PREP_DROME
ID PREP_DROME Reviewed; 1034 AA.
AC Q9V9E3; A4UZ44; B7YZR1; Q0E9P8;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Presequence protease, mitochondrial;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN ORFNames=CG3107;
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).
CC -!- FUNCTION: ATP-independent protease that degrades mitochondrial transit
CC peptides after their cleavage. Also degrades other unstructured
CC peptides (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000305}.
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DR EMBL; AE013599; AAF57348.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68370.1; -; Genomic_DNA.
DR EMBL; AE013599; ABI31021.1; -; Genomic_DNA.
DR EMBL; AY102681; AAM27510.1; -; mRNA.
DR RefSeq; NP_001036470.1; NM_001043005.2.
DR RefSeq; NP_001286139.1; NM_001299210.1.
DR RefSeq; NP_610156.1; NM_136312.2.
DR RefSeq; NP_724396.1; NM_165416.2.
DR AlphaFoldDB; Q9V9E3; -.
DR SMR; Q9V9E3; -.
DR BioGRID; 61395; 9.
DR IntAct; Q9V9E3; 11.
DR STRING; 7227.FBpp0085413; -.
DR PaxDb; Q9V9E3; -.
DR PRIDE; Q9V9E3; -.
DR EnsemblMetazoa; FBtr0086077; FBpp0085413; FBgn0033005.
DR EnsemblMetazoa; FBtr0086078; FBpp0085414; FBgn0033005.
DR EnsemblMetazoa; FBtr0111280; FBpp0110537; FBgn0033005.
DR EnsemblMetazoa; FBtr0345009; FBpp0311260; FBgn0033005.
DR GeneID; 35475; -.
DR KEGG; dme:Dmel_CG3107; -.
DR UCSC; CG3107-RA; d. melanogaster.
DR FlyBase; FBgn0033005; CG3107.
DR VEuPathDB; VectorBase:FBgn0033005; -.
DR eggNOG; KOG2019; Eukaryota.
DR GeneTree; ENSGT00390000018381; -.
DR HOGENOM; CLU_009165_1_0_1; -.
DR InParanoid; Q9V9E3; -.
DR OMA; MTYPDKT; -.
DR OrthoDB; 107079at2759; -.
DR PhylomeDB; Q9V9E3; -.
DR Reactome; R-DME-1268020; Mitochondrial protein import.
DR BioGRID-ORCS; 35475; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35475; -.
DR PRO; PR:Q9V9E3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033005; Expressed in cleaving embryo and 30 other tissues.
DR ExpressionAtlas; Q9V9E3; baseline and differential.
DR Genevisible; Q9V9E3; DM.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..1034
FT /note="Presequence protease, mitochondrial"
FT /id="PRO_0000249937"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1034 AA; 119324 MW; 5BE099A0913A599A CRC64;
MLKGGMLSRW KMWSPQYKIL RNHLINFKSV STYKNISGVN TKQPKSPRQF GCMPHVTKKR
KYKYEEGKTY HGFQCERVEH ISEFELTSYT FRYERTGTEL WHIDRNDSNN VFSINFRTTP
FDSTGLPHIL EHLSLCGSQK YPVRDPFFKM LNRSVATFMN AMTGPDYTIY PFSTMNEIDF
RNLQHIYLDA VFRPNLAYFD FLQEGWRLEN KDIFDKQSKL VIKGVVYNEM KGAFSENAQV
FSQNLLNNIF PDHTYRHVSG GNPLEIPKLA YNDLVEFHKK YYHPSNARIY SYGLFDASKT
LALLDEEYLS DQSWVDNSYS LIRQQERWTQ PRLVHISSRL DNMGTTIDRQ NQIAIALLMC
DATNIQESFE LHVLSEVLIR GPNSPFYKNL IEPNFSGGYN QTTGYSSDTK DTTFVVGLQD
LRVEDFKKCI EIFDKTIINS MNDGFDSQHV ESVLHNLELS LKHQNPNFGN TLLFNSTALW
NHDGDVVSNL RVSDMISGLR ESISQNKKYF QEKIEKYFAN NNHRLTLTMS PDEAYEDKFK
QAELELVEQK VKLLDEVKIE KIYERGLILD SYQKAESNTD LLPCLTMNDV RDPPKWPKLF
IQNVQNVRTQ ICKVPTNEIT YFKCMFNITG LSHEETQLMP LFCNVISAMG TTNYNYREFD
KHILLKTGGF DFKLHLIEDV RDSKSYSLSV MINTHALNNN VPEMFALCQE LIKNVRFDDS
ERLKMLIENY ISYISVGVAS SGHLYAMLGA TSQVCDAGKL KSLLYGVDHI DFMKNFVHST
STVDICDKLS TIASKVFNKD NMRGAINTTQ SYEPSAISNY EKFLESLPTF GKTQTSRNIH
YLDPSCQQYV MNIPVNYCAK ALFTVPYLHQ DHPTLRVLAK LLSAKYLLPV IREKNGAYGA
GAKISSDGIF SFYSYRDPNS TKTLNAFDET YKWLRANQNV IDQQSLFESK LGVLQQLDTP
IAPGNIGIDY FLYEVSQEDF ESYRSRMLSV TIDDLQCAIE NYFGKESMHY GKCILGPVNA
NLELETSHKW IINN
