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Q96KR4 (LMLN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leishmanolysin-like peptidase

EC=3.4.24.-
Alternative name(s):
Invadolysin
Gene names
Name:LMLN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

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. Ref.1 Ref.4

Tissue specificity

Expressed in all cell lines analyzed. Ref.1

Sequence similarities

Belongs to the peptidase M8 family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96KR4-1)

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.
Isoform 2 (identifier: Q96KR4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MVTTLGPKMA...CRHHVPSDTE → MGRRSGLLGLRPGPEPVALER
     411-411: G → GWYKANYSMAEKLDWGRGMGCDFVRKSCKFWIDQQRQK
Isoform 3 (identifier: Q96KR4-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 655655Leishmanolysin-like peptidase
PRO_0000303076

Sites

Active site2731 By similarity
Metal binding2721Zinc; catalytic By similarity
Metal binding2761Zinc; catalytic By similarity
Metal binding3781Zinc; catalytic By similarity

Amino acid modifications

Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation6151N-linked (GlcNAc...) Potential
Disulfide bond172 ↔ 235 By similarity
Disulfide bond358 ↔ 419 By similarity
Disulfide bond431 ↔ 525 By similarity
Disulfide bond555 ↔ 602 By similarity

Natural variations

Alternative sequence1 – 7373MVTTL…PSDTE → MGRRSGLLGLRPGPEPVALE R in isoform 2.
VSP_028002
Alternative sequence4111G → GWYKANYSMAEKLDWGRGMG CDFVRKSCKFWIDQQRQK in isoform 2 and isoform 3.
VSP_028003
Natural variant1061E → D.
Corresponds to variant rs7373165 [ dbSNP | Ensembl ].
VAR_060158

Experimental info

Sequence conflict5391R → K in CAP49203. Ref.1
Sequence conflict5391R → K in CAP49204. Ref.1
Sequence conflict5391R → K in CAC42882. Ref.2
Sequence conflict5391R → K in CAC42883. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: D6A767CE3FA7A915

FASTA65573,568
        10         20         30         40         50         60 
MVTTLGPKMA AEWGGGVGYS GSGPGRSRWR WSGSVWVRSV LLLLGGLRAS ATSTPVSLGS 

        70         80         90        100        110        120 
SPPCRHHVPS DTEVINKVHL KANHVVKRDV DEHLRIKTVY DKSVEELLPE KKNLVKNKLF 

       130        140        150        160        170        180 
PQAISYLEKT FQVRRPAGTI LLSRQCATNQ YLRKENDPHR YCTGECAAHT KCGPVIVPEE 

       190        200        210        220        230        240 
HLQQCRVYRG GKWPHGAVGV PDQEGISDAD FVLYVGALAT ERCSHENIIS YAAYCQQEAN 

       250        260        270        280        290        300 
MDRPIAGYAN LCPNMISTQP QEFVGMLSTV KHEVIHALGF SAGLFAFYHD KDGNPLTSRF 

       310        320        330        340        350        360 
ADGLPPFNYS LGLYQWSDKV VRKVERLWDV RDNKIVRHTV YLLVTPRVVE EARKHFDCPV 

       370        380        390        400        410        420 
LEGMELENQG GVGTELNHWE KRLLENEAMT GSHTQNRVLS RITLALMEDT GRQMLSPYCD 

       430        440        450        460        470        480 
TLRSNPLQLT CRQDQRAVAV CNLQKFPKPL PQEYQYFDEL SGIPAEDLPY YGGSVEIADY 

       490        500        510        520        530        540 
CPFSQEFSWH LSGEYQRSSD CRILENQPEI FKNYGAEKYG PHSVCLIQKS AFVMEKCERK 

       550        560        570        580        590        600 
LSYPDWGSGC YQVSCSPQGL KVWVQDTSYL CSRAGQVLPV SIQMNGWIHD GNLLCPSCWD 

       610        620        630        640        650 
FCELCPPETD PPATNLTRAL PLDLCSCSSS LVVTLWLLLG NLFPLLAGFL LCIWH 

« Hide

Isoform 2 [UniParc].

Checksum: 272AB99BBE391B42
Show »

FASTA64072,780
Isoform 3 [UniParc].

Checksum: 3000E53236452C1D
Show »

FASTA69278,111

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001129521.2. NM_001136049.2.
NP_149018.2. NM_033029.3.
UniGeneHs.518540.

3D structure databases

ProteinModelPortalQ96KR4.
SMRQ96KR4. Positions 242-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000410926.

Protein family/group databases

MEROPSM08.003.

PTM databases

PhosphoSiteQ96KR4.

Polymorphism databases

DMDM296434578.

Proteomic databases

PaxDbQ96KR4.
PRIDEQ96KR4.

Protocols and materials databases

DNASU89782.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330198; ENSP00000328829; ENSG00000185621. [Q96KR4-1]
ENST00000420910; ENSP00000410926; ENSG00000185621. [Q96KR4-3]
ENST00000482695; ENSP00000418324; ENSG00000185621. [Q96KR4-2]
GeneID89782.
KEGGhsa:89782.
UCSCuc003fyt.3. human. [Q96KR4-2]
uc011buo.2. human. [Q96KR4-1]

Organism-specific databases

CTD89782.
GeneCardsGC03P197687.
HGNCHGNC:15991. LMLN.
HPAHPA016481.
HPA028844.
MIM609380. gene.
neXtProtNX_Q96KR4.
PharmGKBPA30402.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279222.
HOGENOMHOG000007103.
HOVERGENHBG087499.
InParanoidQ96KR4.
KOK13539.
OMAIRLNRKC.
OrthoDBEOG780RNG.
PhylomeDBQ96KR4.
TreeFamTF315265.

Gene expression databases

ArrayExpressQ96KR4.
BgeeQ96KR4.
CleanExHS_LMLN.
GenevestigatorQ96KR4.

Family and domain databases

InterProIPR001577. Peptidase_M8.
[Graphical view]
PANTHERPTHR10942. PTHR10942. 1 hit.
PfamPF01457. Peptidase_M8. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi89782.
NextBio35470729.
PROQ96KR4.
SOURCESearch...

Entry information

Entry nameLMLN_HUMAN
AccessionPrimary (citable) accession number: Q96KR4
Secondary accession number(s): B3LDG9 expand/collapse secondary AC list , B3LDH0, C9J796, F8WB28, Q96KR5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM