Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipase member N

Gene

LIPN

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 sitei173 – 1731NucleophileBy similarity
Active sitei344 – 3441Charge relay systemPROSITE-ProRule annotation
Active sitei373 – 3731Charge 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-LIPN. Acidic_Lipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase member N (EC:3.1.1.-)
Alternative name(s):
Lipase-like abhydrolase domain-containing protein 4
Gene namesi
Name:LIPN
Synonyms:LIPL4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:23452. LIPN.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Ichthyosis, congenital, autosomal recessive 8 (ARCI8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs.
See also OMIM:613943

Keywords - Diseasei

Ichthyosis

Organism-specific databases

MalaCardsiLIPN.
MIMi613943. phenotype.
Orphaneti313. Lamellar ichthyosis.
PharmGKBiPA162394123.

Polymorphism and mutation databases

BioMutaiLIPN.
DMDMi147647785.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 398380Lipase member NPRO_0000286831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi247 ↔ 256By similarity
Glycosylationi272 – 2721N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ5VXI9.
PRIDEiQ5VXI9.

Expressioni

Tissue specificityi

Highly expressed in the epidermis in the granular keratinocytes. Also detected in other tissues, although at much lower levels, including lung and spleen.2 Publications

Developmental stagei

Up-regulated during epidermal differentiation.1 Publication

Gene expression databases

BgeeiQ5VXI9.
CleanExiHS_LIPN.

Organism-specific databases

HPAiHPA039997.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000383923.

Structurei

3D structure databases

ProteinModelPortaliQ5VXI9.
SMRiQ5VXI9. Positions 29-394.
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.
InParanoidiQ5VXI9.
OMAiMSLWAGS.
OrthoDBiEOG71RXJN.
PhylomeDBiQ5VXI9.
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.

Q5VXI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMWLLLTTTC LICGTLNAGG FLDLENEVNP EVWMNTSEII IYNGYPSEEY
60 70 80 90 100
EVTTEDGYIL LVNRIPYGRT HARSTGPRPV VYMQHALFAD NAYWLENYAN
110 120 130 140 150
GSLGFLLADA GYDVWMGNSR GNTWSRRHKT LSETDEKFWA FSFDEMAKYD
160 170 180 190 200
LPGVIDFIVN KTGQEKLYFI GHSLGTTIGF VAFSTMPELA QRIKMNFALG
210 220 230 240 250
PTISFKYPTG IFTRFFLLPN SIIKAVFGTK GFFLEDKKTK IASTKICNNK
260 270 280 290 300
ILWLICSEFM SLWAGSNKKN MNQSRMDVYM SHAPTGSSVH NILHIKQLYH
310 320 330 340 350
SDEFRAYDWG NDADNMKHYN QSHPPIYDLT AMKVPTAIWA GGHDVLVTPQ
360 370 380 390
DVARILPQIK SLHYFKLLPD WNHFDFVWGL DAPQRMYSEI IALMKAYS
Length:398
Mass (Da):45,534
Last modified:May 15, 2007 - v2
Checksum:i0EE99ED08A5F5978
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti244 – 2441T → N.
Corresponds to variant rs10788611 [ dbSNP | Ensembl ].
VAR_032192

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF426483 mRNA. Translation: ABR08388.1.
AL358532 Genomic DNA. Translation: CAH71060.2.
CCDSiCCDS44456.1.
RefSeqiNP_001095939.1. NM_001102469.1.
XP_005270106.1. XM_005270049.2.
XP_011538385.1. XM_011540083.1.
XP_011538386.1. XM_011540084.1.
UniGeneiHs.632091.

Genome annotation databases

EnsembliENST00000404459; ENSP00000383923; ENSG00000204020.
GeneIDi643418.
KEGGihsa:643418.
UCSCiuc010qmw.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF426483 mRNA. Translation: ABR08388.1.
AL358532 Genomic DNA. Translation: CAH71060.2.
CCDSiCCDS44456.1.
RefSeqiNP_001095939.1. NM_001102469.1.
XP_005270106.1. XM_005270049.2.
XP_011538385.1. XM_011540083.1.
XP_011538386.1. XM_011540084.1.
UniGeneiHs.632091.

3D structure databases

ProteinModelPortaliQ5VXI9.
SMRiQ5VXI9. Positions 29-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000383923.

Protein family/group databases

ESTHERihuman-LIPN. Acidic_Lipase.

Polymorphism and mutation databases

BioMutaiLIPN.
DMDMi147647785.

Proteomic databases

PaxDbiQ5VXI9.
PRIDEiQ5VXI9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000404459; ENSP00000383923; ENSG00000204020.
GeneIDi643418.
KEGGihsa:643418.
UCSCiuc010qmw.2. human.

Organism-specific databases

CTDi643418.
GeneCardsiLIPN.
HGNCiHGNC:23452. LIPN.
HPAiHPA039997.
MalaCardsiLIPN.
MIMi613924. gene.
613943. phenotype.
neXtProtiNX_Q5VXI9.
Orphaneti313. Lamellar ichthyosis.
PharmGKBiPA162394123.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2624. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00550000074328.
HOGENOMiHOG000240694.
HOVERGENiHBG006265.
InParanoidiQ5VXI9.
OMAiMSLWAGS.
OrthoDBiEOG71RXJN.
PhylomeDBiQ5VXI9.
TreeFamiTF315485.

Enzyme and pathway databases

ReactomeiR-HSA-192456. Digestion of dietary lipid.

Miscellaneous databases

GenomeRNAii643418.
PROiQ5VXI9.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VXI9.
CleanExiHS_LIPN.

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], 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. "A mutation in LIPN, encoding epidermal lipase N, causes a late-onset form of autosomal-recessive congenital ichthyosis."
    Israeli S., Khamaysi Z., Fuchs-Telem D., Nousbeck J., Bergman R., Sarig O., Sprecher E.
    Am. J. Hum. Genet. 88:482-487(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ARCI8, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiLIPN_HUMAN
AccessioniPrimary (citable) accession number: Q5VXI9
Secondary accession number(s): A7KIH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: June 8, 2016
This is version 94 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.