ID E1JGN0_DROME Unreviewed; 1141 AA. AC E1JGN0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 02-JUN-2021, entry version 91. DE RecName: Full=Non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN Name=par-1 {ECO:0000313|EMBL:ACZ94480.1, GN ECO:0000313|FlyBase:FBgn0260934}; GN Synonyms=27C1 {ECO:0000313|EMBL:ACZ94480.1}, anon-WO0210402.19 GN {ECO:0000313|EMBL:ACZ94480.1}, BcDNA:RH48823 GN {ECO:0000313|EMBL:ACZ94480.1}, CG11960 {ECO:0000313|EMBL:ACZ94480.1}, GN CG16701 {ECO:0000313|EMBL:ACZ94480.1}, CG30131 GN {ECO:0000313|EMBL:ACZ94480.1}, CG30132 {ECO:0000313|EMBL:ACZ94480.1}, GN dMARK {ECO:0000313|EMBL:ACZ94480.1}, Dmel\CG8201 GN {ECO:0000313|EMBL:ACZ94480.1}, DPAR-1 {ECO:0000313|EMBL:ACZ94480.1}, GN dPAR-1 {ECO:0000313|EMBL:ACZ94480.1}, dPar-1 GN {ECO:0000313|EMBL:ACZ94480.1}, DPar1 {ECO:0000313|EMBL:ACZ94480.1}, GN dPAR1 {ECO:0000313|EMBL:ACZ94480.1}, dPar1 GN {ECO:0000313|EMBL:ACZ94480.1}, EMK {ECO:0000313|EMBL:ACZ94480.1}, GN l(2)27C1 {ECO:0000313|EMBL:ACZ94480.1}, l(2)k06323 GN {ECO:0000313|EMBL:ACZ94480.1}, MARK {ECO:0000313|EMBL:ACZ94480.1}, GN PAR-1 {ECO:0000313|EMBL:ACZ94480.1}, Par-1 GN {ECO:0000313|EMBL:ACZ94480.1}, PAR1 {ECO:0000313|EMBL:ACZ94480.1}, GN Par1 {ECO:0000313|EMBL:ACZ94480.1}, par1 GN {ECO:0000313|EMBL:ACZ94480.1}; GN ORFNames=CG8201 {ECO:0000313|EMBL:ACZ94480.1, GN ECO:0000313|FlyBase:FBgn0260934}, Dmel_CG8201 GN {ECO:0000313|EMBL:ACZ94480.1}; 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 {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., 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., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L., RA Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., RA 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] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [8] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). 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:0000256|ARBA:ARBA00001433}; 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:0000256|ARBA:ARBA00000775}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}. 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; AE013599; ACZ94480.1; -; Genomic_DNA. DR RefSeq; NP_001163208.1; NM_001169737.2. DR SMR; E1JGN0; -. DR STRING; 7227.FBpp0290718; -. DR PRIDE; E1JGN0; -. DR DNASU; 2768852; -. DR EnsemblMetazoa; FBtr0301503; FBpp0290718; FBgn0260934. DR GeneID; 2768852; -. DR CTD; 2768852; -. DR FlyBase; FBgn0260934; par-1. DR eggNOG; KOG0586; Eukaryota. DR HOGENOM; CLU_000288_157_0_1; -. DR InParanoid; E1JGN0; -. DR SignaLink; E1JGN0; -. DR BioGRID-ORCS; 2768852; 0 hits in 3 CRISPR screens. DR ChiTaRS; par-1; fly. DR GenomeRNAi; 2768852; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0260934; Expressed in central nervous system and 40 other tissues. DR ExpressionAtlas; E1JGN0; baseline and differential. DR Genevisible; E1JGN0; DM. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase. DR GO; GO:0005938; C:cell cortex; IDA:FlyBase. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0045169; C:fusome; IDA:FlyBase. DR GO; GO:0045172; C:germline ring canal; IDA:FlyBase. DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase. DR GO; GO:0061174; C:type I terminal bouton; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase. DR GO; GO:0106311; F:protein threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0050321; F:tau-protein kinase activity; IDA:FlyBase. DR GO; GO:0009798; P:axis specification; IMP:FlyBase. DR GO; GO:0030709; P:border follicle cell delamination; IMP:FlyBase. DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase. DR GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase. DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:FlyBase. DR GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; IMP:FlyBase. DR GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IMP:FlyBase. DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase. DR GO; GO:0045451; P:pole plasm oskar mRNA localization; TAS:FlyBase. DR GO; GO:0007318; P:pole plasm protein localization; IMP:FlyBase. DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase. DR GO; GO:0030860; P:regulation of polarized epithelial cell differentiation; IMP:FlyBase. DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase. DR GO; GO:0051124; P:synaptic growth at neuromuscular junction; IMP:FlyBase. DR InterPro; IPR028375; KA1/Ssp2_C. DR InterPro; IPR001772; KA1_dom. 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 InterPro; IPR015940; UBA. DR Pfam; PF02149; KA1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00165; UBA; 1. DR SUPFAM; SSF103243; SSF103243; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50032; KA1; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50030; UBA; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Proteomics identification {ECO:0007829|PeptideAtlas:E1JGN0}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Transferase {ECO:0000313|EMBL:ACZ94480.1}. FT DOMAIN 481..732 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 751..793 FT /note="UBA" FT /evidence="ECO:0000259|PROSITE:PS50030" FT DOMAIN 1092..1141 FT /note="KA1" FT /evidence="ECO:0000259|PROSITE:PS50032" FT REGION 1..131 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 279..329 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 359..439 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 796..861 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 920..969 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 38..62 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 63..97 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 300..329 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 363..381 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 404..418 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 802..853 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 510 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 1141 AA; 124626 MW; 0798140BE6A3764F CRC64; MEATTTTTPD LNRGDATRKS VRLYAARKGA APAPPKLSVA PSSNQNSNHS SNNNNSSSNL PETEKEMELR QTHLANKDLD GATEDDSIVE LRRRDAQATP LPRIAVSALP TLQPHPTPKE RQKPPMPRLL STEDDAGVSF ALGSIEKHIH NVEESFKQQQ QNQQSQSSMD VMKLEIKRKQ SKRYGETENL LRPGISDMSS ENDFQYLGGR RAGELDDSNE LMLSEFQRGS DGRNSIGAYS KNSAAAANGA NAVKAKLART ASDTKNNDTV LAMRATFKQK QHLQDEKQPA VWRPAGTGPT PAARSSSSTT STSGSASRGG SSSSVVDGVA PSKLTATTIS ASKRREENLR QFEALLAQKS SHRHGASGAS GTGSNAASSK RRSDRPIVAP IPPYNSSRAE HVTSSTRHSV DPRSHSGHES RSGTASTHPP VGHHPTSRVP SVVANRSNVY SNNAAQGSPN MQMRSSAPMR WRATEEHIGK YKLIKTIGKG NFAKVKLAKH LPTGKEVAIK IIDKTQLNPG SLQKLFREVR IMKMLDHPNI VKLFQVIETE KTLYLIMEYA SGGEVFDYLV LHGRMKEKEA RVKFRQIVSA VQYCHQKRII HRDLKAENLL LDSELNIKIA DFGFSNEFTP GSKLDTFCGS PPYAAPELFQ GKKYDGPEVD VWSLGVILYT LVSGSLPFDG STLRELRERV LRGKYRIPFY MSTDCENLLR KFLVLNPAKR ASLETIMGDK WMNMGFEEDE LKPYIEPKAD LADPKRIGKT EALVAMGYNR SEIEASLSQV RYDDVFATYL LLGRKSTDPE SDGSRSGSSL SLRNISGNDA GANAGSASVQ SPTHRGVHRS ISASSTKPSR RASSGAETLR VGPTNAAATV AAATGAVGAV NPSNNYNAAG SAADRASVGS NFKRQNTIDS ATIKENTARL AAQNQRPASA TQKMLTTADT TLNSPAKPRT ATKYDPTNGN RTVSGTSGII PRRSTTLYEK TSSTEKTNVI PAETKARNNT ALEYSGTSGA SGDSSHPGRM SFFSKLSSRF SKRPTIADEA AKPRVLRFTW SMKTTSPLMP DQIMQKIREV LDQNNCDYEQ RERFVLWCVH GDPNTDSLVQ WEIEVCKLPR LSLNGVRFKR ISGTSIGFKN IASRIAFDLK L //