FSCN1_MOUSE
ID FSCN1_MOUSE Reviewed; 493 AA.
AC Q61553; O09099; O09156; Q05DK3; Q7TN32; Q80V75;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Fascin;
DE AltName: Full=Singed-like protein;
GN Name=Fscn1; Synonyms=Fan1, Snl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7738015; DOI=10.1074/jbc.270.18.10764;
RA Edwards R.A., Herrera-Sosa H., Otto J., Bryan J.;
RT "Cloning and expression of a murine fascin homolog from mouse brain.";
RL J. Biol. Chem. 270:10764-10770(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ASSOCIATION WITH CTNNB1.
RC STRAIN=129/SvJ;
RX PubMed=8794867; DOI=10.1083/jcb.134.5.1271;
RA Tao Y.S., Edwards R.A., Tubb B., Wang S., Bryan J., McCrea P.D.;
RT "Beta-catenin associates with the actin-bundling protein fascin in a
RT noncadherin complex.";
RL J. Cell Biol. 134:1271-1281(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryonic brain, and Mammary gland;
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 [5]
RP PROTEIN SEQUENCE OF 23-32; 69-82; 132-149; 168-185; 202-217; 248-271;
RP 380-389 AND 409-426, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 [8]
RP FUNCTION.
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 [9]
RP SUBCELLULAR LOCATION.
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 [10]
RP INTERACTION WITH PLXNB3.
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP INTERACTION WITH RUFY3, AND SUBCELLULAR LOCATION.
RX PubMed=24720729; DOI=10.1111/jnc.12740;
RA Wei Z., Sun M., Liu X., Zhang J., Jin Y.;
RT "Rufy3, a protein specifically expressed in neurons, interacts with actin-
RT bundling protein Fascin to control the growth of axons.";
RL J. Neurochem. 130:678-692(2014).
CC -!- FUNCTION: Actin-binding protein that contains 2 major actin binding
CC sites (By similarity). Organizes filamentous actin into parallel
CC bundles (PubMed:7738015). Plays a role in the organization of actin
CC filament bundles and the formation of microspikes, membrane ruffles,
CC and stress fibers (By similarity). Important for the formation of a
CC diverse set of cell protrusions, such as filopodia, and for cell
CC motility and migration (PubMed:21685497). Mediates reorganization of
CC the actin cytoskeleton and axon growth cone collapse in response to NGF
CC (By similarity). {ECO:0000250|UniProtKB:Q16658,
CC ECO:0000269|PubMed:21685497, ECO:0000269|PubMed:7738015}.
CC -!- SUBUNIT: Interacts with RUFY3 (via N-terminus); the interaction induces
CC neuron axon development (PubMed:24720729). Interacts with NGFR (By
CC similarity). Associates with CTNNB1 (PubMed:8794867). Interacts with
CC PLXNB3 (PubMed:21706053). {ECO:0000250|UniProtKB:P85845,
CC ECO:0000269|PubMed:21706053, ECO:0000269|PubMed:24720729,
CC ECO:0000269|PubMed:8794867}.
CC -!- INTERACTION:
CC Q61553; Q9QY40: Plxnb3; NbExp=3; IntAct=EBI-2308857, EBI-6271317;
CC Q61553; P68135: ACTA1; Xeno; NbExp=2; IntAct=EBI-2308857, EBI-367540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q16658}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q16658}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q16658}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q16658}. Cell projection, growth cone
CC {ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:24720729}. Cell
CC projection, filopodium {ECO:0000269|PubMed:22155786,
CC ECO:0000269|PubMed:24720729}. Cell projection, invadopodium
CC {ECO:0000269|PubMed:24720729}. Cell projection, microvillus
CC {ECO:0000250|UniProtKB:Q16658}. Cell junction
CC {ECO:0000250|UniProtKB:Q16658}. Note=Colocalized with RUFY3 and F-actin
CC at filipodia of the axonal growth cone (PubMed:24720729). Colocalized
CC with DBN1 and F-actin at the transitional domain of the axonal growth
CC cone (PubMed:24720729). {ECO:0000250|UniProtKB:Q16658,
CC ECO:0000269|PubMed:24720729}.
CC -!- TISSUE SPECIFICITY: Most abundant in brain. Detected at lower levels in
CC lung, uterus, small intestine and spleen (at protein level).
CC {ECO:0000269|PubMed:7738015}.
CC -!- DOMAIN: Composed of four fascin beta-trefoil domains.
CC {ECO:0000250|UniProtKB:Q16658}.
CC -!- PTM: Phosphorylation at Ser-39 inhibits actin-binding. Phosphorylation
CC is required for the reorganization of the actin cytoskeleton in
CC response to NGF. {ECO:0000250|UniProtKB:Q16658}.
CC -!- SIMILARITY: Belongs to the fascin family. {ECO:0000305}.
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DR EMBL; L33726; AAB41126.1; -; mRNA.
DR EMBL; U90355; AAB58784.1; -; Genomic_DNA.
DR EMBL; AK167670; BAE39719.1; -; mRNA.
DR EMBL; BC010338; AAH10338.1; -; mRNA.
DR EMBL; BC037137; AAH37137.2; -; mRNA.
DR EMBL; BC052408; AAH52408.1; -; mRNA.
DR CCDS; CCDS19834.1; -.
DR PIR; A56430; A56430.
DR RefSeq; NP_032010.2; NM_007984.2.
DR AlphaFoldDB; Q61553; -.
DR SMR; Q61553; -.
DR BioGRID; 199590; 6.
DR DIP; DIP-54657N; -.
DR IntAct; Q61553; 5.
DR MINT; Q61553; -.
DR STRING; 10090.ENSMUSP00000031565; -.
DR iPTMnet; Q61553; -.
DR PhosphoSitePlus; Q61553; -.
DR SwissPalm; Q61553; -.
DR REPRODUCTION-2DPAGE; IPI00353563; -.
DR EPD; Q61553; -.
DR jPOST; Q61553; -.
DR MaxQB; Q61553; -.
DR PaxDb; Q61553; -.
DR PeptideAtlas; Q61553; -.
DR PRIDE; Q61553; -.
DR ProteomicsDB; 271609; -.
DR Antibodypedia; 1483; 867 antibodies from 45 providers.
DR DNASU; 14086; -.
DR Ensembl; ENSMUST00000031565; ENSMUSP00000031565; ENSMUSG00000029581.
DR GeneID; 14086; -.
DR KEGG; mmu:14086; -.
DR UCSC; uc009ajl.1; mouse.
DR CTD; 6624; -.
DR MGI; MGI:1352745; Fscn1.
DR VEuPathDB; HostDB:ENSMUSG00000029581; -.
DR eggNOG; ENOG502QPRX; Eukaryota.
DR GeneTree; ENSGT00950000183157; -.
DR HOGENOM; CLU_030960_2_0_1; -.
DR InParanoid; Q61553; -.
DR OMA; YNKLAIR; -.
DR OrthoDB; 1419861at2759; -.
DR PhylomeDB; Q61553; -.
DR TreeFam; TF323992; -.
DR BioGRID-ORCS; 14086; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Fscn1; mouse.
DR PRO; PR:Q61553; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q61553; protein.
DR Bgee; ENSMUSG00000029581; Expressed in external carotid artery and 294 other tissues.
DR ExpressionAtlas; Q61553; baseline and differential.
DR Genevisible; Q61553; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0031253; C:cell projection membrane; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0044393; C:microspike; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IMP:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0007043; P:cell-cell junction assembly; ISS:UniProtKB.
DR GO; GO:0035089; P:establishment of apical/basal cell polarity; ISS:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0030035; P:microspike assembly; ISS:UniProtKB.
DR GO; GO:0030046; P:parallel actin filament bundle assembly; ISO:MGI.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0071803; P:positive regulation of podosome assembly; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0032534; P:regulation of microvillus assembly; ISS: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 Acetylation; Actin-binding; Cell junction; Cell projection; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16658,
FT ECO:0000269|PubMed:7738015"
FT CHAIN 2..493
FT /note="Fascin"
FT /id="PRO_0000219380"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16658"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16658"
FT MOD_RES 39
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q16658"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16658"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16658"
FT MOD_RES 239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16658"
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:0000250|UniProtKB:Q16658"
FT CONFLICT 64
FT /note="S -> T (in Ref. 1; AAB41126 and 2; AAB58784)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="Q -> E (in Ref. 1; AAB41126 and 2; AAB58784)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="R -> G (in Ref. 1; AAB41126 and 2; AAB58784)"
FT /evidence="ECO:0000305"
FT CONFLICT 362..363
FT /note="QL -> HV (in Ref. 1; AAB41126 and 2; AAB58784)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="V -> A (in Ref. 1; AAB41126 and 2; AAB58784)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="G -> A (in Ref. 1; AAB41126 and 2; AAB58784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 54508 MW; 1C6DCD5211B74969 CRC64;
MTANGTAEAV QIQFGLISCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ PPDEAGSAAV
CLRSHLGRYL AADKDGNVTC EREVPDGDCR FLVVAHDDGR WSLQSEAHRR YFGGTEDRLS
CFAQSVSPAE KWSVHIAMHP QVNIYSVTRK RYAHLSARPA DEIAVDRDVP WGVDSLITLA
FQDQRYSVQT SDHRFLRHDG RLVARPEPAT GFTLEFRSGK VAFRDCEGRY LAPSGPSGTL
KAGKATKVGK DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR
DTRKCAFRTH TGKYWTLTAT GGVQSTASTK NASCYFDIEW CDRRITLRAS NGKFVTAKKN
GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV TGTLDANRSS YDVFQLEFND
GAYNIKDSTG KYWTVGSDSS VTSSSDTPVD FFLEFCDYNK VALKVGGRYL KGDHAGVLKA
CAETIDPASL WEY
