beta-trefoil domains.
CC {ECO:0000269|PubMed:20393565, ECO:0000269|PubMed:20434460,
CC ECO:0000269|PubMed:21685497, ECO:0000269|PubMed:23184945}.
CC -!- PTM: Phosphorylation at Ser-39 inhibits actin-binding (PubMed:8647875,
CC PubMed:8999969). Phosphorylation is required for the reorganization of
CC the actin cytoskeleton in response to NGF (PubMed:22155786).
CC {ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:8647875,
CC ECO:0000269|PubMed:8999969}.
CC -!- SIMILARITY: Belongs to the fascin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07539.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FSCN1ID44342ch7p22.html";
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DR EMBL; U03057; AAA86442.1; -; mRNA.
DR EMBL; U09873; AAA62201.1; -; mRNA.
DR EMBL; AY044229; AAL01526.1; -; Genomic_DNA.
DR EMBL; AK316607; BAG38194.1; -; mRNA.
DR EMBL; BT006636; AAP35282.1; -; mRNA.
DR EMBL; AC006483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471144; EAW87346.1; -; Genomic_DNA.
DR EMBL; BC000521; AAH00521.1; -; mRNA.
DR EMBL; BC006304; AAH06304.1; -; mRNA.
DR EMBL; BC007539; AAH07539.1; ALT_INIT; mRNA.
DR EMBL; BC007643; AAH07643.1; -; mRNA.
DR EMBL; BC007948; AAH07948.1; -; mRNA.
DR EMBL; BC007988; AAH07988.1; -; mRNA.
DR CCDS; CCDS5342.1; -.
DR PIR; I38621; I38621.
DR RefSeq; NP_003079.1; NM_003088.3.
DR PDB; 1DFC; X-ray; 2.90 A; A/B=1-493.
DR PDB; 3LLP; X-ray; 1.80 A; A/B=1-493.
DR PDB; 3P53; X-ray; 2.00 A; A/B=1-493.
DR PDB; 4GOV; X-ray; 2.20 A; A/B=1-493.
DR PDB; 4GOY; X-ray; 2.30 A; A/B=1-493.
DR PDB; 4GP0; X-ray; 2.50 A; A/B=1-493.
DR PDB; 4GP3; X-ray; 2.25 A; A/B=1-493.
DR PDB; 6B0T; X-ray; 2.80 A; A/B/C/D/E/F=7-493.
DR PDB; 6I0Z; X-ray; 1.77 A; A/B=1-493.
DR PDB; 6I10; X-ray; 2.10 A; A=1-493.
DR PDB; 6I11; X-ray; 1.67 A; A=1-493.
DR PDB; 6I12; X-ray; 1.65 A; A=1-493.
DR PDB; 6I13; X-ray; 1.79 A; A=1-493.
DR PDB; 6I14; X-ray; 1.73 A; A=1-493.
DR PDB; 6I15; X-ray; 1.91 A; A=1-493.
DR PDB; 6I16; X-ray; 2.00 A; A=1-493.
DR PDB; 6I17; X-ray; 1.56 A; A=1-493.
DR PDB; 6I18; X-ray; 1.49 A; A=1-493.
DR PDBsum; 1DFC; -.
DR PDBsum; 3LLP; -.
DR PDBsum; 3P53; -.
DR PDBsum; 4GOV; -.
DR PDBsum; 4GOY; -.
DR PDBsum; 4GP0; -.
DR PDBsum; 4GP3; -.
DR PDBsum; 6B0T; -.
DR PDBsum; 6I0Z; -.
DR PDBsum; 6I10; -.
DR PDBsum; 6I11; -.
DR PDBsum; 6I12; -.
DR PDBsum; 6I13; -.
DR PDBsum; 6I14; -.
DR PDBsum; 6I15; -.
DR PDBsum; 6I16; -.
DR PDBsum; 6I17; -.
DR PDBsum; 6I18; -.
DR AlphaFoldDB; Q16658; -.
DR SMR; Q16658; -.
DR BioGRID; 112508; 263.
DR DIP; DIP-33171N; -.
DR IntAct; Q16658; 53.
DR MINT; Q16658; -.
DR STRING; 9606.ENSP00000371798; -.
DR BindingDB; Q16658; -.
DR ChEMBL; CHEMBL4523304; -.
DR GlyGen; Q16658; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16658; -.
DR MetOSite; Q16658; -.
DR PhosphoSitePlus; Q16658; -.
DR SwissPalm; Q16658; -.
DR BioMuta; FSCN1; -.
DR DMDM; 2498357; -.
DR REPRODUCTION-2DPAGE; IPI00163187; -.
DR REPRODUCTION-2DPAGE; Q16658; -.
DR UCD-2DPAGE; Q16658; -.
DR CPTAC; CPTAC-1403; -.
DR CPTAC; CPTAC-1404; -.
DR CPTAC; CPTAC-1405; -.
DR CPTAC; CPTAC-1406; -.
DR CPTAC; CPTAC-373; -.
DR CPTAC; CPTAC-709; -.
DR EPD; Q16658; -.
DR jPOST; Q16658; -.
DR MassIVE; Q16658; -.
DR MaxQB; Q16658; -.
DR PaxDb; Q16658; -.
DR PeptideAtlas; Q16658; -.
DR PRIDE; Q16658; -.
DR ProteomicsDB; 61017; -.
DR ABCD; Q16658; 1 sequenced antibody.
DR Antibodypedia; 1483; 867 antibodies from 45 providers.
DR CPTC; Q16658; 4 antibodies.
DR DNASU; 6624; -.
DR Ensembl; ENST00000382361.8; ENSP00000371798.3; ENSG00000075618.18.
DR GeneID; 6624; -.
DR KEGG; hsa:6624; -.
DR MANE-Select; ENST00000382361.8; ENSP00000371798.3; NM_003088.4; NP_003079.1.
DR UCSC; uc003sou.4; human.
DR CTD; 6624; -.
DR DisGeNET; 6624; -.
DR GeneCards; FSCN1; -.
DR HGNC; HGNC:11148; FSCN1.
DR HPA; ENSG00000075618; Low tissue specificity.
DR MIM; 602689; gene.
DR neXtProt; NX_Q16658; -.
DR OpenTargets; ENSG00000075618; -.
DR PharmGKB; PA128394534; -.
DR VEuPathDB; HostDB:ENSG00000075618; -.
DR eggNOG; ENOG502QPRX; Eukaryota.
DR GeneTree; ENSGT00950000183157; -.
DR HOGENOM; CLU_030960_2_0_1; -.
DR InParanoid; Q16658; -.
DR OMA; YNKLAIR; -.
DR OrthoDB; 1419861at2759; -.
DR PhylomeDB; Q16658; -.
DR TreeFam; TF323992; -.
DR PathwayCommons; Q16658; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; Q16658; -.
DR SIGNOR; Q16658; -.
DR BioGRID-ORCS; 6624; 8 hits in 1082 CRISPR screens.
DR ChiTaRS; FSCN1; human.
DR EvolutionaryTrace; Q16658; -.
DR GeneWiki; FSCN1; -.
DR GenomeRNAi; 6624; -.
DR Pharos; Q16658; Tchem.
DR PRO; PR:Q16658; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q16658; protein.
DR Bgee; ENSG00000075618; Expressed in stromal cell of endometrium and 185 other tissues.
DR ExpressionAtlas; Q16658; baseline and differential.
DR Genevisible; Q16658; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0031253; C:cell projection membrane; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0044393; C:microspike; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0002102; C:podosome; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0048870; P:cell motility; IDA:UniProtKB.
DR GO; GO:0007043; P:cell-cell junction assembly; IDA:UniProtKB.
DR GO; GO:0035089; P:establishment of apical/basal cell polarity; IDA:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0030035; P:microspike assembly; IDA:UniProtKB.
DR GO; GO:0030046; P:parallel actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IDA:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IDA:UniProtKB.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IDA:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0032534; P:regulation of microvillus assembly; IDA:UniProtKB.
DR CDD; cd00257; Fascin; 4.
DR InterPro; IPR008999; Actin-crosslinking.
DR InterPro; IPR010431; Fascin.
DR InterPro; IPR022768; Fascin-domain.
DR InterPro; IPR024703; Fascin_metazoans.
DR InterPro; IPR030146; FSCN1.
DR PANTHER; PTHR10551; PTHR10551; 1.
DR PANTHER; PTHR10551:SF23; PTHR10551:SF23; 1.
DR Pfam; PF06268; Fascin; 4.
DR PIRSF; PIRSF005682; Fascin; 1.
DR SUPFAM; SSF50405; SSF50405; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell junction; Cell projection;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895"
FT CHAIN 2..493
FT /note="Fascin"
FT /id="PRO_0000219379"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 39
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8999969,
FT ECO:0000305|PubMed:22155786"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61553"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 239
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 403
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P85845"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT MUTAGEN 22
FT /note="K->E: Decreased actin-binding and loss of actin-
FT bundling activity; when associated with E-43 and E-398.
FT Decreased actin-binding and loss of actin-bundling
FT activity; when associated with E-43; E-100 and E-109."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 29
FT /note="F->A: Strongly decreases actin-bundling activity."
FT /evidence="ECO:0000269|PubMed:23184945"
FT MUTAGEN 36..39
FT /note="SASS->AAAA: Abolishes axon growth cone collapse in
FT response to NGF."
FT /evidence="ECO:0000269|PubMed:22155786"
FT MUTAGEN 39
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:8999969"
FT MUTAGEN 39
FT /note="S->D: Phosphomimetic mutant that strongly decreases
FT actin-bundling activity."
FT /evidence="ECO:0000269|PubMed:23184945"
FT MUTAGEN 43
FT /note="K->E: Decreased actin-binding and loss of actin-
FT bundling activity; when associated with E-22 and E-398.
FT Decreased actin-binding and loss of actin-bundling
FT activity; when associated with E-22; E-100 and E-109."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 49
FT /note="E->A: Strongly decreases actin-bundling activity."
FT /evidence="ECO:0000269|PubMed:23184945"
FT MUTAGEN 100
FT /note="R->E: Mildly decreased actin-binding and actin-
FT bundling activity; when associated with E-109 and E-247.
FT Decreased actin-binding and loss of actin-bundling
FT activity; when associated with E-22; E-43 and E-109."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 109
FT /note="R->E: Mildly decreased actin-binding and actin-
FT bundling activity; when associated with E-100 and E-247.
FT Decreased actin-binding and loss of actin-bundling
FT activity; when associated with E-22; E-43 and E-100."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 149..151
FT /note="RKR->AAA: Strongly decreases actin-bundling
FT activity."
FT /evidence="ECO:0000269|PubMed:23184945"
FT MUTAGEN 150..151
FT /note="KR->EE: No significant effect on actin-binding and
FT actin-bundling activity; when associated with E-313."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 247..250
FT /note="KVGK->AVGA: Decreases actin-bundling activity."
FT /evidence="ECO:0000269|PubMed:23184945"
FT MUTAGEN 247
FT /note="K->E: Mildly decreased actin-binding and actin-
FT bundling activity; when associated with E-100 and E-109."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 271
FT /note="R->E: Decreased actin-binding and actin-bundling
FT activity; when associated with E-353 and E-358."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 313
FT /note="K->E: No significant effect on actin-binding and
FT actin-bundling activity; when associated with 150-E-E-151."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 341
FT /note="R->E: No significant effect on actin-binding and
FT actin-bundling activity; when associated with E-348 and Q-
FT 464."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 348
FT /note="R->E: No significant effect on actin-binding and
FT actin-bundling activity; when associated with E-341 and Q-
FT 464."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 353
FT /note="K->E: Decreased actin-binding and actin-bundling
FT activity; when associated with E-271 and E-358."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 358
FT /note="K->A: Strongly decreases actin-bundling activity."
FT /evidence="ECO:0000269|PubMed:23184945"
FT MUTAGEN 358
FT /note="K->E: Decreased actin-binding and actin-bundling
FT activity; when associated with E-271 and E-353."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 392
FT /note="H->A: Decreased actin-bundling activity."
FT /evidence="ECO:0000269|PubMed:20393565"
FT MUTAGEN 398
FT /note="R->E: Decreased actin-binding and loss of actin-
FT bundling activity; when associated with E-22 and E-43."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 464
FT /note="K->Q: No significant effect on actin-binding and
FT actin-bundling activity; when associated with E-341 and E-
FT 348."
FT /evidence="ECO:0000269|PubMed:21685497"
FT MUTAGEN 471
FT /note="K->A: Decreased actin-bundling activity."
FT /evidence="ECO:0000269|PubMed:20393565"
FT MUTAGEN 488
FT /note="A->W: Decreased actin-bundling activity."
FT /evidence="ECO:0000269|PubMed:20393565"
FT CONFLICT 440
FT /note="A -> V (in Ref. 8; AAH06304)"
FT /evidence="ECO:0000305"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:6I18"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:6I18"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3P53"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6B0T"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:6I18"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1DFC"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:6I18"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:6I18"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:6I18"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6I13"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:6I18"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3LLP"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:3LLP"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:6I18"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:6I18"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:6I18"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:6I18"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:6I10"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:6I18"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:6I18"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:6I18"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:1DFC"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 321..329
FT /evidence="ECO:0007829|PDB:6I18"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 361..369
FT /evidence="ECO:0007829|PDB:6I18"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:6I18"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 439..447
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 476..484
FT /evidence="ECO:0007829|PDB:6I18"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:6I18"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:4GOV"
SQ SEQUENCE 493 AA; 54530 MW; C1453714BED6109A CRC64;
MTANGTAEAV QIQFGLINCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ PPDEAGSAAV
CLRSHLGRYL AADKDGNVTC EREVPGPDCR FLIVAHDDGR WSLQSEAHRR YFGGTEDRLS
CFAQTVSPAE KWSVHIAMHP QVNIYSVTRK RYAHLSARPA DEIAVDRDVP WGVDSLITLA
FQDQRYSVQT ADHRFLRHDG RLVARPEPAT GYTLEFRSGK VAFRDCEGRY LAPSGPSGTL
KAGKATKVGK DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR
DTKKCAFRTH TGKYWTLTAT GGVQSTASSK NASCYFDIEW RDRRITLRAS NGKFVTSKKN
GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV TGTLDANRSS YDVFQLEFND
GAYNIKDSTG KYWTVGSDSA VTSSGDTPVD FFFEFCDYNK VAIKVGGRYL KGDHAGVLKA
SAETVDPASL WEY
