Q10071 (STE24_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable CAAX prenyl protease 1
EC=3.4.24.84

Alternative name(s):
Prenyl protein-specific endoprotease 1
Short name=PPSEP 1

Gene names

ORF Names:

SPAC3H1.05

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Proteolytically removes the C-terminal three residues of farnesylated proteins By similarity.
Catalytic activity	The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the peptidase M48A family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	CAAX-box protein processing Inferred from sequence or structural similarity. Source: GeneDB_Spombe proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 474	474	Probable CAAX prenyl protease 1		PRO_0000138847
Regions
	Transmembrane	103 – 123	21	Helical; Potential
	Transmembrane	196 – 216	21	Helical; Potential
	Transmembrane	230 – 250	21	Helical; Potential
	Transmembrane	344 – 364	21	Helical; Potential
	Transmembrane	381 – 401	21	Helical; Potential
Sites
	Active site	333	1	By similarity
	Active site	415	1	Proton donor By similarity
	Metal binding	332	1	Zinc; catalytic By similarity
	Metal binding	336	1	Zinc; catalytic By similarity
	Metal binding	411	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q10071 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 50AC2F96E25C76C5	FASTA	474	54,001
	10 20 30 40 50 60 MSPGLCFLKE ISVIQATPKP TTRSFANCCK MGILQHLMHI LDIPGFPWKI VIAGFSIGKY 70 80 90 100 110 120 AWDLYLRRRQ VPYLLREKPP AILAEHVDEK KYQKALSYAR DKSWFSTIVS TFTLAVDLLI 130 140 150 160 170 180 IKYDGLSYLW NITKFPWMDK LAASSSRFSL STSITHSCVF MFGLTLFSRL IQIPFNLYST 190 200 210 220 230 240 FVIEEKYGFN KSTLKIFVID LLKELSLGGL LMSVVVGVFV KILTKFGDNF IMYAWGAYIV 250 260 270 280 290 300 FGLILQTIAP SLIMPLFYKF TPLENGSLRT QIEELAASIN FPLKKLYVID ASRRSTHSNA 310 320 330 340 350 360 FFYGLPWNKG IVLFDTLVKN HTEPELIAIL GHELGHWYMS HNLINTIIDY GMSLFHLFLF 370 380 390 400 410 420 AAFIRNNSLY TSFNFITEKP VIVGLLLFSD ALGPLSSILT FASNKVSRLC EYQADAFAKQ 430 440 450 460 470 LGYAKDLGDG LIRIHDDNLS PLEFDSLYTS YYHSHPILVD RLNAIDYTTL KKNN

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: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAA92258.1.
PIR	T38737.
RefSeq	NP_593547.1. NM_001018980.1.
3D structure databases
ProteinModelPortal	Q10071.
ModBase	Search...
Protein-protein interaction databases
STRING	Q10071.
Protein family/group databases
MEROPS	M48.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC3H1.05.1; SPAC3H1.05.1:pep; SPAC3H1.05.
GeneID	2543456.
KEGG	spo:SPAC3H1.05.
NMPDR	fig|4896.1.peg.3517.
Organism-specific databases
GeneDB_Spombe	SPAC3H1.05.
Phylogenomic databases
eggNOG	fuNOG04614.
GeneTree	EFGT00050000006328.
HOGENOM	HBG435738.
OMA	SALHYTH.
OrthoDB	EOG4ZW8KQ.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001224-MONOMER.
Gene expression databases
ArrayExpress	Q10071.
Family and domain databases
InterPro	IPR001915. Peptidase_M48. [Graphical view]
KO	K06013.
Pfam	PF01435. Peptidase_M48. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

STE24_SCHPO

Accession

Primary (citable) accession number: Q10071

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	December 14, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program