LMLN_DROME
ID LMLN_DROME Reviewed; 683 AA.
AC Q9VH19; Q9NH00;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Leishmanolysin-like peptidase {ECO:0000305};
DE EC=3.4.24.- {ECO:0000269|PubMed:15557119};
DE AltName: Full=Invadolysin;
GN Name=Invadolysin; Synonyms=l(3)IX-14; ORFNames=CG3953;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15557119; DOI=10.1083/jcb.200405155;
RA McHugh B., Krause S.A., Yu B., Deans A.M., Heasman S., McLaughlin P.,
RA Heck M.M.;
RT "Invadolysin: a novel, conserved metalloprotease links mitotic structural
RT rearrangements with cell migration.";
RL J. Cell Biol. 167:673-686(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=Head;
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: Essential for the coordination of mitotic progression, and
CC also plays a role in cell migration. {ECO:0000269|PubMed:15557119}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P08148};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08148};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15557119}.
CC Note=Found in ring-like structures resembling invadopodia. In migrating
CC cells it relocalizes from internal structures to the leading edge of
CC cells. {ECO:0000269|PubMed:15557119}.
CC -!- SIMILARITY: Belongs to the peptidase M8 family. {ECO:0000305}.
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DR EMBL; AF234630; AAF40433.1; -; mRNA.
DR EMBL; AE014297; AAF54501.2; -; Genomic_DNA.
DR EMBL; BT001861; AAN71624.1; -; mRNA.
DR RefSeq; NP_652072.1; NM_143815.4.
DR AlphaFoldDB; Q9VH19; -.
DR SMR; Q9VH19; -.
DR BioGRID; 72358; 31.
DR STRING; 7227.FBpp0081659; -.
DR MEROPS; M08.002; -.
DR PaxDb; Q9VH19; -.
DR PRIDE; Q9VH19; -.
DR EnsemblMetazoa; FBtr0082181; FBpp0081659; FBgn0086359.
DR GeneID; 49580; -.
DR KEGG; dme:Dmel_CG3953; -.
DR CTD; 49580; -.
DR FlyBase; FBgn0086359; Invadolysin.
DR VEuPathDB; VectorBase:FBgn0086359; -.
DR eggNOG; KOG2556; Eukaryota.
DR GeneTree; ENSGT00390000008796; -.
DR HOGENOM; CLU_023820_1_0_1; -.
DR InParanoid; Q9VH19; -.
DR OMA; HSESMWE; -.
DR OrthoDB; 1310134at2759; -.
DR PhylomeDB; Q9VH19; -.
DR BioGRID-ORCS; 49580; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 49580; -.
DR PRO; PR:Q9VH19; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0086359; Expressed in seminal fluid secreting gland and 33 other tissues.
DR Genevisible; Q9VH19; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IDA:FlyBase.
DR GO; GO:0007420; P:brain development; IMP:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051298; P:centrosome duplication; IMP:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:FlyBase.
DR GO; GO:0022900; P:electron transport chain; IDA:FlyBase.
DR GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR GO; GO:0008406; P:gonad development; IMP:FlyBase.
DR GO; GO:0007444; P:imaginal disc development; IMP:FlyBase.
DR GO; GO:0019915; P:lipid storage; IMP:FlyBase.
DR GO; GO:0007100; P:mitotic centrosome separation; IMP:FlyBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:FlyBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:1902769; P:regulation of choline O-acetyltransferase activity; IDA:FlyBase.
DR InterPro; IPR001577; Peptidase_M8.
DR PANTHER; PTHR10942; PTHR10942; 1.
DR Pfam; PF01457; Peptidase_M8; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Mitosis; Protease; Reference proteome; Zinc.
FT CHAIN 1..683
FT /note="Leishmanolysin-like peptidase"
FT /id="PRO_0000303080"
FT ACT_SITE 258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 683 AA; 76978 MW; C359D526F006CD9E CRC64;
MAKTPPLRPH GNMAKFLAAL GICSWLLVSA TAHNCQHQHP KAHEVVHGVR IQLADSEDDS
AGDPARHSVR RRSVAAEQPL RILLVYDESV YRLEEEKFNL INDTVLPEAV QFWEQALMVR
ETKGVIRLNR KCDSTQVYVK NGHTHCIDHC KATTMCGEVQ VPDAHLDVCR VCNATGQNCR
IDSNTQPGEG IENADFVFYV SARQTQRCFK GLTVAYAAHC QQEAALDRPI AGHANLCPES
ISTKPQELQT LISTVKHEIL HALGFSVSLY AFFRDDDGKP RTPRKLDTGK PYLNEKLQIH
QWSNETIRKV VRENWSVRGG HVNKVVDMMV TPRVIAEVRA HFNCNKLEGA ELEDQGGEGT
ALTHWEKRIL ENEAMTGTHT QSPVFSRITL ALMEDSGWYR ANYSMATPLT WGKGLGCAFA
MRSCKDWIQY NHARGRSIHP FCSKVKQDPL QTECTDDRNS VALCNLIRHE FELPKGYQNF
DSLNHVKDGE EGFYGGSVSL ADHCPYIQEF TWRSKNVIVR GSHCRFTENN PRPEKNFALE
SYGEGAKCFD HSESMWEERS CHQTREWQHW GSGCYKYDCF DGRLHILVGN YSYKCSFPGQ
KLSIRIAANG WLHKGAIMCP PCHELCGAQF AAQGKQCRPG EEPDPLNKYP RDNLACGAGS
EKSRSVAIIT AVLLLFGLRW GFS
