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Protein

Lipase member M

Gene

Lipm

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei186NucleophileBy similarity1
Active sitei357Charge relay systemPROSITE-ProRule annotation1
Active sitei386Charge relay systemPROSITE-ProRule annotation1

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-MMU-192456. Digestion of dietary lipid.

Protein family/group databases

ESTHERimouse-LIPM. Acidic_Lipase.
MEROPSiS33.A58.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1926003. Lipm.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000028683034 – 422Lipase member MAdd BLAST389

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi48N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi260 ↔ 269By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8K2A6.
PRIDEiQ8K2A6.

PTM databases

iPTMnetiQ8K2A6.
PhosphoSitePlusiQ8K2A6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000056078.
CleanExiMM_LIPM.
GenevisibleiQ8K2A6. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025685.

Structurei

3D structure databases

ProteinModelPortaliQ8K2A6.
SMRiQ8K2A6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini92 – 392AB hydrolase-1Sequence analysisAdd BLAST301

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2624. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00550000074328.
HOGENOMiHOG000240694.
HOVERGENiHBG006265.
InParanoidiQ8K2A6.
KOiK19406.
OMAiMPREESK.
OrthoDBiEOG091G09AX.
PhylomeDBiQ8K2A6.
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]

Sequencei

Sequence statusi: Complete.

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

Q8K2A6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEILSRVWT VSHRVEIWLL ILVAYLLQRN VNSGHLPTKA ADPEAFMNVS
60 70 80 90 100
EIIKHKGYPS EEYEVATEDG YILSVNRIPR GQTRLKKEGS RPVVLLQHGL
110 120 130 140 150
LGDASNWISN LPNNSLGFIL ADAGFDVWMG NSRGNTWSRK HKTLSIDQDE
160 170 180 190 200
FWAFSYDEMA RFDLPAVINF ILQKTGQKKV YYVGYSQGTT MGFIAFSTMP
210 220 230 240 250
ELAHKIKMYF ALAPIATVKY ARSPGTKFLL LPDMMIKVLF GRQEFLYQTR
260 270 280 290 300
FFRQLFIYLC GQMILDQICS NIILLLGGFN TNNMNMSRAN VYVAHTPAGT
310 320 330 340 350
SVQNILHWSQ AVNSGELRAF DWGSETKNQE KCNQPTPIRY KVRDMMVPTA
360 370 380 390 400
MWTGGQDWLS NPDDVKTLLS EVTNLIYHKN IPEWAHVDFI WGLDAPQRVY
410 420
NEIIHLMKQE PNLPQGTCRV KL
Length:422
Mass (Da):48,254
Last modified:October 1, 2002 - v1
Checksum:iC6EFBC140963E051
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti72I → F in BAC29757 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK037091 mRNA. Translation: BAC29699.1.
AK037214 mRNA. Translation: BAC29757.1.
AK085719 mRNA. Translation: BAC39517.1.
BC031933 mRNA. Translation: AAH31933.1.
CCDSiCCDS50419.1.
RefSeqiNP_076392.1. NM_023903.1.
XP_006527529.1. XM_006527466.3.
UniGeneiMm.195937.

Genome annotation databases

EnsembliENSMUST00000025685; ENSMUSP00000025685; ENSMUSG00000056078.
GeneIDi78753.
KEGGimmu:78753.
UCSCiuc008hga.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK037091 mRNA. Translation: BAC29699.1.
AK037214 mRNA. Translation: BAC29757.1.
AK085719 mRNA. Translation: BAC39517.1.
BC031933 mRNA. Translation: AAH31933.1.
CCDSiCCDS50419.1.
RefSeqiNP_076392.1. NM_023903.1.
XP_006527529.1. XM_006527466.3.
UniGeneiMm.195937.

3D structure databases

ProteinModelPortaliQ8K2A6.
SMRiQ8K2A6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025685.

Protein family/group databases

ESTHERimouse-LIPM. Acidic_Lipase.
MEROPSiS33.A58.

PTM databases

iPTMnetiQ8K2A6.
PhosphoSitePlusiQ8K2A6.

Proteomic databases

PaxDbiQ8K2A6.
PRIDEiQ8K2A6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025685; ENSMUSP00000025685; ENSMUSG00000056078.
GeneIDi78753.
KEGGimmu:78753.
UCSCiuc008hga.2. mouse.

Organism-specific databases

CTDi340654.
MGIiMGI:1926003. Lipm.

Phylogenomic databases

eggNOGiKOG2624. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00550000074328.
HOGENOMiHOG000240694.
HOVERGENiHBG006265.
InParanoidiQ8K2A6.
KOiK19406.
OMAiMPREESK.
OrthoDBiEOG091G09AX.
PhylomeDBiQ8K2A6.
TreeFamiTF315485.

Enzyme and pathway databases

ReactomeiR-MMU-192456. Digestion of dietary lipid.

Miscellaneous databases

PROiQ8K2A6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000056078.
CleanExiMM_LIPM.
GenevisibleiQ8K2A6. MM.

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...

Entry informationi

Entry nameiLIPM_MOUSE
AccessioniPrimary (citable) accession number: Q8K2A6
Secondary accession number(s): Q8BJ28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 102 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. 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.