Q6E213 (AWAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-CoA wax alcohol acyltransferase 2
EC=2.3.1.75

Alternative name(s):
Acyl-CoA retinol O-fatty-acyltransferase
Short name=ARAT
Short name=Retinol O-fatty-acyltransferase
EC=2.3.1.76
Diacylglycerol O-acyltransferase 2-like protein 4
Diacylglycerol O-acyltransferase candidate 4
Short name=hDC4
Long-chain-alcohol O-fatty-acyltransferase 2
Multifunctional O-acyltransferase
Wax synthase
Short name=hWS

Gene names

Name:	AWAT2
Synonyms:	DC4, DGAT2L4, MFAT, WS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl-CoA:retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo. Ref.1 Ref.4 Ref.5
Catalytic activity	Acyl-CoA + a long-chain alcohol = CoA + a long-chain ester. Ref.5 Acyl-CoA + retinol = CoA + retinyl ester. Ref.5
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.
Tissue specificity	Abundant in tissues rich in sebaceous glands such as the preputial gland and eyelid. Highly expressed in skin, where it is primarily restricted to undifferentiated peripheral sebocytes. Also expressed at lower level in other tissues except pancreas. Ref.1 Ref.4 Ref.5
Sequence similarities	Belongs to the diacylglycerol acyltransferase family.
Biophysicochemical properties	Kinetic parameters: Vmax=1232 pmol/min/mg enzyme with [14C]cetyl-CoA as substrate Ref.4

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	wax biosynthetic process Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	long-chain-alcohol O-fatty-acyltransferase activity Inferred from electronic annotation. Source: EC retinol O-fatty-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 333	333	Acyl-CoA wax alcohol acyltransferase 2		PRO_0000249052
Regions
	Transmembrane	15 – 35	21	Helical; Potential
	Transmembrane	38 – 58	21	Helical; Potential
	Transmembrane	130 – 150	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6E213 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: B2F1BAAF331BAE4C	FASTA	333	38,094
	10 20 30 40 50 60 MLLPSKKDLK TALDVFAVFQ WSFSALLITT TVIAVNLYLV VFTPYWPVTV LILTWLAFDW 70 80 90 100 110 120 KTPQRGGRRF TCVRHWRLWK HYSDYFPLKL LKTHDICPSR NYILVCHPHG LFAHGWFGHF 130 140 150 160 170 180 ATEASGFSKI FPGITPYILT LGAFFWMPFL REYVMSTGAC SVSRSSIDFL LTHKGTGNMV 190 200 210 220 230 240 IVVIGGLAEC RYSLPGSSTL VLKNRSGFVR MALQHGVPLI PAYAFGETDL YDQHIFTPGG 250 260 270 280 290 300 FVNRFQKWFQ SMVHIYPCAF YGRGFTKNSW GLLPYSRPVT TIVGEPLPMP KIENPSQEIV 310 320 330 AKYHTLYIDA LRKLFDQHKT KFGISETQEL EII

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family." Cheng J.B., Russell D.W. J. Biol. Chem. 279:37798-37807(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-333. Tissue: Skin.
[3]	"Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals." Winter A., van Eckeveld M., Bininda-Emonds O.R.P., Habermann F.A., Fries R. Cytogenet. Genome Res. 102:42-47(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[4]	"Identification of two novel human Acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily." Turkish A.R., Henneberry A.L., Cromley D., Padamsee M., Oelkers P., Bazzi H., Christiano A.M., Billheimer J.T., Sturley S.L. J. Biol. Chem. 280:14755-14764(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[5]	"A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters." Yen C.-L.E., Brown C.H. IV, Monetti M., Farese R.V. Jr. J. Lipid Res. 46:2388-2397(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY605053 mRNA. Translation: AAT68764.1. BC063698 mRNA. Translation: AAH63698.1. BN000156 mRNA. Translation: CAD89267.1.
IPI	IPI00163334.
RefSeq	NP_001002254.1. NM_001002254.1.
UniGene	Hs.661507.
3D structure databases
ProteinModelPortal	Q6E213.
ModBase	Search...
PTM databases
PhosphoSite	Q6E213.
Polymorphism databases
DMDM	74748433.
Proteomic databases
PRIDE	Q6E213.
Protocols and materials databases
DNASU	158835.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000276101; ENSP00000421172; ENSG00000147160.
GeneID	158835.
KEGG	hsa:158835.
UCSC	uc004dxt.1. human.
Organism-specific databases
CTD	158835.
GeneCards	GC0XM069178.
HGNC	HGNC:23251. AWAT2.
neXtProt	NX_Q6E213.
PharmGKB	PA164716410.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HOG000179738.
HOVERGEN	HBG065791.
InParanoid	Q6E213.
KO	K11156.
OMA	NRFQKWF.
OrthoDB	EOG43TZVQ.
Enzyme and pathway databases
BRENDA	2.3.1.75. 2681.
Gene expression databases
ArrayExpress	Q6E213.
Bgee	Q6E213.
CleanEx	HS_DGAT2L4.
Genevestigator	Q6E213.
Family and domain databases
InterPro	IPR007130. DAGAT. [Graphical view]
PANTHER	PTHR12317. PTHR12317. 1 hit.
Pfam	PF03982. DAGAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	158835.
NextBio	87830.

Entry information

Entry name

AWAT2_HUMAN

Accession

Primary (citable) accession number: Q6E213
Secondary accession number(s): Q6IEE3, Q6P437

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	August 16, 2004
Last modified:	April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.