PROF_DROME
ID PROF_DROME Reviewed; 126 AA.
AC P25843; Q3YMV6; Q9VMJ9;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Profilin;
DE AltName: Full=Protein chickadee;
GN Name=chic; Synonyms=chi; ORFNames=CG9553;
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 [MRNA].
RX PubMed=1339308; DOI=10.1016/0092-8674(92)90128-y;
RA Cooley L., Verheyen E., Caverly K.;
RT "Chickadee encodes a profilin required for intercellular cytoplasm
RT transport during Drosophila oogenesis.";
RL Cell 69:173-184(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Head;
RX PubMed=15917496; DOI=10.1093/molbev/msi175;
RA Jagadeeshan S., Singh R.S.;
RT "Rapidly evolving genes of Drosophila: differing levels of selective
RT pressure in testis, ovary, and head tissues between sibling species.";
RL Mol. Biol. Evol. 22:1793-1801(2005).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Binds to actin and affects the structure of the cytoskeleton.
CC At high concentrations, profilin prevents the polymerization of actin,
CC whereas it enhances it at low concentrations. By binding to PIP2, it
CC inhibits the formation of IP3 and DG. This profilin is required for
CC intercellular cytoplasm transport during Drosophila oogenesis.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio.
CC -!- INTERACTION:
CC P25843; Q24306: Diap1; NbExp=2; IntAct=EBI-156199, EBI-456419;
CC P25843; Q8T4F7: ena; NbExp=3; IntAct=EBI-156199, EBI-466810;
CC P25843; P40792: Rac1; NbExp=3; IntAct=EBI-156199, EBI-74845;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Expressed in ovary and head.
CC {ECO:0000269|PubMed:15917496}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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; M84528; AAA28418.1; -; mRNA.
DR EMBL; M84529; AAA28419.1; -; mRNA.
DR EMBL; DQ062770; AAY56643.1; -; mRNA.
DR EMBL; AE014134; AAF52315.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52316.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10565.1; -; Genomic_DNA.
DR EMBL; AE014134; AAS64643.1; -; Genomic_DNA.
DR EMBL; AY069444; AAL39589.1; -; mRNA.
DR EMBL; AY128443; AAM75036.1; -; mRNA.
DR PIR; A38154; A38154.
DR RefSeq; NP_001245905.1; NM_001258976.2.
DR RefSeq; NP_001245906.1; NM_001258977.2.
DR RefSeq; NP_477016.1; NM_057668.6.
DR RefSeq; NP_599131.1; NM_134304.3.
DR RefSeq; NP_723136.1; NM_164667.2.
DR RefSeq; NP_995635.1; NM_205913.3.
DR AlphaFoldDB; P25843; -.
DR SMR; P25843; -.
DR BioGRID; 59999; 72.
DR DIP; DIP-22165N; -.
DR IntAct; P25843; 6.
DR STRING; 7227.FBpp0089196; -.
DR PaxDb; P25843; -.
DR PRIDE; P25843; -.
DR DNASU; 33834; -.
DR EnsemblMetazoa; FBtr0079233; FBpp0078864; FBgn0000308.
DR EnsemblMetazoa; FBtr0079234; FBpp0078865; FBgn0000308.
DR EnsemblMetazoa; FBtr0079235; FBpp0078866; FBgn0000308.
DR EnsemblMetazoa; FBtr0079236; FBpp0089196; FBgn0000308.
DR EnsemblMetazoa; FBtr0309212; FBpp0301151; FBgn0000308.
DR EnsemblMetazoa; FBtr0309213; FBpp0301152; FBgn0000308.
DR GeneID; 33834; -.
DR KEGG; dme:Dmel_CG9553; -.
DR UCSC; CG9553-RA; d. melanogaster.
DR CTD; 33834; -.
DR FlyBase; FBgn0000308; chic.
DR VEuPathDB; VectorBase:FBgn0000308; -.
DR eggNOG; KOG1755; Eukaryota.
DR GeneTree; ENSGT00730000112841; -.
DR HOGENOM; CLU_120772_1_1_1; -.
DR InParanoid; P25843; -.
DR OMA; WAQSSGF; -.
DR OrthoDB; 1428600at2759; -.
DR PhylomeDB; P25843; -.
DR SignaLink; P25843; -.
DR BioGRID-ORCS; 33834; 1 hit in 1 CRISPR screen.
DR ChiTaRS; chic; fly.
DR GenomeRNAi; 33834; -.
DR PRO; PR:P25843; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000308; Expressed in embryonic/larval hemocyte (Drosophila) and 26 other tissues.
DR ExpressionAtlas; P25843; baseline and differential.
DR Genevisible; P25843; DM.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0030041; P:actin filament polymerization; TAS:FlyBase.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; TAS:FlyBase.
DR GO; GO:0007420; P:brain development; IMP:FlyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; TAS:FlyBase.
DR GO; GO:0007488; P:histoblast morphogenesis; IMP:FlyBase.
DR GO; GO:0035193; P:larval central nervous system remodeling; IGI:FlyBase.
DR GO; GO:0007436; P:larval salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0032507; P:maintenance of protein location in cell; IMP:FlyBase.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0007300; P:ovarian nurse cell to oocyte transport; HMP:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; TAS:FlyBase.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IMP:CACAO.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IMP:FlyBase.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0042989; P:sequestering of actin monomers; IBA:GO_Central.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0042060; P:wound healing; IMP:FlyBase.
DR CDD; cd00148; PROF; 1.
DR InterPro; IPR005455; PFN.
DR InterPro; IPR036140; PFN_sf.
DR InterPro; IPR027310; Profilin_CS.
DR PANTHER; PTHR11604; PTHR11604; 1.
DR Pfam; PF00235; Profilin; 1.
DR PRINTS; PR00392; PROFILIN.
DR PRINTS; PR01640; PROFILINPLNT.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
DR PROSITE; PS00414; PROFILIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..126
FT /note="Profilin"
FT /id="PRO_0000199597"
SQ SEQUENCE 126 AA; 13723 MW; 6E2942C12A81ADEA CRC64;
MSWQDYVDNQ LLASQCVTKA CIAGHDGNIW AQSSGFEVTK EELSKLISGF DQQDGLTSNG
VTLAGQRYIY LSGTDRVVRA KLGRSGVHCM KTTQAVIVSI YEDPVQPQQA ASVVEKLGDY
LITCGY
