CT2NL_DROME
ID CT2NL_DROME Reviewed; 609 AA.
AC Q8SX68; A0A0B4LFS3; Q9V8D0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=CTTNBP2 N-terminal-like protein {ECO:0000305};
DE AltName: Full=Protein Nausicaa {ECO:0000303|PubMed:31164339};
GN Name=Naus {ECO:0000303|PubMed:31164339, ECO:0000312|FlyBase:FBgn0034308};
GN ORFNames=CG10915 {ECO:0000312|FlyBase:FBgn0034308};
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 [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 [2]
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 [3]
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 564-PRO--PRO-568.
RX PubMed=31164339; DOI=10.1242/bio.038232;
RA O'Connell M.E., Sridharan D., Driscoll T., Krishnamurthy I., Perry W.G.,
RA Applewhite D.A.;
RT "The Drosophila protein, Nausicaa, regulates lamellipodial actin dynamics
RT in a Cortactin-dependent manner.";
RL Biol. Open 8:0-0(2019).
CC -!- FUNCTION: Regulates lamellipodial actin dynamics in a Cortactin-
CC dependent manner and is therefore likely involved in controlling actin
CC branch density, actin-retrograde flow rates and lamellipodial
CC protrusion. Functions by slowing the dissociation of Cortactin from
CC Arp2/3 nucleated branches thereby increasing branch nucleation and
CC junction stability. {ECO:0000269|PubMed:31164339}.
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000269|PubMed:31164339}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:31164339}. Note=Localization to the lamellipodia is
CC dependent on Cortactin. {ECO:0000269|PubMed:31164339}.
CC -!- MISCELLANEOUS: Named 'Nausicaa' after the princess in Homer's 'The
CC Odyssey' who helps to ensure Odysseus' safe passage home from Phaeacia.
CC {ECO:0000303|PubMed:31164339}.
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DR EMBL; AE013599; AAF57737.2; -; Genomic_DNA.
DR EMBL; AE013599; AHN56360.1; -; Genomic_DNA.
DR EMBL; AY094820; AAM11173.1; -; mRNA.
DR RefSeq; NP_001286565.1; NM_001299636.1.
DR RefSeq; NP_611299.2; NM_137455.5.
DR AlphaFoldDB; Q8SX68; -.
DR SMR; Q8SX68; -.
DR BioGRID; 62758; 3.
DR STRING; 7227.FBpp0085925; -.
DR iPTMnet; Q8SX68; -.
DR PaxDb; Q8SX68; -.
DR PRIDE; Q8SX68; -.
DR DNASU; 37076; -.
DR EnsemblMetazoa; FBtr0086746; FBpp0085925; FBgn0034308.
DR EnsemblMetazoa; FBtr0345416; FBpp0311543; FBgn0034308.
DR GeneID; 37076; -.
DR KEGG; dme:Dmel_CG10915; -.
DR UCSC; CG10915-RA; d. melanogaster.
DR CTD; 37076; -.
DR FlyBase; FBgn0034308; Naus.
DR VEuPathDB; VectorBase:FBgn0034308; -.
DR eggNOG; KOG1103; Eukaryota.
DR GeneTree; ENSGT00950000182852; -.
DR HOGENOM; CLU_019330_0_0_1; -.
DR InParanoid; Q8SX68; -.
DR OMA; SPAKMQP; -.
DR OrthoDB; 765473at2759; -.
DR PhylomeDB; Q8SX68; -.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR BioGRID-ORCS; 37076; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37076; -.
DR PRO; PR:Q8SX68; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034308; Expressed in cleaving embryo and 21 other tissues.
DR Genevisible; Q8SX68; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IDA:FlyBase.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0061573; P:actin filament bundle retrograde transport; IMP:UniProtKB.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IMP:UniProtKB.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; IMP:UniProtKB.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; IMP:UniProtKB.
DR GO; GO:1903119; P:protein localization to actin cytoskeleton; IMP:UniProtKB.
DR InterPro; IPR019131; Cortactin-binding_p2_N.
DR Pfam; PF09727; CortBP2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..609
FT /note="CTTNBP2 N-terminal-like protein"
FT /id="PRO_0000372638"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 182..264
FT /evidence="ECO:0000255"
FT COILED 303..370
FT /evidence="ECO:0000255"
FT COMPBIAS 556..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MUTAGEN 564..568
FT /note="PPPIP->AAAIA: Reduced localization to the
FT lamellipodia, likely resulting from decreased interaction
FT with Cortactin."
FT /evidence="ECO:0000269|PubMed:31164339"
SQ SEQUENCE 609 AA; 65422 MW; 480A18A76ADA7A25 CRC64;
MEQNSNSSVA DTFAEAPATD ADYGTENCSG SGMSVGDTVS ANHEFQTMKP GPGVVHKVMP
VANSASSATA TNGRTRSEMP HSELVKMLYY LEGELQARDV CIAALRNERV KQLIAQLRTK
RLQPNDPYAA IFRDKIALNG NLISRESSTQ AAQAEMEVRQ IIEQQMEQQY QMVSKQRATH
VRMVNILTES LENNQRMLQE LEEEKRKHEN TTAQGDDITY GLELERNKLK QDLEEERAQV
AKMEKDLKKL QETLEYERNR QKQIVLLLIA ERKKILMKYI EEGKRSEDLA QILAEEKQRS
DTIAEGLEEE SKKSLRMEEE LEKQTHAMEQ ERKVLFAKLA KEELRVKELE QELNALRSEH
EALKKQQQLG GSGSSVAAAK ARQFSDDACA TPPMVNIAKI VQPTATVSSM PVSGPQTGIA
RSIAPGQNIR SAGIATAPTG TATAAIAPLT AVLNHTTTIT TTTNNTTTSS NSNSSGSIGV
AATAAAVAAS VETAATVTVP MVAPPSPSPA KMQPTATIQR APGGKYAALA AAAALDQTTT
PHPHPVPIAV PPVTVPPAGA RGAPPPIPTK PIVPPKREPS LSRLGSITGS SAIAAATAAT
TAAGTAKQN
