Reviewed, UniProtKB/Swiss-Prot Q9UU82 (AREH2_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable sterol O-acyltransferase 2
    EC=2.3.1.26
Alternative name(s):
    Sterol-ester synthase 2

Gene names

ORF Names:

SPCP1E11.05c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Acyl-CoA + cholesterol = CoA + cholesterol ester.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cholesterol O-acyltransferase activity Inferred from electronic annotation. Source: EC ergosterol O-acyltransferase activity Inferred from electronic annotation. Source: EC lanosterol 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 – 472	472	Probable sterol O-acyltransferase 2		PRO_0000315968
Regions
	Transmembrane	61 – 81	21	Potential
	Transmembrane	111 – 131	21	Potential
	Transmembrane	135 – 155	21	Potential
	Transmembrane	170 – 190	21	Potential
	Transmembrane	262 – 282	21	Potential
	Transmembrane	317 – 337	21	Potential
	Transmembrane	452 – 472	21	Potential
Amino acid modifications
	Modified residue	12	1	Phosphoserine Ref.2
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	233	1	N-linked (GlcNAc...) Potential
	Glycosylation	342	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9UU82-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: C0325046AE97FAF8	FASTA	472	55,157
	10 20 30 40 50 60 MIAATPAKSK PSDVNLEQTF KGVSETSKID LRRSRAAYRP LELSPTPSIF ARNYQRNAVD 70 80 90 100 110 120 FTGFFVLFWV AVSIMIFMSF LENFELTGRP VVGTIFKYFQ SNLLDLAKAD LAMSSMFLLA 130 140 150 160 170 180 FPFQKIFALG YLRWYGLGVY LYSILILLFL SHCVLRCCLS NWSWTHRAMF ILHSMVILMK 190 200 210 220 230 240 LHSYNVVNGW YSYCYHSLNK LQSKKTDLDD DERSSVEFYE HCLNHHGNTY PENLTIPNAL 250 260 270 280 290 300 DFLFMPSLCY QLYYPRTAHV RIHYLIECAL GTFGCIFLLV IISDHFMVPV LAKAIRTIIE 310 320 330 340 350 360 APEDASATYF AIRLGHTVAF LMFPFMLSFL LVFWVIFEGV CNFSAEITRF ADRNFYDDWW 370 380 390 400 410 420 NCWTWDQFAR TWNKPVHYFL LRHVYVPLNS FMSKSLSTFF TFFVSSVLHE LVMGCITLKI 430 440 450 460 470 RGYGLFFQMT QIPYIIIQRQ KFVRRHRLLG NIAFWFSIII GIALIAALYI LF

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAB54864.1.
PIR	T41684.
RefSeq	NP_588558.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2538854.
KEGG	spo:SPCP1E11.05c.
NMPDR	fig|4896.1.peg.896.
Organism-specific databases
GeneDB_Spombe	SPCP1E11.05c.
Phylogenomic databases
OMA	QINYPRT.
Enzyme and pathway databases
BRENDA	2.3.1.26. 653.
Gene expression databases
ArrayExpress	Q9UU82.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. [Graphical view]
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AREH2_SCHPO

Accession

Primary (citable) accession number: Q9UU82

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)