TRC_DROPS
ID TRC_DROPS Reviewed; 458 AA.
AC Q2LZZ7;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Serine/threonine-protein kinase tricornered {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9NBK5};
DE AltName: Full=NDR protein kinase;
DE AltName: Full=Serine/threonine-protein kinase 38-like;
DE AltName: Full=Serine/threonine-protein kinase tricorner {ECO:0000305};
GN Name=trc {ECO:0000250|UniProtKB:Q9NBK5}; ORFNames=GA21227;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in controlling cell
CC structure and proliferation of a variety of polarized outgrowths
CC including epidermal hairs, bristles, arista laterals, and dendrites.
CC Together with fry, maintains the integrity of epidermal hairs and is an
CC essential component of the signaling pathway regulating dendritic
CC branching of sensory neurons. Reduces neurite outgrowth by
CC phosphorylating pav/pavarotti, thereby inhibiting its function in
CC microtubule-microtubule sliding. {ECO:0000250|UniProtKB:Q9NBK5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q9NBK5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9NBK5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9NBK5};
CC -!- SUBUNIT: Interacts with, and is activated by, Mob1.
CC {ECO:0000250|UniProtKB:Q9NBK5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NBK5}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NBK5}. Note=Trc colocalizes with Mob1 to the
CC cell periphery in wing cells and wing hairs.
CC {ECO:0000250|UniProtKB:Q9NBK5}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL31140.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH379069; EAL31140.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001353626.3; XM_001353590.3.
DR AlphaFoldDB; Q2LZZ7; -.
DR SMR; Q2LZZ7; -.
DR STRING; 7237.FBpp0274389; -.
DR EnsemblMetazoa; FBtr0275951; FBpp0274389; FBgn0081215.
DR GeneID; 4813412; -.
DR KEGG; dpo:Dpse_GA21227; -.
DR eggNOG; KOG0605; Eukaryota.
DR InParanoid; Q2LZZ7; -.
DR PhylomeDB; Q2LZZ7; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0081215; Expressed in insect adult head and 2 other tissues.
DR GO; GO:0030424; C:axon; IEA:EnsemblMetazoa.
DR GO; GO:0044297; C:cell body; IEA:EnsemblMetazoa.
DR GO; GO:0005938; C:cell cortex; IEA:EnsemblMetazoa.
DR GO; GO:0070451; C:cell hair; IEA:EnsemblMetazoa.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0048800; P:antennal morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0022416; P:chaeta development; IEA:EnsemblMetazoa.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0070593; P:dendrite self-avoidance; IEA:EnsemblMetazoa.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; IEA:EnsemblMetazoa.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0051012; P:microtubule sliding; ISS:UniProtKB.
DR GO; GO:0150013; P:negative regulation of neuron projection arborization; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0050773; P:regulation of dendrite development; ISS:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..458
FT /note="Serine/threonine-protein kinase tricornered"
FT /id="PRO_0000279718"
FT DOMAIN 92..389
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 390..458
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 118..179
FT /note="Interaction with mats and Mob1"
FT /evidence="ECO:0000250|UniProtKB:Q9NBK5"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 98..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NBK5"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NBK5"
SQ SEQUENCE 458 AA; 52935 MW; F89062F77098B518 CRC64;
MMSSRTDTDG SSIRFSDHTL DKATKAKVTL ENYYSNLVTQ YGERKQRLAK LEAQLKDESL
TESQRQEKRL QHAQKETEYL RLKRLRLGVE DFEALKVIGR GAFGEVRLVQ KKDTGHVYAM
KVLRKADMLE KEQVAHVRAE RDVLVEADHQ WVVKMYYSFQ DQVNLYLIME FLPGGDMMTL
LMKKDTLSEE GTQFYISETA LAIDSIHKLG FIHRDIKPDN LLLDARGHLK LSDFGLCTGL
KKSHRTDFYR DLSQAKPSDF IGTCASPMDS KRRAESWKRN RRALAYSTVG TPDYIAPEVF
LQTGYGPACD WWSLGVIMYE MLMGYPPFCS DNPQDTYRKV MNWRETLIFP PEIPISEEAK
ETIIKFCCEA DRRLGSQRGL EDLKSVPFFR GVDWEHIRER PAAIPVEVRS IDDTSNFDEF
PDVSLEIPSA PIPQGGEIAK DWVFINYTYK RFEVRNLE
