FSCN1_RAT
ID FSCN1_RAT Reviewed; 493 AA.
AC P85845; B5DEI1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Fascin;
GN Name=Fscn1 {ECO:0000250|UniProtKB:Q16658};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, ACTIN-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=8769857; DOI=10.1046/j.1471-4159.1996.66030980.x;
RA Sasaki Y., Hayashi K., Shirao T., Ishikawa R., Kohama K.;
RT "Inhibition by drebrin of the actin-bundling activity of brain fascin, a
RT protein localized in filopodia of growth cones.";
RL J. Neurochem. 66:980-988(1996).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
RN [4]
RP FUNCTION, INTERACTION WITH NGFR, TISSUE SPECIFICITY, MUTAGENESIS OF, AND
RP PHOSPHORYLATION AT.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-403, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Actin-binding protein that contains 2 major actin binding
CC sites (PubMed:8769857). Organizes filamentous actin into parallel
CC bundles (PubMed:8769857). Plays a role in the organization of actin
CC filament bundles and the formation of microspikes, membrane ruffles,
CC and stress fibers. Important for the formation of a diverse set of cell
CC protrusions, such as filopodia, and for cell motility and migration.
CC Mediates reorganization of the actin cytoskeleton and axon growth cone
CC collapse in response to NGF (By similarity).
CC {ECO:0000250|UniProtKB:Q16658, ECO:0000269|PubMed:8769857}.
CC -!- SUBUNIT: Interacts with RUFY3 (via N-terminus); the interaction induces
CC neuron axon development (By similarity). Interacts with NGFR
CC (PubMed:22155786). Associates with CTNNB1 (By similarity). Interacts
CC with PLXNB3 (By similarity). {ECO:0000250|UniProtKB:Q16658,
CC ECO:0000250|UniProtKB:Q61553, ECO:0000269|PubMed:22155786}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19343716}.
CC Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q16658}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q16658}. Cytoplasm, cytoskeleton,
CC stress fiber {ECO:0000250|UniProtKB:Q16658}. Cell projection, growth
CC cone {ECO:0000269|PubMed:8769857}. Cell projection, filopodium
CC {ECO:0000269|PubMed:8769857}. Cell projection, invadopodium
CC {ECO:0000250|UniProtKB:Q61553}. 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. Colocalized with DBN1 and F-
CC actin at the transitional domain of the axonal growth cone.
CC {ECO:0000250|UniProtKB:Q16658, ECO:0000250|UniProtKB:Q61553}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic brain and brain from young
CC rats (at protein level). {ECO:0000269|PubMed:22155786,
CC ECO:0000269|PubMed:8769857}.
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:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC168678; AAI68678.1; -; mRNA.
DR RefSeq; NP_001094276.1; NM_001100806.1.
DR AlphaFoldDB; P85845; -.
DR SMR; P85845; -.
DR BioGRID; 598682; 3.
DR IntAct; P85845; 4.
DR MINT; P85845; -.
DR iPTMnet; P85845; -.
DR PhosphoSitePlus; P85845; -.
DR World-2DPAGE; 0004:P85845; -.
DR jPOST; P85845; -.
DR PRIDE; P85845; -.
DR GeneID; 683788; -.
DR KEGG; rno:683788; -.
DR CTD; 6624; -.
DR RGD; 1583309; Fscn1.
DR InParanoid; P85845; -.
DR OrthoDB; 1419861at2759; -.
DR PhylomeDB; P85845; -.
DR PRO; PR:P85845; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0030175; C:filopodium; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0044393; C:microspike; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:RGD.
DR GO; GO:0001725; C:stress fiber; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0007043; P:cell-cell junction assembly; ISS:UniProtKB.
DR GO; GO:0071460; P:cellular response to cell-matrix adhesion; IEP:RGD.
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:0001889; P:liver development; IEP:RGD.
DR GO; GO:0030035; P:microspike assembly; ISS:UniProtKB.
DR GO; GO:0030046; P:parallel actin filament bundle assembly; ISO:RGD.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS: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; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16658"
FT CHAIN 2..493
FT /note="Fascin"
FT /id="PRO_0000343450"
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:0000250|UniProtKB:Q61553"
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:0007744|PubMed:22673903"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16658"
SQ SEQUENCE 493 AA; 54491 MW; 5680527FA91F7B10 CRC64;
MTANGTAEAV QIQFGLISCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ PPDEAGSAAV
CLRSHLGPYL 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 CERRITLRAS NGKFVTAKKN
GQLAATVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV TGTLDANRSS YDVFQLEFND
GAYNIKDSTG KYWTVGSDSS VTSSSDTPVD FFLEFCDYNK VALKVGGRYL KGDHAGVLKA
CAETIDPATL WEY
