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Protein

Leishmanolysin-like peptidase

Gene

LMLN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 bindingi272 – 2721Zinc; catalyticBy similarity
Active sitei273 – 2731By similarity
Metal bindingi276 – 2761Zinc; catalyticBy similarity
Metal bindingi378 – 3781Zinc; catalyticBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro

GO - Biological processi

  1. cell adhesion Source: InterPro
  2. cell division Source: UniProtKB-KW
  3. mitotic nuclear division Source: UniProtKB-KW
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.-)
Alternative name(s):
Invadolysin
Gene namesi
Name:LMLN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:15991. LMLN.

Subcellular locationi

Cytoplasm. Lipid droplet
Note: Found in ring-like structures resembling invadopodia. In migrating cells it relocalizes from internal structures to the leading edge of cells.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. focal adhesion Source: HPA
  3. lipid particle Source: UniProtKB-SubCell
  4. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lipid droplet

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30402.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 655655Leishmanolysin-like peptidasePRO_0000303076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi172 ↔ 235By similarity
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi358 ↔ 419By similarity
Disulfide bondi431 ↔ 525By similarity
Disulfide bondi555 ↔ 602By similarity
Glycosylationi615 – 6151N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ96KR4.
PRIDEiQ96KR4.

PTM databases

PhosphoSiteiQ96KR4.

Expressioni

Tissue specificityi

Expressed in all cell lines analyzed.1 Publication

Gene expression databases

BgeeiQ96KR4.
CleanExiHS_LMLN.
ExpressionAtlasiQ96KR4. baseline and differential.
GenevestigatoriQ96KR4.

Organism-specific databases

HPAiHPA016481.
HPA028844.

Interactioni

Protein-protein interaction databases

BioGridi124601. 2 interactions.
STRINGi9606.ENSP00000410926.

Structurei

3D structure databases

ProteinModelPortaliQ96KR4.
SMRiQ96KR4. Positions 242-282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M8 family.Curated

Phylogenomic databases

eggNOGiNOG279222.
GeneTreeiENSGT00390000008796.
HOGENOMiHOG000007103.
HOVERGENiHBG087499.
InParanoidiQ96KR4.
KOiK13539.
OMAiMWEERSC.
OrthoDBiEOG780RNG.
PhylomeDBiQ96KR4.
TreeFamiTF315265.

Family and domain databases

InterProiIPR001577. Peptidase_M8.
[Graphical view]
PANTHERiPTHR10942. PTHR10942. 1 hit.
PfamiPF01457. Peptidase_M8. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96KR4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVTTLGPKMA AEWGGGVGYS GSGPGRSRWR WSGSVWVRSV LLLLGGLRAS
60 70 80 90 100
ATSTPVSLGS SPPCRHHVPS DTEVINKVHL KANHVVKRDV DEHLRIKTVY
110 120 130 140 150
DKSVEELLPE KKNLVKNKLF PQAISYLEKT FQVRRPAGTI LLSRQCATNQ
160 170 180 190 200
YLRKENDPHR YCTGECAAHT KCGPVIVPEE HLQQCRVYRG GKWPHGAVGV
210 220 230 240 250
PDQEGISDAD FVLYVGALAT ERCSHENIIS YAAYCQQEAN MDRPIAGYAN
260 270 280 290 300
LCPNMISTQP QEFVGMLSTV KHEVIHALGF SAGLFAFYHD KDGNPLTSRF
310 320 330 340 350
ADGLPPFNYS LGLYQWSDKV VRKVERLWDV RDNKIVRHTV YLLVTPRVVE
360 370 380 390 400
EARKHFDCPV LEGMELENQG GVGTELNHWE KRLLENEAMT GSHTQNRVLS
410 420 430 440 450
RITLALMEDT GRQMLSPYCD TLRSNPLQLT CRQDQRAVAV CNLQKFPKPL
460 470 480 490 500
PQEYQYFDEL SGIPAEDLPY YGGSVEIADY CPFSQEFSWH LSGEYQRSSD
510 520 530 540 550
CRILENQPEI FKNYGAEKYG PHSVCLIQKS AFVMEKCERK LSYPDWGSGC
560 570 580 590 600
YQVSCSPQGL KVWVQDTSYL CSRAGQVLPV SIQMNGWIHD GNLLCPSCWD
610 620 630 640 650
FCELCPPETD PPATNLTRAL PLDLCSCSSS LVVTLWLLLG NLFPLLAGFL

LCIWH
Length:655
Mass (Da):73,568
Last modified:May 18, 2010 - v2
Checksum:iD6A767CE3FA7A915
GO
Isoform 2 (identifier: Q96KR4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MVTTLGPKMA...CRHHVPSDTE → MGRRSGLLGLRPGPEPVALER
     411-411: G → GWYKANYSMAEKLDWGRGMGCDFVRKSCKFWIDQQRQK

Show »
Length:640
Mass (Da):72,780
Checksum:i272AB99BBE391B42
GO
Isoform 3 (identifier: Q96KR4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     411-411: G → GWYKANYSMAEKLDWGRGMGCDFVRKSCKFWIDQQRQK

Show »
Length:692
Mass (Da):78,111
Checksum:i3000E53236452C1D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti539 – 5391R → K in CAP49203 (PubMed:19706689).Curated
Sequence conflicti539 – 5391R → K in CAP49204 (PubMed:19706689).Curated
Sequence conflicti539 – 5391R → K in CAC42882 (Ref. 2) Curated
Sequence conflicti539 – 5391R → K in CAC42883 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061E → D.
Corresponds to variant rs7373165 [ dbSNP | Ensembl ].
VAR_060158

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7373MVTTL…PSDTE → MGRRSGLLGLRPGPEPVALE R in isoform 2. 2 PublicationsVSP_028002Add
BLAST
Alternative sequencei411 – 4111G → GWYKANYSMAEKLDWGRGMG CDFVRKSCKFWIDQQRQK in isoform 2 and isoform 3. 2 PublicationsVSP_028003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM920777 mRNA. Translation: CAP49203.1.
AM920778 mRNA. Translation: CAP49204.1.
AJ312398 mRNA. Translation: CAC42882.1.
AJ312399 mRNA. Translation: CAC42883.1.
AC135893 Genomic DNA. No translation available.
CCDSiCCDS3332.1. [Q96KR4-1]
CCDS46988.1. [Q96KR4-3]
RefSeqiNP_001129521.2. NM_001136049.2. [Q96KR4-3]
NP_149018.2. NM_033029.3. [Q96KR4-1]
UniGeneiHs.518540.

Genome annotation databases

EnsembliENST00000330198; ENSP00000328829; ENSG00000185621. [Q96KR4-1]
ENST00000420910; ENSP00000410926; ENSG00000185621. [Q96KR4-3]
ENST00000482695; ENSP00000418324; ENSG00000185621. [Q96KR4-2]
GeneIDi89782.
KEGGihsa:89782.
UCSCiuc003fyt.3. human. [Q96KR4-2]
uc011buo.2. human. [Q96KR4-1]

Polymorphism databases

DMDMi296434578.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM920777 mRNA. Translation: CAP49203.1.
AM920778 mRNA. Translation: CAP49204.1.
AJ312398 mRNA. Translation: CAC42882.1.
AJ312399 mRNA. Translation: CAC42883.1.
AC135893 Genomic DNA. No translation available.
CCDSiCCDS3332.1. [Q96KR4-1]
CCDS46988.1. [Q96KR4-3]
RefSeqiNP_001129521.2. NM_001136049.2. [Q96KR4-3]
NP_149018.2. NM_033029.3. [Q96KR4-1]
UniGeneiHs.518540.

3D structure databases

ProteinModelPortaliQ96KR4.
SMRiQ96KR4. Positions 242-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124601. 2 interactions.
STRINGi9606.ENSP00000410926.

Protein family/group databases

MEROPSiM08.003.

PTM databases

PhosphoSiteiQ96KR4.

Polymorphism databases

DMDMi296434578.

Proteomic databases

PaxDbiQ96KR4.
PRIDEiQ96KR4.

Protocols and materials databases

DNASUi89782.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330198; ENSP00000328829; ENSG00000185621. [Q96KR4-1]
ENST00000420910; ENSP00000410926; ENSG00000185621. [Q96KR4-3]
ENST00000482695; ENSP00000418324; ENSG00000185621. [Q96KR4-2]
GeneIDi89782.
KEGGihsa:89782.
UCSCiuc003fyt.3. human. [Q96KR4-2]
uc011buo.2. human. [Q96KR4-1]

Organism-specific databases

CTDi89782.
GeneCardsiGC03P197687.
HGNCiHGNC:15991. LMLN.
HPAiHPA016481.
HPA028844.
MIMi609380. gene.
neXtProtiNX_Q96KR4.
PharmGKBiPA30402.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG279222.
GeneTreeiENSGT00390000008796.
HOGENOMiHOG000007103.
HOVERGENiHBG087499.
InParanoidiQ96KR4.
KOiK13539.
OMAiMWEERSC.
OrthoDBiEOG780RNG.
PhylomeDBiQ96KR4.
TreeFamiTF315265.

Miscellaneous databases

GenomeRNAii89782.
NextBioi35470729.
PROiQ96KR4.
SOURCEiSearch...

Gene expression databases

BgeeiQ96KR4.
CleanExiHS_LMLN.
ExpressionAtlasiQ96KR4. baseline and differential.
GenevestigatoriQ96KR4.

Family and domain databases

InterProiIPR001577. Peptidase_M8.
[Graphical view]
PANTHERiPTHR10942. PTHR10942. 1 hit.
PfamiPF01457. Peptidase_M8. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The conserved metalloprotease invadolysin localizes to the surface of lipid droplets."
    Cobbe N., Marshall K.M., Gururaja Rao S., Chang C.W., Di Cara F., Duca E., Vass S., Kassan A., Heck M.M.
    J. Cell Sci. 122:3414-3423(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Cloning and expression of splice variants of leishmanolysin-like protein, a human form of the protozoan leishmanolysin, EC 3.4.24.36."
    Chen J.M., Fortunato M., Barrett A.J.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Colon and Testis.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Invadolysin: a novel, conserved metalloprotease links mitotic structural rearrangements with cell migration."
    McHugh B., Krause S.A., Yu B., Deans A.M., Heasman S., McLaughlin P., Heck M.M.
    J. Cell Biol. 167:673-686(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiLMLN_HUMAN
AccessioniPrimary (citable) accession number: Q96KR4
Secondary accession number(s): B3LDG9
, B3LDH0, C9J796, F8WB28, Q96KR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 18, 2010
Last modified: February 4, 2015
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.