MPND_DROME
ID MPND_DROME Reviewed; 1412 AA.
AC Q9VKJ1;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=MPN domain-containing protein CG4751;
DE EC=3.4.-.-;
GN ORFNames=CG4751;
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-699; SER-701; SER-705;
RP SER-719; SER-723; SER-728; SER-1288; SER-1290 AND THR-1297, AND
RP IDENTIFICATION 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: Probable protease. {ECO:0000250}.
CC -!- DOMAIN: The JAMM motif may mediate the protease activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67 family. {ECO:0000305}.
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DR EMBL; AE014134; AAF53077.1; -; Genomic_DNA.
DR EMBL; AY051978; AAK93402.1; -; mRNA.
DR RefSeq; NP_609495.1; NM_135651.3.
DR AlphaFoldDB; Q9VKJ1; -.
DR BioGRID; 60613; 3.
DR IntAct; Q9VKJ1; 9.
DR STRING; 7227.FBpp0079789; -.
DR iPTMnet; Q9VKJ1; -.
DR PaxDb; Q9VKJ1; -.
DR PRIDE; Q9VKJ1; -.
DR DNASU; 34551; -.
DR EnsemblMetazoa; FBtr0080200; FBpp0079789; FBgn0032348.
DR GeneID; 34551; -.
DR KEGG; dme:Dmel_CG4751; -.
DR UCSC; CG4751-RA; d. melanogaster.
DR FlyBase; FBgn0032348; CG4751.
DR VEuPathDB; VectorBase:FBgn0032348; -.
DR eggNOG; KOG1555; Eukaryota.
DR HOGENOM; CLU_005253_0_0_1; -.
DR InParanoid; Q9VKJ1; -.
DR OMA; MMKPPKS; -.
DR OrthoDB; 183341at2759; -.
DR PhylomeDB; Q9VKJ1; -.
DR Reactome; R-DME-3214858; RMTs methylate histone arginines.
DR Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR BioGRID-ORCS; 34551; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34551; -.
DR PRO; PR:Q9VKJ1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032348; Expressed in eye disc (Drosophila) and 26 other tissues.
DR Genevisible; Q9VKJ1; DM.
DR GO; GO:0016514; C:SWI/SNF complex; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR040843; RAMA.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF18755; RAMA; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..1412
FT /note="MPN domain-containing protein CG4751"
FT /id="PRO_0000278807"
FT DOMAIN 113..219
FT /note="RAMA"
FT /evidence="ECO:0000255"
FT DOMAIN 284..420
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 572..600
FT /evidence="ECO:0000255"
FT COMPBIAS 100..115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1297
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 1412 AA; 149953 MW; 00BE0AD3F87862F0 CRC64;
MENGVEHGVD ESGENQVLSS SDGEGDCDGD GEVEGEVLQP PPPPPLQITN DCVGEGVQAE
EGERAPATTG AVDVTPDPGP PPTDGAAPVA ILEDNMCDKD VDSDAGDEDN DDETKENYEG
FNGTGRTVTL QTLMAANVLQ PGLGLMTIEY LGQKFVGDLL ADGKIKSHET ETIFLTPSAW
AMHCKRIINP DKKSGCGWAS VKYKGKKLDA YKNTYLRKCA LQKETPLDDC ELDAERKTDT
PEIVVKRTVF AHNTVSNRNV VHDANMLIES VPFTSVGKLQ PFLITVNSSA LLLADFHCHL
TVREVCGYLG GTWDMNTHTL SITKTYPCRS TRFDRQRAGE VERDIQKMMI QDQLLLVGWY
HSHPKFQAEP TLRDCDAQLD YQIKMRGASD LTYTPCVSLI ISPYYDENPT LESVVKCIWI
VPPNENRQSM EYGRPMLMQY SVLPDKEIPE EVRSEIQLCV DYYSQYRSEM VKFRNIYNND
VTYNEKLKNT LYPKFPSKQS DKALWNWICA VLDCEQEDDF IPPKTIKIID NDDLEVKEED
KPVVLMDLSG DVKINPPKEE QFSEAMGGLE DSGRKAEEES NAQAEQKASE LKVMSLQEQL
CMPSGLNMNP VRMLSPLATP NPTSLPPVLP NLGAPVLPAT PSQLLPPQVP AVTAPPAITP
AVTTSALTSA LNASPRDSPI TIQSNSASPA KFEVPVRASP SPAKSDTSSH ASTSRTRNSP
APSPGKFSVS DIARNSPSIT PNKYEAAAAA LVPPAAACLP TANDLMAASL AQLAGQLPPN
FLQGDLAALF QQQRKDYGSS SLNQLAAAAA KVGGSKQSNA SASSGLNDPN VAAAVAAYSN
SFNMPLPTGV GIGGSGNSNA HSSSKSKSER SSKSSSSSSS SNSSSTSNSY KTKLMKELDE
LKNDPLKMSE LIRSPEYAAL LLQQAEALGA TTLGTLGFGS DYSYLTGAGL GVPAANALTG
GQSSNSSSSK SSKSSPAAAA AAALSADYNN LIQASKLLGY DSYMQQSKQS NDLNAFLQQQ
MAVAAASIPP PPQTASSGSS NSSSSKKQQQ LQQQQHQQQQ QQQQQQAAAQ ADYTALLQTY
TKLFDPNNQF AAAMSSNKHM AGAHNELSAL LSSGVGVGGG ASGGGSKQKQ KDIQSDMLNQ
LLQLEKQDSE IKALLYRQNK AAADLDALFA TPSGAVVGAG SSANAMKSGS SAGNSGVSGM
SSPSSLSNQA AYYNALAQEK MQDYAAFFQQ QHGKYGIPDP LSKTTLAANN MFMTPSALFK
IQQESLSAMM MKPPKSTTPS SARTRESSAS PALERLTPTK SASSGGSGGG GSNSNSGGKY
NFSAVDLAIS SVPSNTPSPA PSDGSSGSSH RRPSPDIGRL YGELAPPGAL LGSGGVPKKR
MEFASVADLA APPPAKMPKN NMGDDILNLS HD
