ID   LMLN2_HUMAN             Reviewed;         788 AA.
AC   A0A1B0GTW7;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2016, sequence version 1.
DT   16-JAN-2019, entry version 15.
DE   RecName: Full=Leishmanolysin-like peptidase 2 {ECO:0000305};
DE            EC=3.4.24.- {ECO:0000250|UniProtKB:Q9VH19};
DE   Flags: Precursor;
GN   Name=LMLN2 {ECO:0000312|HGNC:HGNC:53647};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(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: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the peptidase M8 family. {ECO:0000305}.
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DR   EMBL; AL117258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS86373.1; -.
DR   UniGene; Hs.578287; -.
DR   SMR; A0A1B0GTW7; -.
DR   BioMuta; ENSG00000283654; -.
DR   jPOST; A0A1B0GTW7; -.
DR   PeptideAtlas; A0A1B0GTW7; -.
DR   Ensembl; ENST00000637218; ENSP00000489869; ENSG00000283654.
DR   GeneCards; LMLN2; -.
DR   HGNC; HGNC:53647; LMLN2.
DR   neXtProt; NX_A0A1B0GTW7; -.
DR   GeneTree; ENSGT00940000163573; -.
DR   OMA; CFLANLT; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   InterPro; IPR001577; Peptidase_M8.
DR   PANTHER; PTHR10942; PTHR10942; 2.
DR   Pfam; PF01457; Peptidase_M8; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    788       Leishmanolysin-like peptidase 2.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_5008408627.
FT   TOPO_DOM     21    735       Extracellular. {ECO:0000305}.
FT   TRANSMEM    736    756       Helical. {ECO:0000255}.
FT   TOPO_DOM    757    788       Cytoplasmic. {ECO:0000305}.
FT   ACT_SITE    306    306       {ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       305    305       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       309    309       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       385    385       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   CARBOHYD    333    333       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    425    425       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    491    491       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    524    524       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    713    713       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
SQ   SEQUENCE   788 AA;  85397 MW;  8051E168BBD3EAF8 CRC64;
     MLLLLLLLLL LPPLVLRVAA SRCLHDETQK SVSLLRPPFS QLPSKSRSSS LTLPSSRDPQ
     PLRIQSCYLG DHISDGAWDP EGEGMRGGSR ALAAVREATQ RIQAVLAVQG PLLLSRDPAQ
     YCHAVWGDPD SPNYHRCSLL NPGYKGESCL GAKIPDTHLR GYALWPEQGP PQLVQPDGPG
     VQNTDFLLYV RVAHTSKCHQ ETVSLCCPGW STAAQSQLTA ALTSWAQRRG FVMLPRLCLK
     LLGSSNLPTL ASQSIRITGP SVIAYAACCQ LDSEDRPLAG TIVYCAQHLT SPSLSHSDIV
     MATLHELLHA LGFSGQLFKK WRDCPSGFSV RENCSTRQLV TRQDEWGQLL LTTPAVSLSL
     AKHLGVSGAS LGVPLEEEEG LLSSHWEARL LQGSLMTATF DGAQRTRLDP ITLAAFKDSG
     WYQVNHSAAE ELLWGQGSGP EFGLVTTCGT GSSDFFCTGS GLGCHYLHLD KGSCSSDPML
     EGCRMYKPLA NGSECWKKEN GFPAGVDNPH GEIYHPQSRC FFANLTSQLL PGDKPRHPSL
     TPHLKEAELM GRCYLHQCTG RGAYKVQVEG SPWVPCLPGK VIQIPGYYGL LFCPRGRLCQ
     TNEDINAVTS PPVSLSTPDP LFQLSLELAG PPGHSLGKEQ QEGLAEAVLE ALASKGGTGR
     CYFHGPSITT SLVFTVHMWK SPGCQGPSVA TLHKALTLTL QKKPLEVYHG GANFTTQPSK
     LLVTSDHNPS MTHLRLSMGL CLMLLILVGV MGTTAYQKRA TLPVRPSASY HSPELHSTRV
     PVRGIREV
//