Reviewed, UniProtKB/Swiss-Prot O94511 (YN67_SCHPO)

Names and origin

Protein names

Recommended name:
    Putative enoyl reductase C646.07c
    EC=1.3.1.38

Gene names

ORF Names:

SPBC646.07c

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	295 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Ref.2
Sequence similarities	Belongs to the steroid 5-alpha reductase family.

Ontologies

Keywords
Biological process	Lipid synthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid elongation Non-traceable author statement. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	enoyl-[acyl-carrier-protein] reductase activity Non-traceable author statement. Source: GeneDB_SPombe trans-2-enoyl-CoA reductase (NADPH) 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 – 295	295	Putative enoyl reductase C646.07c		PRO_0000317698
Regions
	Topological domain	1 – 84	84	Cytoplasmic Potential
	Transmembrane	85 – 105	21	Potential
	Topological domain	106 – 157	52	Lumenal Potential
	Transmembrane	158 – 178	21	Potential
	Topological domain	179 – 186	8	Cytoplasmic Potential
	Transmembrane	187 – 207	21	Potential
	Topological domain	208 – 223	16	Lumenal Potential
	Transmembrane	224 – 246	23	Potential
	Topological domain	247 – 250	4	Cytoplasmic Potential
	Transmembrane	251 – 268	18	Potential
	Topological domain	269 – 295	27	Lumenal Potential

Sequences

	Sequence		Length	Mass (Da)
	O94511-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: B4181D13E0F3C333	FASTA	295	34,640
	10 20 30 40 50 60 MSITLSSRGR KIRKLPKSLE FPLDGSIDKL RDEVSSVTRL PVERLRFSTA DGTTLLPNTT 70 80 90 100 110 120 LRKYGVGPGA TIWVKDLGPQ IGWRTVFMIE YLGPLVIHLF FILNYKWIYR KDYNLCLNQK 130 140 150 160 170 180 IAFVLVMLHF MKREYESIFV HRFSLATMPL RNIFKNCAHY HLLSGLFLAY FIYGPWHAND 190 200 210 220 230 240 YIKPNHLLFL IVGWAFAVLS NFRTHIILRD LRPAGSKKRV IPTGYGFNLV SFPNYFFESL 250 260 270 280 290 GWLFFALLTK SWASWIFLFV GSAQMFVWAK KKHARYLKEF PNYPRSRKIM IPFFL

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]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA22811.1.
PIR	T40583.
RefSeq	NP_595365.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2541070.
KEGG	spo:SPBC646.07c.
NMPDR	fig|4896.1.peg.1231.
Organism-specific databases
GeneDB_Spombe	SPBC646.07c.
Phylogenomic databases
OMA	O94511. KSHPQWY.
Enzyme and pathway databases
BRENDA	1.3.1.38. 653.
Gene expression databases
ArrayExpress	O94511.
Family and domain databases
InterPro	IPR001104. 3-oxo-5_a-steroid_4-DH_C. [Graphical view]
Pfam	PF02544. Steroid_dh. 1 hit. [Graphical view]
PROSITE	PS50244. S5A_REDUCTASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

YN67_SCHPO

Accession

Primary (citable) accession number: O94511

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)