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Protein

Leishmanolysin-like peptidase

Gene

Lmln

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Metalloprotease essential for the coordination of mitotic progression, and also plays a role in cell migration.By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi261 – 2611Zinc; catalyticBy similarity
Active sitei262 – 2621By similarity
Metal bindingi265 – 2651Zinc; catalyticBy similarity
Metal bindingi367 – 3671Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM08.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Leishmanolysin-like peptidase (EC:3.4.24.-)
Gene namesi
Name:Lmln
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:2444736. Lmln.

Subcellular locationi

  • Cytoplasm
  • Lipid droplet By similarity

  • Note: Found in ring-like structures resembling invadopodia. In migrating cells it relocalizes from internal structures to the leading edge of cells (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lipid droplet

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 681681Leishmanolysin-like peptidasePRO_0000303077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi161 ↔ 224By similarity
Disulfide bondi347 ↔ 445By similarity
Disulfide bondi457 ↔ 551By similarity
Disulfide bondi581 ↔ 628By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ8BMN4.
PRIDEiQ8BMN4.

PTM databases

PhosphoSiteiQ8BMN4.

Expressioni

Gene expression databases

BgeeiQ8BMN4.
CleanExiMM_LMLN.
GenevisibleiQ8BMN4. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023497.

Structurei

3D structure databases

ProteinModelPortaliQ8BMN4.
SMRiQ8BMN4. Positions 216-271.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M8 family.Curated

Phylogenomic databases

eggNOGiKOG2556. Eukaryota.
ENOG410XSAG. LUCA.
GeneTreeiENSGT00390000008796.
HOGENOMiHOG000007103.
HOVERGENiHBG087499.
InParanoidiQ8BMN4.
KOiK13539.
OMAiNFALESY.
OrthoDBiEOG780RNG.
PhylomeDBiQ8BMN4.
TreeFamiTF315265.

Family and domain databases

InterProiIPR001577. Peptidase_M8.
[Graphical view]
PANTHERiPTHR10942. PTHR10942. 2 hits.
PfamiPF01457. Peptidase_M8. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BMN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAGSGGAG GPGPGPRGRW GGCLWVRGVL LVLGGLPAGA GAAPVSLGTS
60 70 80 90 100
PPCRHHVLSD TEVINKVHLK TNHVTKRDAD GHLRIKTIYD QSIEELLPEK
110 120 130 140 150
RYLVKNKLFP QAISYLEKTF QVRRPAGRIL LSRQCATNQY LRKENDPHRY
160 170 180 190 200
CTGECAVHTK CGPVIVPEEH LQQCRVCREG KWPCGAVGVL DPEGVRDADF
210 220 230 240 250
VLYVGALATE RCSHENIISY AAYCQQEAKM DRPIAGYANL CPNMISTQPQ
260 270 280 290 300
EFIGMLSTVK HEIIHALGFS AGLFAFYHDQ DGNPLTSRSA DGLPPFNYSL
310 320 330 340 350
GLYQWSDKVV RKVERLWNVR DNKIVRHTVY LLVTPRVVEE ARKHFNCPVL
360 370 380 390 400
EGMELENQGG MGTELNHWEK RLLENEAMTG SHTQNRVLSR ITLALMEDTG
410 420 430 440 450
WYKANYSMAE KLDWGRGLGC EFVRKSCKFW IDQHRQRRQV PSPYCDTLRS
460 470 480 490 500
NPLQLTCRQD QRAVAVCNLQ RFPNPLPPEY QYFDELTGIP AEDLPYYGGS
510 520 530 540 550
VEIADYCPFS QEFSWHLSGE YQRSSDCRIL ENQPELFKNY GAEQYGPHSV
560 570 580 590 600
CLLQKSAFIM EQCERKLSYP DWGSGCYQVS CSPQGLKVWV QDTSYLCSRA
610 620 630 640 650
GQVLPVRIQM NGWIHNGNLL CPSCWDFCEQ CPPETDPPAA NLTRALPLDL
660 670 680
CSCSSSLVVT LWLLLGNLFP LLAGFLLCVW H
Length:681
Mass (Da):76,575
Last modified:March 1, 2003 - v1
Checksum:i5E7A286E2F62D46B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK030463 mRNA. Translation: BAC26972.1.
BC111899 mRNA. Translation: AAI11900.1.
BC112428 mRNA. Translation: AAI12429.1.
CCDSiCCDS28127.1.
RefSeqiNP_766411.1. NM_172823.2.
UniGeneiMm.131951.

Genome annotation databases

EnsembliENSMUST00000023497; ENSMUSP00000023497; ENSMUSG00000022802.
GeneIDi239833.
KEGGimmu:239833.
UCSCiuc007yzx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK030463 mRNA. Translation: BAC26972.1.
BC111899 mRNA. Translation: AAI11900.1.
BC112428 mRNA. Translation: AAI12429.1.
CCDSiCCDS28127.1.
RefSeqiNP_766411.1. NM_172823.2.
UniGeneiMm.131951.

3D structure databases

ProteinModelPortaliQ8BMN4.
SMRiQ8BMN4. Positions 216-271.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023497.

Protein family/group databases

MEROPSiM08.003.

PTM databases

PhosphoSiteiQ8BMN4.

Proteomic databases

PaxDbiQ8BMN4.
PRIDEiQ8BMN4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023497; ENSMUSP00000023497; ENSMUSG00000022802.
GeneIDi239833.
KEGGimmu:239833.
UCSCiuc007yzx.1. mouse.

Organism-specific databases

CTDi89782.
MGIiMGI:2444736. Lmln.

Phylogenomic databases

eggNOGiKOG2556. Eukaryota.
ENOG410XSAG. LUCA.
GeneTreeiENSGT00390000008796.
HOGENOMiHOG000007103.
HOVERGENiHBG087499.
InParanoidiQ8BMN4.
KOiK13539.
OMAiNFALESY.
OrthoDBiEOG780RNG.
PhylomeDBiQ8BMN4.
TreeFamiTF315265.

Miscellaneous databases

NextBioi384299.
PROiQ8BMN4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BMN4.
CleanExiMM_LMLN.
GenevisibleiQ8BMN4. MM.

Family and domain databases

InterProiIPR001577. Peptidase_M8.
[Graphical view]
PANTHERiPTHR10942. PTHR10942. 2 hits.
PfamiPF01457. Peptidase_M8. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pituitary.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiLMLN_MOUSE
AccessioniPrimary (citable) accession number: Q8BMN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 1, 2003
Last modified: November 11, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.