Reviewed, UniProtKB/Swiss-Prot Q9DBL9 (ABHD5_MOUSE)

Names and origin

Protein names

Recommended 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
      Short name=Protein CGI-58

Gene names

Name:

Abhd5

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Evidence 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.4
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
Subunit structure	Interacts with ADRP By similarity. Interacts with PLIN. Interacts with and PNPLA2. Ref.4 Ref.3
Subcellular location	Cytoplasm. Lipid droplet. 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. Ref.3 Ref.5 Ref.6
Tissue specificity	Highly expressed in the adipose tissue and testes. Weakly expressed in the liver, muscle, kidney, and heart. Expressed by upper epidermal layers and dermal fibroblasts in skin, hepatocytes and hypothalamus in brain (at protein level). Ref.4 Ref.3 Ref.5
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.
Sequence similarities	Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.

Ontologies

Keywords
Biological process	Differentiation Fatty acid metabolism Lipid metabolism Phospholipid biosynthesis
Cellular component	Cytoplasm Lipid droplet
Coding sequence diversity	Alternative splicing
Disease	Cataract Deafness Disease mutation Ichthyosis
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	cell 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 Ref.4 Inferred from direct assay. Source: UniProtKB phosphatidic acid biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of lipoprotein lipase activity Inferred from direct assay. Source: MGI positive regulation of triglyceride catabolic process Ref.4 Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Ref.3 Ref.6 Inferred from direct assay. Source: UniProtKB monolayer-surrounded lipid storage body Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-acylglycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: EC protein binding Ref.4 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9DBL9-1)

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: Q9DBL9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     19-171: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 351	351	1-acylglycerol-3-phosphate O-acyltransferase ABHD5		PRO_0000080867
Regions
	Motif	329 – 334	6	HXXXXD motif
Natural variations
	Alternative sequence	19 – 171	153	Missing in isoform 2.		VSP_015345

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 04068BFB77D33E67	FASTA	351	39,155
	10 20 30 40 50 60 MKAMAAEEEV DSADAGGGSG WLTGWLPTWC PTSTSHLKEA EEKMLKCVPC TYKKEPVRIS 70 80 90 100 110 120 NGNRIWTLMF SHNISSKTPL VLLHGFGGGL GLWALNFEDL STDRPVYAFD LLGFGRSSRP 130 140 150 160 170 180 RFDSDAEEVE NQFVESIEEW RCALRLDKMI LLGHNLGGFL AAAYSLKYPS RVSHLILVEP 190 200 210 220 230 240 WGFPERPDLA DQERPIPVWI RALGAALTPF NPLAGLRIAG PFGLSLVQRL RPDFKRKYSS 250 260 270 280 290 300 MFEDDTVTEY IYHCNVQTPS GETAFKNMTI PYGWAKRPML QRIGGLHPDI PVSVIFGARS 310 320 330 340 350 CIDGNSGTSI QSLRPKSYVK TIAILGAGHY VYADQPEEFN QKVKEICHTV D
	Isoform 2. Checksum: 724796B08B1653D0	FASTA	198	21,846
	10 20 30 40 50 60 MKAMAAEEEV DSADAGGGVS HLILVEPWGF PERPDLADQE RPIPVWIRAL GAALTPFNPL 70 80 90 100 110 120 AGLRIAGPFG LSLVQRLRPD FKRKYSSMFE DDTVTEYIYH CNVQTPSGET AFKNMTIPYG 130 140 150 160 170 180 WAKRPMLQRI GGLHPDIPVS VIFGARSCID GNSGTSIQSL RPKSYVKTIA ILGAGHYVYA 190 DQPEEFNQKV KEICHTVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Liver.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N. Tissue: Colon and Mammary gland.
[3]	"Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in 3T3-L1 adipocytes." Subramanian V., Rothenberg A., Gomez C., Cohen A.W., Garcia A., Bhattacharyya S., Shapiro L., Dolios G., Wang R., Lisanti M.P., Brasaemle D.L. J. Biol. Chem. 279:42062-42071(2004) [PubMed: 15292255] [Abstract] Cited for: INTERACTION WITH PLIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]	"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: 16679289] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PLIN AND PNPLA2.
[5]	"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: 18832586] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]	"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: 18606822] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK004873 mRNA. Translation: BAB23632.1. AK019488 mRNA. Translation: BAB31755.2. AK050377 mRNA. Translation: BAC34220.1. BC037063 mRNA. Translation: AAH37063.1.
IPI	IPI00119852. IPI00623458.
RefSeq	NP_080455.1.
UniGene	Mm.280254
3D structure databases
SMR	Q9DBL9. Positions 16-180, 47-349.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9DBL9.
Protein family/group databases
MEROPS	S33.975.
Proteomic databases
PRIDE	Q9DBL9.
Genome annotation databases
Ensembl	ENSMUST00000035128; ENSMUSP00000035128; ENSMUSG00000032540; Mus musculus. [Genome view] ENSMUST00000111497; ENSMUSP00000107123; ENSMUSG00000032540; Mus musculus. [Genome view]
GeneID	67469.
KEGG	mmu:67469.
NMPDR	fig|10090.3.peg.21086.
UCSC	uc009sew.1. mouse. uc009sey.1. mouse.
Organism-specific databases
CTD	67469.
MGI	MGI:1914719. Abhd5.
Phylogenomic databases
HOGENOM	HBG522421.
HOVERGEN	Q9DBL9.
InParanoid	Q9DBL9.
OMA	LNFGDLC.
OrthoDB	EOG9M949V.
PhylomeDB	Q9DBL9.
Gene expression databases
ArrayExpress	Q9DBL9.
Bgee	Q9DBL9.
CleanEx	MM_ABHD5.
Genevestigator	Q9DBL9.
GermOnline	ENSMUSG00000032540. Mus musculus.
Family and domain databases
InterPro	IPR000073. AB_hydrolase_1. [Graphical view]
Pfam	PF00561. Abhydrolase_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	324670.
SOURCE	Search...

Entry information

Entry name

ABHD5_MOUSE

Accession

Primary (citable) accession number: Q9DBL9
Secondary accession number(s): Q9CTY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	June 1, 2001
Last modified:	February 9, 2010
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)