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Protein

Lipase member M

Gene

LIPM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a highly specific role in the last step of keratinocyte differentiation. May have an essential function in lipid metabolism of the most differentiated epidermal layers.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei186 – 1861NucleophileBy similarity
Active sitei357 – 3571Charge relay systemPROSITE-ProRule annotation
Active sitei386 – 3861Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-HSA-192456. Digestion of dietary lipid.

Protein family/group databases

ESTHERihuman-LIPM. Acidic_Lipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase member M (EC:3.1.1.-)
Alternative name(s):
Lipase-like abhydrolase domain-containing protein 3
Gene namesi
Name:LIPM
Synonyms:LIPL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:23455. LIPM.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162394101.

Polymorphism and mutation databases

BioMutaiLIPM.
DMDMi147647745.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence analysisAdd
BLAST
Chaini34 – 423390Lipase member MPRO_0000286829Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi260 ↔ 269By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ5VYY2.
PaxDbiQ5VYY2.
PRIDEiQ5VYY2.

PTM databases

iPTMnetiQ5VYY2.
PhosphoSiteiQ5VYY2.

Expressioni

Tissue specificityi

Exclusively expressed in the epidermis within the granular keratinocytes.1 Publication

Gene expression databases

BgeeiQ5VYY2.
CleanExiHS_LIPM.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000383901.

Structurei

3D structure databases

ProteinModelPortaliQ5VYY2.
SMRiQ5VYY2. Positions 42-407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2624. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00550000074328.
HOGENOMiHOG000240694.
HOVERGENiHBG006265.
InParanoidiQ5VYY2.
KOiK19406.
OMAiDWLSNPE.
OrthoDBiEOG71RXJN.
PhylomeDBiQ5VYY2.
TreeFamiTF315485.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR025483. Lipase_euk.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000862. Steryl_ester_lip. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5VYY2-1) [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
MLETLSRQWI VSHRMEMWLL ILVAYMFQRN VNSVHMPTKA VDPEAFMNIS
60 70 80 90 100
EIIQHQGYPC EEYEVATEDG YILSVNRIPR GLVQPKKTGS RPVVLLQHGL
110 120 130 140 150
VGGASNWISN LPNNSLGFIL ADAGFDVWMG NSRGNAWSRK HKTLSIDQDE
160 170 180 190 200
FWAFSYDEMA RFDLPAVINF ILQKTGQEKI YYVGYSQGTT MGFIAFSTMP
210 220 230 240 250
ELAQKIKMYF ALAPIATVKH AKSPGTKFLL LPDMMIKGLF GKKEFLYQTR
260 270 280 290 300
FLRQLVIYLC GQVILDQICS NIMLLLGGFN TNNMNMSRAS VYAAHTLAGT
310 320 330 340 350
SVQNILHWSQ AVNSGELRAF DWGSETKNLE KCNQPTPVRY RVRDMTVPTA
360 370 380 390 400
MWTGGQDWLS NPEDVKMLLS EVTNLIYHKN IPEWAHVDFI WGLDAPHRMY
410 420
NEIIHLMQQE ETNLSQGRCE AVL
Length:423
Mass (Da):48,233
Last modified:May 15, 2007 - v2
Checksum:i9B622EEB88F05478
GO
Isoform 2 (identifier: Q5VYY2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MLETLSRQWIVSHRMEMWLLILVAYMFQRNVNSVHMPTKAVDPEAFMNI → MTRPLDRKQ

Note: No experimental confirmation available.
Show »
Length:383
Mass (Da):43,498
Checksum:iEE47A6D52316C0FE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti274 – 2741L → S.
Corresponds to variant rs3910680 [ dbSNP | Ensembl ].
VAR_059382
Natural varianti418 – 4181R → W.
Corresponds to variant rs11202862 [ dbSNP | Ensembl ].
VAR_032191

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4949MLETL…AFMNI → MTRPLDRKQ in isoform 2. 1 PublicationVSP_056261Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF426484 mRNA. Translation: ABR08389.1.
AL353113, AL358532 Genomic DNA. Translation: CAH72238.2.
AL358532, AL353113 Genomic DNA. Translation: CAO77925.1.
BC157888 mRNA. Translation: AAI57889.1.
BC171908 mRNA. Translation: AAI71908.1.
CCDSiCCDS44457.1. [Q5VYY2-1]
RefSeqiNP_001121687.1. NM_001128215.1. [Q5VYY2-1]
UniGeneiHs.55118.

Genome annotation databases

EnsembliENST00000404743; ENSP00000383901; ENSG00000173239. [Q5VYY2-1]
ENST00000539337; ENSP00000440375; ENSG00000173239. [Q5VYY2-2]
GeneIDi340654.
KEGGihsa:340654.
UCSCiuc009xtm.2. human. [Q5VYY2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF426484 mRNA. Translation: ABR08389.1.
AL353113, AL358532 Genomic DNA. Translation: CAH72238.2.
AL358532, AL353113 Genomic DNA. Translation: CAO77925.1.
BC157888 mRNA. Translation: AAI57889.1.
BC171908 mRNA. Translation: AAI71908.1.
CCDSiCCDS44457.1. [Q5VYY2-1]
RefSeqiNP_001121687.1. NM_001128215.1. [Q5VYY2-1]
UniGeneiHs.55118.

3D structure databases

ProteinModelPortaliQ5VYY2.
SMRiQ5VYY2. Positions 42-407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000383901.

Protein family/group databases

ESTHERihuman-LIPM. Acidic_Lipase.

PTM databases

iPTMnetiQ5VYY2.
PhosphoSiteiQ5VYY2.

Polymorphism and mutation databases

BioMutaiLIPM.
DMDMi147647745.

Proteomic databases

EPDiQ5VYY2.
PaxDbiQ5VYY2.
PRIDEiQ5VYY2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000404743; ENSP00000383901; ENSG00000173239. [Q5VYY2-1]
ENST00000539337; ENSP00000440375; ENSG00000173239. [Q5VYY2-2]
GeneIDi340654.
KEGGihsa:340654.
UCSCiuc009xtm.2. human. [Q5VYY2-1]

Organism-specific databases

CTDi340654.
GeneCardsiLIPM.
HGNCiHGNC:23455. LIPM.
MIMi613923. gene.
neXtProtiNX_Q5VYY2.
PharmGKBiPA162394101.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2624. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00550000074328.
HOGENOMiHOG000240694.
HOVERGENiHBG006265.
InParanoidiQ5VYY2.
KOiK19406.
OMAiDWLSNPE.
OrthoDBiEOG71RXJN.
PhylomeDBiQ5VYY2.
TreeFamiTF315485.

Enzyme and pathway databases

ReactomeiR-HSA-192456. Digestion of dietary lipid.

Miscellaneous databases

GenomeRNAii340654.
PROiQ5VYY2.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VYY2.
CleanExiHS_LIPM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR025483. Lipase_euk.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000862. Steryl_ester_lip. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Large-scale identification of human genes implicated in epidermal barrier function."
    Toulza E., Mattiuzzo N.R., Galliano M.F., Jonca N., Dossat C., Jacob D., de Daruvar A., Wincker P., Serre G., Guerrin M.
    Genome Biol. 8:R107.1-R107.23(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Keratinocyte.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 2).

Entry informationi

Entry nameiLIPM_HUMAN
AccessioniPrimary (citable) accession number: Q5VYY2
Secondary accession number(s): A6PVS3, B2RXK7, B5MCR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: June 8, 2016
This is version 100 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 10
    Human chromosome 10: 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. 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.