MARS_DROME
ID MARS_DROME Reviewed; 921 AA.
AC Q7K3L1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Guanylate kinase-associated protein mars;
GN Name=mars; Synonyms=gkap; ORFNames=CG17064;
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=15261830; DOI=10.1016/j.modgep.2004.02.006;
RA Bennett D., Alphey L.;
RT "Cloning and expression of mars, a novel member of the guanylate kinase
RT associated protein family in Drosophila.";
RL Gene Expr. Patterns 4:529-535(2004).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=15922738; DOI=10.1016/j.yexcr.2005.03.004;
RA Yang C.-P., Chen M.-S., Liaw G.-J., Chen S.-F., Chou G., Fan S.-S.;
RT "Using Drosophila eye as a model system to characterize the function of
RT mars gene in cell-cycle regulation.";
RL Exp. Cell Res. 307:183-193(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-554, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; THR-51; SER-170; TYR-172;
RP SER-444; THR-519; SER-554; SER-785; SER-792 AND THR-826, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Cell cycle regulator. {ECO:0000269|PubMed:15922738}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15922738};
CC Peripheral membrane protein {ECO:0000269|PubMed:15922738}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:15922738}. Cytoplasm
CC {ECO:0000269|PubMed:15922738}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:15922738}. Note=Localizes to the cell membrane of
CC epithelial cells. Its subcellular localization dynamically changes
CC during cell-cycle progression. At the prophase, it concentrates at the
CC nucleoplasm. In the metaphase cells, it becomes diffusive in the
CC cytoplasm and some is concentrated at the mitotic spindles and spindle
CC poles.
CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system and at
CC different stages of gametogenesis. In embryos, it is expressed in
CC central nervous system and brain. In testis, it is strongly expressed
CC in pre-meiotic germ cells, but is not found in somatic or post-meiotic
CC cells.
CC -!- DEVELOPMENTAL STAGE: Predominantly expressed in embryos and in the
CC adult germline (at protein level). Only present in mitotic cells; at
CC the anaphase and telophase, its begins to degrade.
CC {ECO:0000269|PubMed:15922738}.
CC -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
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DR EMBL; AJ565928; CAD92805.1; -; mRNA.
DR EMBL; AE013599; AAF58367.1; -; Genomic_DNA.
DR EMBL; AY058511; AAL13740.1; -; mRNA.
DR RefSeq; NP_001163142.1; NM_001169671.2.
DR RefSeq; NP_001286387.1; NM_001299458.1.
DR RefSeq; NP_001286388.1; NM_001299459.1.
DR RefSeq; NP_610878.1; NM_137034.4.
DR AlphaFoldDB; Q7K3L1; -.
DR SMR; Q7K3L1; -.
DR BioGRID; 62257; 18.
DR IntAct; Q7K3L1; 22.
DR STRING; 7227.FBpp0290601; -.
DR iPTMnet; Q7K3L1; -.
DR PaxDb; Q7K3L1; -.
DR DNASU; 36498; -.
DR EnsemblMetazoa; FBtr0087668; FBpp0086788; FBgn0033845.
DR EnsemblMetazoa; FBtr0301387; FBpp0290601; FBgn0033845.
DR EnsemblMetazoa; FBtr0344895; FBpp0311206; FBgn0033845.
DR EnsemblMetazoa; FBtr0344896; FBpp0311207; FBgn0033845.
DR GeneID; 36498; -.
DR KEGG; dme:Dmel_CG17064; -.
DR UCSC; CG17064-RA; d. melanogaster.
DR CTD; 36498; -.
DR FlyBase; FBgn0033845; mars.
DR VEuPathDB; VectorBase:FBgn0033845; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT00940000158652; -.
DR HOGENOM; CLU_308428_0_0_1; -.
DR InParanoid; Q7K3L1; -.
DR OMA; NDWLDPD; -.
DR OrthoDB; 1473267at2759; -.
DR PhylomeDB; Q7K3L1; -.
DR Reactome; R-DME-6794361; Neurexins and neuroligins.
DR SignaLink; Q7K3L1; -.
DR BioGRID-ORCS; 36498; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 36498; -.
DR PRO; PR:Q7K3L1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033845; Expressed in germ band (Drosophila) and 59 other tissues.
DR ExpressionAtlas; Q7K3L1; baseline and differential.
DR Genevisible; Q7K3L1; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IDA:FlyBase.
DR GO; GO:0000922; C:spindle pole; IDA:FlyBase.
DR GO; GO:0031616; C:spindle pole centrosome; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IPI:FlyBase.
DR GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
DR GO; GO:0007059; P:chromosome segregation; IGI:FlyBase.
DR GO; GO:0051382; P:kinetochore assembly; IMP:FlyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0023052; P:signaling; IEA:InterPro.
DR GO; GO:0007051; P:spindle organization; IDA:FlyBase.
DR InterPro; IPR005026; SAPAP.
DR PANTHER; PTHR12353; PTHR12353; 1.
DR Pfam; PF03359; GKAP; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..921
FT /note="Guanylate kinase-associated protein mars"
FT /id="PRO_0000372841"
FT REGION 179..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 172
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 519
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 826
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 921 AA; 101946 MW; 0139CBDF715F5346 CRC64;
MQRHKELYKE QSLVLSPRNH CQENRDRLQA ARAKKREDCF YQNRIISVSP TPVKIKQLAA
AQAALTQENV APKLESPERL DTKPAELLKE SNPKVSRQKL YLQRYMEWKI AKTKEHKQQD
QKRRGAAINV PTVKQSKALP KSQTFRVPDN LASAKQKEAA PMFQPPKRCS LYMIANPTGK
GKAAEPIKPS IPKPTSAAAP PSSNTVAASS ALARHKSAAS ATKIVPAIRQ NNNPVALARQ
KAAARPIPNT TKQTTSVRQP GIEAKKITTT IPRPTPATVT KAKTPGIRQQ PPVVSTKPRL
PEPPAPRTAR LPNVLSKPFE KPLGNKAPVT RRANVVKPQP IRGGGGAAAK FKDTAGATSK
AASHSIRMKA TKIKSQYTRL QDNVRKLPQL KAELLHAATL DIPPLTPLDD IHNPFIDQAT
STQCKSNNSS GHLLEAFGDT ILLSPVAPVK AEGESSVKRQ LLPEGKKEAS GPVAKKKFDF
TRYSVANSPA EDSLILDPQQ TTVKEDTGDS TLVPEGTKTP PRRESNGMPN YLSPFVSVSR
GKVNSRCEKE KRNSFYLSNE ESPLEVRRAI ESVLYFRLQL ENEITRLQAL CAEWEAYSKE
NEARLQETGG IDMINVTIGQ TRLLTTKKMM QFSGLIDRCE AGATGKNSQP NDGSEDSKPV
QAEDLEGWWD MLRLQSENVD KRFDNLKRWK ANDWLDPDAV AEEPKQPKPK PKISRNMKIK
SKAKPSSNLQ QFLRKAHANM KKTKVEEPTL EDGLPATSSR HSSPRVIVVR NRRSFSPART
VLRMSTGEGR QSIAPNALLK SAILAAAEQN AAKTPPPKPR TSILKTPGTT KRQNRGVLFS
AKKSVRRFQF TYEEGNISND ETVGADKLED CEEDMSLEAS TESGSLEQNP GRDSNQENEA
TPRTYTLRNR RVNLRPSSEF M
