ID   LMLN_CAEBR              Reviewed;         663 AA.
AC   Q61YG1; A8WVB9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Leishmanolysin-like peptidase {ECO:0000305};
DE            EC=3.4.24.- {ECO:0000250|UniProtKB:Q9VH19};
GN   ORFNames=CBG03556;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Metalloprotease. {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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M8 family. {ECO:0000305}.
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DR   EMBL; HE601339; CAP24430.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q61YG1; -.
DR   SMR; Q61YG1; -.
DR   STRING; 6238.CBG03556; -.
DR   EnsemblMetazoa; CBG03556a.1; CBG03556a.1; WBGene00026399.
DR   WormBase; CBG03556a; CBP37311; WBGene00026399; -.
DR   eggNOG; KOG2556; Eukaryota.
DR   HOGENOM; CLU_023820_1_0_1; -.
DR   InParanoid; Q61YG1; -.
DR   OMA; HSESMWE; -.
DR   OrthoDB; 1310134at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..663
FT                   /note="Leishmanolysin-like peptidase"
FT                   /id="PRO_0000303078"
FT   ACT_SITE        247
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   663 AA;  76389 MW;  3FFA0709991143FE CRC64;
     MKPRLIFQYF AYSFLVFLPF INTLPCSYQN PRIEDVLLEV PIEHHHPHRH RRDSENPTET
     PPDLQKFAPL RIQLHYDKSI QNLTAEVQHF VNTTLLPEAV GYWENALRVR PMKTPIRLRR
     KCISSFYYYK QGMRNVACDK GCRERTTCGE ADIPNDHLLD CLACNNTDDC QTTGEMGEGV
     KESDFILYVT AHNSKRCEGP ETLSYAAHCQ QEADFDRPIA GNVNLCPSAL SVHNHDYEIL
     TSTVKHEILH ALGFSVGLYA FFRDKDGKPR TKRNRYGRPT SLNKQRGYYD WDKNTITTVL
     REEWWTGEGK VIHPIQMMVT PKVREEARRH FGCDKLEGAE LENQGGEGTV LTHWEKRAYE
     NEAMTGTHTQ NPVYSRLTLA FLEDTGWYQP NYEVAEDLHW GKQLGCDFAM KSCGEWIHQK
     RILGEDAYPY CSDIKHDGTK SMAITRCTSQ RDSLALCNLI PFQKELPPQY RNFMSLPGVN
     PDGAKYYGGS VEMADYCPFL QEFEWKMPEK EHKDSRCELE GNGKEGEDIL EVYGENSKCF
     EFPKPWTERK CGRIRVLSHY MAGCYEYQCT NGTLYVGSYN ATDMYPCYAE NQKVHIKKVV
     DGWLREGSLI CPKCSDYCSS CGPPIVIPDY IGDPELDEPC FAFSKFSVFG LFSCYLAILY
     IRF