P84285 (ARE2_CANAX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sterol O-acyltransferase 2
EC=2.3.1.26

Alternative name(s):
ASAT
Sterol-ester synthase

Gene names

Name:

ARE2

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	609 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Acyl-CoA + cholesterol = CoA + cholesterol ester. Ref.1
Enzyme regulation	Inhibited by the protoberberine derivative HWY-289 in a non-competitive manner. Inhibited by miconazole. Not inhibited by CI-976, polyoxin D, amphotericin B or nikkomycin Z. Ref.1
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.
Induction	Transcription is induced by HWY-289, but not by CI-976. HWY-289 may deplete protein levels causing an increase in transcription. Ref.1
Sequence similarities	Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	cholesterol metabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Inferred from direct assay Ref.1. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cholesterol O-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 – 609	609	Sterol O-acyltransferase 2		PRO_0000207649
Regions
	Transmembrane	152 – 172	21	Helical; Potential
	Transmembrane	195 – 215	21	Helical; Potential
	Transmembrane	229 – 249	21	Helical; Potential
	Transmembrane	253 – 273	21	Helical; Potential
	Transmembrane	402 – 422	21	Helical; Potential
	Transmembrane	451 – 471	21	Helical; Potential
	Transmembrane	534 – 554	21	Helical; Potential
	Transmembrane	589 – 609	21	Helical; Potential
Sites
	Active site	546	1	Potential UniProtKB P53629

Sequences

	Sequence		Length	Mass (Da)
	P84285 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: 884CD6EEAD9C7430	FASTA	609	71,347
	10 20 30 40 50 60 MGRTNTSDQL NAISDKNTKR KSLALDNEYH NNSSSEDDSS KIELSYTIPD NNNIISQETT 70 80 90 100 110 120 TSVEDVLSLS SAPQNELRLR KQKSNNQDSP VDLNGVIVDV SKREKIFLKR KRQIDNKHGS 130 140 150 160 170 180 DKSKYLSRFN DITFKAKSST IFESDEFYKT DFFGMYVLFW LATAFAMVNN LIHTYFENST 190 200 210 220 230 240 PILQWTVVKV FKRDLFKVGL VDLAMYLSTY FAFFVQYACK NGYLSWKKVG WWLQAAFDGL 250 260 270 280 290 300 FLFFWLWIAS EYCLDFPWIA KVFLVLHSLV FIMKMHSYAF YNGYLWSIYK EGLYSEKYLD 310 320 330 340 350 360 KLTNGKVTLP KGHTKNETEK VLQESIAFTK YELEYQSHAT TENPDDHHVF DIDQTDKSIA 370 380 390 400 410 420 KLQQEGLIKF PQNITLFNYF EYSMFPTLVY TLNFPRTKRI RWSYVFGKTF GIFGLIFLMI 430 440 450 460 470 480 LIAENNLYPI VLRCEIARKL PVSERIPQYF FLLMDMIPPF LMVYLFTFFL IWDAILNAIA 490 500 510 520 530 540 ELSKFADRDF YGPWWSCTDF SEFANQWNRC VHKFLLRHVY HSSISAFDVN KQSAAIITFL 550 560 570 580 590 600 LSSLVHELVM YVIFGTLRGY LLLFQMSQIP LIIMSRSKFM KDKKVLGNII CWFGFISGPS IICTLYLVF

References

[1]

"Molecular cloning and biochemical characterization of Candida albicans acyl-CoA:sterol acyltransferase, a potential target of antifungal agents." Kim K.-Y., Shin Y.-K., Park J.-C., Kim J.-H., Yang H., Han D.-M., Paik Y.-K. Biochem. Biophys. Res. Commun. 319:911-919(2004) [PubMed: 15184069] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, INDUCTION. Strain: ATCC 10231 / CBS 6431 / DSM 1386 / NBRC 1594.

Cross-references

3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P84285.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR004299. MBOAT_fam. IPR014371. Oat_ACAT_DAG_ARE. [Graphical view]
PANTHER	PTHR10408. PTHR10408. 1 hit.
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
PIRSF	PIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARE2_CANAX

Accession

Primary (citable) accession number: P84285

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	December 7, 2004
Last modified:	October 19, 2011
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program