LMLN_MOUSE
ID LMLN_MOUSE Reviewed; 681 AA.
AC Q8BMN4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Leishmanolysin-like peptidase {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q9VH19};
GN Name=Lmln;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. Lipid droplet {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M8 family. {ECO:0000305}.
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DR EMBL; AK030463; BAC26972.1; -; mRNA.
DR EMBL; BC111899; AAI11900.1; -; mRNA.
DR EMBL; BC112428; AAI12429.1; -; mRNA.
DR CCDS; CCDS28127.1; -.
DR RefSeq; NP_766411.1; NM_172823.2.
DR AlphaFoldDB; Q8BMN4; -.
DR SMR; Q8BMN4; -.
DR STRING; 10090.ENSMUSP00000023497; -.
DR MEROPS; M08.003; -.
DR iPTMnet; Q8BMN4; -.
DR PhosphoSitePlus; Q8BMN4; -.
DR PaxDb; Q8BMN4; -.
DR PRIDE; Q8BMN4; -.
DR ProteomicsDB; 290133; -.
DR Antibodypedia; 2701; 23 antibodies from 8 providers.
DR DNASU; 239833; -.
DR Ensembl; ENSMUST00000023497; ENSMUSP00000023497; ENSMUSG00000022802.
DR GeneID; 239833; -.
DR KEGG; mmu:239833; -.
DR UCSC; uc007yzx.1; mouse.
DR CTD; 89782; -.
DR MGI; MGI:2444736; Lmln.
DR VEuPathDB; HostDB:ENSMUSG00000022802; -.
DR eggNOG; KOG2556; Eukaryota.
DR GeneTree; ENSGT00390000008796; -.
DR HOGENOM; CLU_023820_1_0_1; -.
DR InParanoid; Q8BMN4; -.
DR OMA; HSESMWE; -.
DR OrthoDB; 1310134at2759; -.
DR PhylomeDB; Q8BMN4; -.
DR TreeFam; TF315265; -.
DR BioGRID-ORCS; 239833; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Lmln; mouse.
DR PRO; PR:Q8BMN4; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BMN4; protein.
DR Bgee; ENSMUSG00000022802; Expressed in otolith organ and 203 other tissues.
DR Genevisible; Q8BMN4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
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; 2.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Hydrolase; Lipid droplet;
KW Metal-binding; Metalloprotease; Mitosis; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..681
FT /note="Leishmanolysin-like peptidase"
FT /id="PRO_0000303077"
FT ACT_SITE 262
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 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 681 AA; 76575 MW; 5E7A286E2F62D46B CRC64;
MAAAGSGGAG GPGPGPRGRW GGCLWVRGVL LVLGGLPAGA GAAPVSLGTS PPCRHHVLSD
TEVINKVHLK TNHVTKRDAD GHLRIKTIYD QSIEELLPEK RYLVKNKLFP QAISYLEKTF
QVRRPAGRIL LSRQCATNQY LRKENDPHRY CTGECAVHTK CGPVIVPEEH LQQCRVCREG
KWPCGAVGVL DPEGVRDADF VLYVGALATE RCSHENIISY AAYCQQEAKM DRPIAGYANL
CPNMISTQPQ EFIGMLSTVK HEIIHALGFS AGLFAFYHDQ DGNPLTSRSA DGLPPFNYSL
GLYQWSDKVV RKVERLWNVR DNKIVRHTVY LLVTPRVVEE ARKHFNCPVL EGMELENQGG
MGTELNHWEK RLLENEAMTG SHTQNRVLSR ITLALMEDTG WYKANYSMAE KLDWGRGLGC
EFVRKSCKFW IDQHRQRRQV PSPYCDTLRS NPLQLTCRQD QRAVAVCNLQ RFPNPLPPEY
QYFDELTGIP AEDLPYYGGS VEIADYCPFS QEFSWHLSGE YQRSSDCRIL ENQPELFKNY
GAEQYGPHSV CLLQKSAFIM EQCERKLSYP DWGSGCYQVS CSPQGLKVWV QDTSYLCSRA
GQVLPVRIQM NGWIHNGNLL CPSCWDFCEQ CPPETDPPAA NLTRALPLDL CSCSSSLVVT
LWLLLGNLFP LLAGFLLCVW H
