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Q8WTS1 (ABHD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-acylglycerol-3-phosphate O-acyltransferase ABHD5

EC=2.3.1.51
Alternative name(s):
Abhydrolase domain-containing protein 5
Lipid droplet-binding protein CGI-58
Gene names
Name:ABHD5
Synonyms:NCIE2
ORF Names:CGI-58
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lysophosphatidic acid acyltransferase which functions in phosphatidic acid biosynthesis. May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2. Involved in keratinocyte differentiation. Ref.7 Ref.8 Ref.9

Catalytic activity

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. Ref.9

Subunit structure

Interacts with ADRP, PLIN and PNPLA2. Interacts with PLIN5; promotes interaction with PNPLA2 By similarity.

Subcellular location

Cytoplasm. Lipid droplet By similarity. Note: Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA By similarity. Ref.8

Tissue specificity

Widely expressed in various tissues, including lymphocytes, liver, skeletal muscle and brain. Expressed by upper epidermal layers and dermal fibroblasts in skin, hepatocytes and neurons (at protein level). Ref.1 Ref.8

Developmental stage

Detected in fetal epidermis from 49 to 135 days estimated gestational age (at protein level). Ref.8

Induction

Up-regulated upon keratinocyte differentiation (at protein level). Ref.8

Domain

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity.

Involvement in disease

Chanarin-Dorfman syndrome (CDS) [MIM:275630]: An autosomal recessive inborn error of lipid metabolism with multisystemic accumulation of triglycerides although plasma concentrations are normal. Clinical characteristics are congenital generalized ichthyosis, vacuolated leukocytes, hepatomegaly, myopathy, cataracts, neurosensory hearing loss and developmental delay. The disorder presents at birth with generalized, fine, white scaling of the skin and a variable degree of erythema resembling non-bullous congenital ichthyosiform erythroderma.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.7 Ref.9 Ref.12

Sequence similarities

Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.

Ontologies

Keywords
   Biological processDifferentiation
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Phospholipid biosynthesis
Phospholipid metabolism
   Cellular componentCytoplasm
Lipid droplet
   DiseaseCataract
Deafness
Disease mutation
Ichthyosis
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

fatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of sequestering of triglyceride

Inferred from direct assay Ref.7. Source: UniProtKB

phosphatidic acid biosynthetic process

Inferred from direct assay Ref.9. Source: UniProtKB

positive regulation of lipoprotein lipase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of triglyceride catabolic process

Inferred from direct assay Ref.7. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride catabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

lipid particle

Inferred from direct assay PubMed 21498505. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_function1-acylglycerol-3-phosphate O-acyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

lysophosphatidic acid acyltransferase activity

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 3493481-acylglycerol-3-phosphate O-acyltransferase ABHD5
PRO_0000080866

Regions

Motif327 – 3326HXXXXD motif

Amino acid modifications

Modified residue21N-acetylalanine Ref.10

Natural variations

Natural variant71E → K in CDS. Ref.1
Corresponds to variant rs104893676 [ dbSNP | Ensembl ].
VAR_023387
Natural variant721I → T.
Corresponds to variant rs2302349 [ dbSNP | Ensembl ].
VAR_037574
Natural variant821H → R Found in a patient with CDS but without evidence it may cause the disease. Ref.11
VAR_057953
Natural variant1151S → G in CDS. Ref.12
VAR_057954
Natural variant1301Q → P in CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity. Ref.1 Ref.7 Ref.9
Corresponds to variant rs28939077 [ dbSNP | Ensembl ].
VAR_023388
Natural variant2601E → K in CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity. Ref.1 Ref.7 Ref.9
Corresponds to variant rs28939078 [ dbSNP | Ensembl ].
VAR_023389

Experimental info

Sequence conflict2631F → S in AAD34053. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8WTS1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 85958A2DEC169C82

FASTA34939,096
        10         20         30         40         50         60 
MAAEEEEVDS ADTGERSGWL TGWLPTWCPT SISHLKEAEE KMLKCVPCTY KKEPVRISNG 

        70         80         90        100        110        120 
NKIWTLKFSH NISNKTPLVL LHGFGGGLGL WALNFGDLCT NRPVYAFDLL GFGRSSRPRF 

       130        140        150        160        170        180 
DSDAEEVENQ FVESIEEWRC ALGLDKMILL GHNLGGFLAA AYSLKYPSRV NHLILVEPWG 

       190        200        210        220        230        240 
FPERPDLADQ DRPIPVWIRA LGAALTPFNP LAGLRIAGPF GLSLVQRLRP DFKRKYSSMF 

       250        260        270        280        290        300 
EDDTVTEYIY HCNVQTPSGE TAFKNMTIPY GWAKRPMLQR IGKMHPDIPV SVIFGARSCI 

       310        320        330        340 
DGNSGTSIQS LRPHSYVKTI AILGAGHYVY ADQPEEFNQK VKEICDTVD 

« Hide

References

« Hide 'large scale' references
[1]"Mutations in CGI-58, the gene encoding a new protein of the esterase/lipase/thioesterase subfamily, in Chanarin-Dorfman syndrome."
Lefevre C., Jobard F., Caux F., Bouadjar B., Karaduman A., Heilig R., Lakhdar H., Wollenberg A., Verret J.-L., Weissenbach J., Oezguec M., Lathrop M., Prud'homme J.-F., Fischer J.
Am. J. Hum. Genet. 69:1002-1012(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, VARIANTS CDS LYS-7; PRO-130 AND LYS-260.
[2]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Substantia nigra.
[4]"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].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Skin.
[7]"Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome."
Lass A., Zimmermann R., Haemmerle G., Riederer M., Schoiswohl G., Schweiger M., Kienesberger P., Strauss J.G., Gorkiewicz G., Zechner R.
Cell Metab. 3:309-319(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION OF VARIANTS CDS PRO-130 AND LYS-260.
[8]"CGI-58 is an alpha/beta-hydrolase within lipid transporting lamellar granules of differentiated keratinocytes."
Akiyama M., Sakai K., Takayama C., Yanagi T., Yamanaka Y., McMillan J.R., Shimizu H.
Am. J. Pathol. 173:1349-1360(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
[9]"CGI-58, the causative gene for Chanarin-Dorfman syndrome, mediates acylation of lysophosphatidic acid."
Ghosh A.K., Ramakrishnan G., Chandramohan C., Rajasekharan R.
J. Biol. Chem. 283:24525-24533(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANTS CDS PRO-130 AND LYS-260.
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Two new mutations of the ABHD5 gene in a new adult case of Chanarin Dorfman syndrome: an uncommon lipid storage disease."
Schleinitz N., Fischer J., Sanchez A., Veit V., Harle J.-R., Pelissier J.-F.
Arch. Dermatol. 141:798-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-82.
[12]"A novel S115G mutation of CGI-58 in a Turkish patient with Dorfman-Chanarin syndrome."
Ben Selma Z., Yilmaz S., Schischmanoff P.O., Blom A., Ozogul C., Laroche L., Caux F.
J. Invest. Dermatol. 127:2273-2276(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDS GLY-115.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL606838 Genomic DNA. Translation: CAD12731.1.
AF151816 mRNA. Translation: AAD34053.1.
AK313811 mRNA. Translation: BAG36547.1.
AC105903 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64699.1.
BC021958 mRNA. Translation: AAH21958.1.
CCDSCCDS2711.1.
RefSeqNP_057090.2. NM_016006.4.
UniGeneHs.19385.

3D structure databases

ProteinModelPortalQ8WTS1.
SMRQ8WTS1. Positions 70-242.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119288. 5 interactions.
IntActQ8WTS1. 3 interactions.
MINTMINT-4650384.
STRING9606.ENSP00000390849.

Protein family/group databases

MEROPSS33.975.

PTM databases

PhosphoSiteQ8WTS1.

Polymorphism databases

DMDM73921640.

Proteomic databases

MaxQBQ8WTS1.
PaxDbQ8WTS1.
PeptideAtlasQ8WTS1.
PRIDEQ8WTS1.

Protocols and materials databases

DNASU51099.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000458276; ENSP00000390849; ENSG00000011198.
GeneID51099.
KEGGhsa:51099.
UCSCuc003cmx.3. human.

Organism-specific databases

CTD51099.
GeneCardsGC03P043707.
HGNCHGNC:21396. ABHD5.
HPACAB020685.
HPA035851.
HPA035852.
MIM275630. phenotype.
604780. gene.
neXtProtNX_Q8WTS1.
Orphanet98907. Dorfman-Chanarin disease.
PharmGKBPA134891622.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0596.
HOGENOMHOG000007445.
HOVERGENHBG054445.
InParanoidQ8WTS1.
KOK13699.
OMAPWGFAEK.
PhylomeDBQ8WTS1.
TreeFamTF314196.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ8WTS1.
BgeeQ8WTS1.
CleanExHS_ABHD5.
GenevestigatorQ8WTS1.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PRINTSPR00111. ABHYDROLASE.
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

GeneWikiABHD5.
GenomeRNAi51099.
NextBio53805.
PROQ8WTS1.
SOURCESearch...

Entry information

Entry nameABHD5_HUMAN
AccessionPrimary (citable) accession number: Q8WTS1
Secondary accession number(s): B2R9K0, Q9Y369
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 117 of the entry and version 1 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