SING_DROME
ID SING_DROME Reviewed; 512 AA.
AC Q24524; Q9W3L8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein singed;
GN Name=sn; ORFNames=CG1536;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=1723709; DOI=10.1093/genetics/129.4.1073;
RA Paterson J., O'Hare K.;
RT "Structure and transcription of the singed locus of Drosophila
RT melanogaster.";
RL Genetics 129:1073-1084(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP FUNCTION, AND INTERACTION WITH RAB35.
RX PubMed=19729655; DOI=10.1126/science.1174921;
RA Zhang J., Fonovic M., Suyama K., Bogyo M., Scott M.P.;
RT "Rab35 controls actin bundling by recruiting fascin as an effector
RT protein.";
RL Science 325:1250-1254(2009).
CC -!- FUNCTION: Acts as an actin bundling protein (PubMed:1723709,
CC PubMed:19729655). May have a role in the asymmetric organization and/or
CC movement of cytoplasmic components (PubMed:1723709). It has a role in
CC somatic cells during the formation of adult bristles and hairs, and in
CC the female germline during oogenesis (PubMed:1723709, PubMed:19729655).
CC {ECO:0000269|PubMed:1723709, ECO:0000269|PubMed:19729655}.
CC -!- SUBUNIT: Interacts with Rab35, with stronger binding to the Rab35-GTP
CC form compared to the Rab35-GDP form. {ECO:0000269|PubMed:19729655}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fascin family. {ECO:0000305}.
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DR EMBL; X17549; CAA35585.1; -; Genomic_DNA.
DR EMBL; X17550; CAA35585.1; JOINED; Genomic_DNA.
DR EMBL; AE014298; AAF46307.1; -; Genomic_DNA.
DR RefSeq; NP_001162697.1; NM_001169226.2.
DR RefSeq; NP_511076.3; NM_078521.3.
DR RefSeq; NP_727226.1; NM_167142.3.
DR RefSeq; NP_727227.1; NM_167143.3.
DR AlphaFoldDB; Q24524; -.
DR SMR; Q24524; -.
DR BioGRID; 58189; 8.
DR STRING; 7227.FBpp0290893; -.
DR iPTMnet; Q24524; -.
DR PaxDb; Q24524; -.
DR DNASU; 31717; -.
DR EnsemblMetazoa; FBtr0071101; FBpp0071057; FBgn0003447.
DR EnsemblMetazoa; FBtr0071102; FBpp0071058; FBgn0003447.
DR EnsemblMetazoa; FBtr0301677; FBpp0290891; FBgn0003447.
DR EnsemblMetazoa; FBtr0301679; FBpp0290893; FBgn0003447.
DR GeneID; 31717; -.
DR KEGG; dme:Dmel_CG32858; -.
DR UCSC; CG32858-RA; d. melanogaster.
DR CTD; 31717; -.
DR FlyBase; FBgn0003447; sn.
DR VEuPathDB; VectorBase:FBgn0003447; -.
DR eggNOG; ENOG502QPRX; Eukaryota.
DR GeneTree; ENSGT00950000183157; -.
DR HOGENOM; CLU_030960_2_0_1; -.
DR InParanoid; Q24524; -.
DR OMA; GHETFQL; -.
DR OrthoDB; 1419861at2759; -.
DR PhylomeDB; Q24524; -.
DR BioGRID-ORCS; 31717; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31717; -.
DR PRO; PR:Q24524; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003447; Expressed in wing disc and 57 other tissues.
DR ExpressionAtlas; Q24524; baseline and differential.
DR Genevisible; Q24524; DM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0043005; C:neuron projection; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:FlyBase.
DR GO; GO:0048800; P:antennal morphogenesis; IMP:FlyBase.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
DR GO; GO:0035017; P:cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0016358; P:dendrite development; IMP:FlyBase.
DR GO; GO:0009913; P:epidermal cell differentiation; IMP:FlyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:FlyBase.
DR GO; GO:0046847; P:filopodium assembly; IMP:FlyBase.
DR GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; IMP:FlyBase.
DR GO; GO:0030034; P:microvillar actin bundle assembly; IMP:FlyBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0042060; P:wound healing; IMP:FlyBase.
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 Actin-binding; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Oogenesis; Reference proteome.
FT CHAIN 1..512
FT /note="Protein singed"
FT /id="PRO_0000219387"
SQ SEQUENCE 512 AA; 57279 MW; A021886A9C7B6C48 CRC64;
MNGQGCELGH SNGDIISQNQ QKGWWTIGLI NGQHKYMTAE TFGFKLNANG ASLKKKQLWT
LEPSNTGESI IYLRSHLNKY LSVDQFGNVL CESDERDAGS RFQISISEDG SGRWALKNES
RGYFLGGTPD KLVCTAKTPG ASEFWTVHLA ARPQVNLRSI GRKRFAHLSE SQDEIHVDAN
IPWGEDTLFT LEFRAEEGGR YALHTCNNKY LNANGKLQVV CNEDCLFSAE YHGGHLALRD
RQGQYLSPIG SKAVLKSRSS SVTRDELFSL EDSLPQASFI AGLNLRYVSV KQGVDVTANQ
DEVGENETFQ LEYDWSAHRW ALRTTQDRYW CLSAGGGIQA TGNRRCADAL FELIWHGDGS
LSFRANNGKF LATKRSGHLF ATSESIEEIA KFYFYLINRP ILVLKCEQGF VGYRTPGNLK
LECNKATYET ILVERAQKGL VHLKAHSGKY WRIEGESISV DADAPSDGFF LELREPTRIC
IRSQQGKYLG ATKNGAFKLL DDGTDSATQW EF
