TPPP_DROME
ID TPPP_DROME Reviewed; 192 AA.
AC Q9VV43;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Tubulin polymerization-promoting protein homolog {ECO:0000250|UniProtKB:O94811};
DE Short=TPPP {ECO:0000250|UniProtKB:O94811};
DE AltName: Full=Protein ringmaker {ECO:0000303|PubMed:27422099};
GN Name=ringer {ECO:0000303|PubMed:27422099, ECO:0000312|FlyBase:FBgn0266417};
GN ORFNames=CG45057 {ECO:0000312|FlyBase:FBgn0266417};
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=27422099; DOI=10.1242/jcs.187294;
RA Mino R.E., Rogers S.L., Risinger A.L., Rohena C., Banerjee S., Bhat M.A.;
RT "Drosophila Ringmaker regulates microtubule stabilization and axonal
RT extension during embryonic development.";
RL J. Cell Sci. 129:3282-3294(2016).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=31156389; DOI=10.3389/fncel.2019.00192;
RA Shi Q., Lin Y.Q., Saliba A., Xie J., Neely G.G., Banerjee S.;
RT "Tubulin polymerization promoting protein, ringmaker, and MAP1B homolog
RT futsch coordinate microtubule organization and synaptic growth.";
RL Front. Cell. Neurosci. 13:192-192(2019).
CC -!- FUNCTION: Regulator of microtubule required for axonal extension during
CC embryonic development (PubMed:27422099). Promotes microtubule bundling
CC and polymerization (PubMed:27422099). Together with futsch, required
CC for neuromuscular junction (NMJ) bouton growth by regulating synaptic
CC microtubules (PubMed:31156389). {ECO:0000269|PubMed:27422099,
CC ECO:0000269|PubMed:31156389}.
CC -!- SUBUNIT: Found in a complex with tubulin and Futsch.
CC {ECO:0000269|PubMed:31156389}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:31156389}. Cell projection, axon
CC {ECO:0000269|PubMed:27422099}. Presynapse
CC {ECO:0000269|PubMed:31156389}. Note=Localizes at the presynaptic
CC neuromuscular junction (NMJ). {ECO:0000269|PubMed:31156389}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adult head (at protein level).
CC {ECO:0000269|PubMed:27422099}.
CC -!- DEVELOPMENTAL STAGE: Mainly expressed in neurons and later in midline
CC glia during ventral nerve cord (VNC) development (at protein level).
CC {ECO:0000269|PubMed:27422099}.
CC -!- DISRUPTION PHENOTYPE: Embryonic nervous system defects characterized by
CC cell misplacement and errors in axonal extension and targeting
CC (PubMed:27422099). Neurons display defective axonal extension
CC (PubMed:27422099). Defects are probably caused by impaired microtubule
CC organization and integrity (PubMed:27422099). During larval
CC neuromuscular junction (NMJ) synaptic development, larvae show reduced
CC synaptic growth and transmission (PubMed:31156389). Flies lacking both
CC Ringer and Futsch display a significant reduction in microtubule loops
CC at the neuromuscular junctions (NMJ) and reduced acetylated-tubulin
CC levels (PubMed:31156389). {ECO:0000269|PubMed:27422099,
CC ECO:0000269|PubMed:31156389}.
CC -!- SIMILARITY: Belongs to the TPPP family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49479.1; -; Genomic_DNA.
DR EMBL; AY071493; AAL49115.1; -; mRNA.
DR EMBL; AY071358; AAL48980.1; -; mRNA.
DR RefSeq; NP_001246792.1; NM_001259863.2.
DR RefSeq; NP_001261938.1; NM_001275009.1.
DR RefSeq; NP_001261939.1; NM_001275010.1.
DR RefSeq; NP_648881.1; NM_140624.3.
DR AlphaFoldDB; Q9VV43; -.
DR SMR; Q9VV43; -.
DR BioGRID; 65120; 13.
DR DIP; DIP-18084N; -.
DR STRING; 7227.FBpp0075183; -.
DR PaxDb; Q9VV43; -.
DR PRIDE; Q9VV43; -.
DR EnsemblMetazoa; FBtr0344398; FBpp0310766; FBgn0266417.
DR EnsemblMetazoa; FBtr0344399; FBpp0310767; FBgn0266417.
DR EnsemblMetazoa; FBtr0344400; FBpp0310768; FBgn0266417.
DR EnsemblMetazoa; FBtr0344401; FBpp0310769; FBgn0266417.
DR GeneID; 39813; -.
DR KEGG; dme:Dmel_CG45057; -.
DR UCSC; CG4893-RA; d. melanogaster.
DR CTD; 39813; -.
DR FlyBase; FBgn0266417; ringer.
DR VEuPathDB; VectorBase:FBgn0266417; -.
DR eggNOG; KOG4070; Eukaryota.
DR GeneTree; ENSGT00940000153875; -.
DR HOGENOM; CLU_091734_1_0_1; -.
DR InParanoid; Q9VV43; -.
DR OMA; PKASGHE; -.
DR OrthoDB; 1317210at2759; -.
DR PhylomeDB; Q9VV43; -.
DR BioGRID-ORCS; 39813; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39813; -.
DR PRO; PR:Q9VV43; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0266417; Expressed in oviduct (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q9VV43; baseline and differential.
DR Genevisible; Q9VV43; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; IMP:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:FlyBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; IDA:FlyBase.
DR GO; GO:0032273; P:positive regulation of protein polymerization; IBA:GO_Central.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR008907; P25-alpha.
DR PANTHER; PTHR12932; PTHR12932; 1.
DR Pfam; PF05517; p25-alpha; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Cytoskeleton; Reference proteome; Synapse.
FT CHAIN 1..192
FT /note="Tubulin polymerization-promoting protein homolog"
FT /id="PRO_0000221141"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 192 AA; 20596 MW; 95654DBB481A3E50 CRC64;
MSEVAAANGS PSPAPTPEVP ATELAQLALE DEPKVSFSDQ FKAFSKFGDS KSDGKLITLS
QSDKWMKQAK VIDKKITTTD TGIHFKKFKA MKISLSDYNK FLDDLAKTKK VELSEIKQKL
ASCGAPGVVS VSAGKAAAAV DRLTDTSKYT GSHKERFDAS GKGKGIAGRR NVVDGSGYVS
GYQHKDTYDN AH
