Reviewed, UniProtKB/Swiss-Prot Q9UT97 (PSA5_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable proteasome subunit alpha type-5
    EC=3.4.25.1

Gene names

ORF Names:

SPAC323.02c

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	247 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity By similarity.
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteasomal ubiquitin-dependent protein catabolic process Non-traceable author statement. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe proteasome core complex, alpha-subunit complex Inferred from electronic annotation. Source: InterPro
Molecular function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 247	247	Probable proteasome subunit alpha type-5		PRO_0000124128
Amino acid modifications
	Modified residue	55	1	Phosphothreonine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9UT97-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 713E1AB3A3ADE658	FASTA	247	27,573
	10 20 30 40 50 60 MFMTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGV KTKDAVVLGV EKRLTSPLME 70 80 90 100 110 120 SHSVEKLFEI DSHIGCAISG LTADARTIIE HARVQTQNHR FTYDEPQGIE STTQSICDLA 130 140 150 160 170 180 LRFGEGEDGE ERIMSRPFGV ALLIAGIDEH GPQLYHSEPS GTYFRYEAKA IGSGSEPAKS 190 200 210 220 230 240 ELVKEFHKDM TLEEAEVLIL KVLRQVMEEK LDSKNVQLAK VTAEGGFHIY NDEEMADAVA REQQRMD

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 THR-55, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB53405.1.
PIR	T38639.
RefSeq	NP_594372.1.
3D structure databases
SMR	Q9UT97. Positions 6-245.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UT97.
Protein family/group databases
MEROPS	T01.975.
Genome annotation databases
GeneID	2543205.
KEGG	spo:SPAC323.02c.
NMPDR	fig|4896.1.peg.4342.
Organism-specific databases
GeneDB_Spombe	SPAC323.02c.
Phylogenomic databases
eggNOG	fuNOG04476.
HOGENOM	HBG499923.
OMA	LMSRPFG.
OrthoDB	EOG9VX3NQ.
PhylomeDB	Q9UT97.
Enzyme and pathway databases
BRENDA	3.4.25.1. 653.
Gene expression databases
ArrayExpress	Q9UT97.
Family and domain databases
InterPro	IPR000426. Proteasome_asu_CS. IPR001353. Proteasome_sua/b. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view]
PROSITE	PS00388. PROTEASOME_A_1. 1 hit. PS51475. PROTEASOME_A_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PSA5_SCHPO

Accession

Primary (citable) accession number: Q9UT97

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)