LMLN_DROPS
ID LMLN_DROPS Reviewed; 684 AA.
AC Q29AK2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Leishmanolysin-like peptidase {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q9VH19};
GN ORFNames=GA17800;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Essential for the coordination of mitotic progression, and
CC also plays a role in cell migration. {ECO:0000250|UniProtKB:Q9VH19}.
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. Note=Found in ring-like structures
CC resembling invadopodia. In migrating cells it relocalizes from internal
CC structures to the leading edge of cells.
CC -!- SIMILARITY: Belongs to the peptidase M8 family. {ECO:0000305}.
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DR EMBL; CM000070; EAL27347.1; -; Genomic_DNA.
DR RefSeq; XP_001358210.1; XM_001358173.2.
DR RefSeq; XP_015038642.1; XM_015183156.1.
DR AlphaFoldDB; Q29AK2; -.
DR SMR; Q29AK2; -.
DR STRING; 7237.FBpp0282469; -.
DR MEROPS; M08.002; -.
DR EnsemblMetazoa; FBtr0284031; FBpp0282469; FBgn0077809.
DR EnsemblMetazoa; FBtr0379758; FBpp0340309; FBgn0077809.
DR GeneID; 4801047; -.
DR KEGG; dpo:Dpse_GA17800; -.
DR eggNOG; KOG2556; Eukaryota.
DR HOGENOM; CLU_023820_1_0_1; -.
DR InParanoid; Q29AK2; -.
DR OMA; HSESMWE; -.
DR PhylomeDB; Q29AK2; -.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0077809; Expressed in insect adult head and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS: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; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; IEA:EnsemblMetazoa.
DR GO; GO:0008354; P:germ cell migration; ISS:UniProtKB.
DR GO; GO:0008406; P:gonad development; ISS:UniProtKB.
DR GO; GO:0007444; P:imaginal disc development; ISS:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IEA:EnsemblMetazoa.
DR GO; GO:0007100; P:mitotic centrosome separation; ISS:UniProtKB.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:1902769; P:regulation of choline O-acetyltransferase activity; IEA:EnsemblMetazoa.
DR InterPro; IPR001577; Peptidase_M8.
DR PANTHER; PTHR10942; PTHR10942; 1.
DR Pfam; PF01457; Peptidase_M8; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Mitosis; Protease; Reference proteome; Zinc.
FT CHAIN 1..684
FT /note="Leishmanolysin-like peptidase"
FT /id="PRO_0000303081"
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 684 AA; 76821 MW; D6460C88BBD7C324 CRC64;
MGLPPLQTQP GTFLVALGLC CWLLATANAH NCQHQHPKAH EVVHGVRIQL ADSDDDDAAG
SSDAAVHSVR RRSVTAEQPL RILLVYDDSV YRLEEEKFNL INDTVLPEAV QFWEQALMVR
ETKGIIRLNR KCDSTQVYVK NGHTHCIDQC KATTMCGEVQ VPNEHLDVCR VCNATGQNCR
IDSNTQPGDG IQNADFVFYV SARQTQRCFK GLTVAYAAHC QQEAALDRPI AGHANLCPES
ISTKPQELQT LISTVKHEIL HALGFSVSLY AFFRDDEGRP RTPRKSETGK PFLNEKLQIH
QWSNETIRKV VRENWSVRGG HVNKEVDMMV TPRVVAEARA HFDCDKLEGA ELEDQGGEGT
ALTHWEKRIL ENEAMTGTHT QSPVFSRITL ALMEDSGWYR ANYSMATPLS WGKGLGCSFA
MRSCKDWIQM NHARGRSIHP FCSKVKQDPL QTECTDDRNS VALCNLIRHD YELPKSYQNF
DSLQNVKSGE EGFYGGSVSL ADHCPYIQEF TWRSKNIIVR GSHCRFVENN PKPEKNFALE
SYGHGSKCFD HSEAMWEERS CHQTREWQHW GSGCYKYTCF DGRLHILVGN YTYKCSFPGQ
KLSIRIAANG WLHKGAIMCP PCHELCGSHF AAQGKQCRPG EEADPLNKYP RDNLACGAES
RQQRSVAIIS AALLLAAGLR LGHS
