Reviewed, UniProtKB/Swiss-Prot Q9P371 (SST2_SCHPO)

Names and origin

Protein names

Recommended name:
    AMSH-like protease sst2
    EC=3.1.2.15
Alternative name(s):
    Suppressor of ste12 deletion protein 2

Gene names

Name:	sst2
ORF Names:	SPAC19B12.10

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

General annotation (Comments)

Function	Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains By similarity. Plays a role in the multivesicular body (MVB) sorting pathway. Required for ubiquitin-dependent sorting of proteins into the endosome and subsequent trafficking to the vacuole. May regulate MVB sorting through deubiquitination of ubiquitinated ESCRT proteins. Ref.3
Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
Cofactor	Binds 2 zinc ion per subunit By similarity.
Subcellular location	Cytoplasm. Endosome Ref.2.
Domain	The JAMM motif is essential for the protease activity By similarity.
Sequence similarities	Belongs to the peptidase M67C family. Contains 1 MPN (JAB/Mov34) domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Endosome
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein targeting to vacuole during ubiquitin-dependent protein catabolic process via the MVB pathway Ref.3 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	endosome Non-traceable author statement. Source: GeneDB_SPombe
Molecular function	metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: EC zinc ion binding 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 – 435	435	AMSH-like protease sst2		PRO_0000358323
Regions
	Domain	258 – 367	110	MPN
	Motif	341 – 354	14	JAMM motif
Sites
	Metal binding	341	1	Zinc 1; catalytic By similarity
	Metal binding	343	1	Zinc 1; catalytic By similarity
	Metal binding	354	1	Zinc 1; catalytic By similarity
	Metal binding	356	1	Zinc 2 By similarity
	Metal binding	397	1	Zinc 2 By similarity
	Metal binding	404	1	Zinc 2 By similarity
	Metal binding	406	1	Zinc 2 By similarity
	Site	286	1	Indirect Zinc-binding By similarity
Amino acid modifications
	Modified residue	192	1	Phosphothreonine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9P371-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 94A674F36234A18B	FASTA	435	49,349
	10 20 30 40 50 60 MNILQGSEAP LSYEEIASRA GAFDFNKNIP LKNWLRTSTT ISKQAHVYVS EHDYSNGVFL 70 80 90 100 110 120 LFRYCELFMK CQKHPDAAAY KKELFDYYQG VRNALEEIEL IKPIVKEQYE QYQCQKNDLD 130 140 150 160 170 180 DLKKLSMKDS QPSLEKPVSY VDEPILEQWA LSDLQILPPS STDLLSPDSQ KLSKSSSDLP 190 200 210 220 230 240 QFDYPSLNSS PTFNSNLPIS SSRFEKTSLS DSKLVSPEPL DDNKDIQFIK KPIYTRTSEP 250 260 270 280 290 300 RPKPAGTFKI HAYTEGGKPL RTIYLPKLLK KVFLDVVKPN TKKNLETCGI LCGKLRQNAF 310 320 330 340 350 360 FITHLVIPLQ EATSDTCGTT DEASLFEFQD KHNLLTLGWI HTHPTQTCFM SSVDLHTHCS 370 380 390 400 410 420 YQLMLPEAIA IVMAPSKNTS GIFRLLDPEG LQTIVKCRKP GLFHPHEGKV YTMVAQPGHV 430 REINSKLQVV DLRVK

References

	« Hide 'large scale' referencesShow 'large scale' 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].
[3]	"Essential roles of class E Vps proteins for sorting into multivesicular bodies in Schizosaccharomyces pombe." Iwaki T., Onishi M., Ikeuchi M., Kita A., Sugiura R., Giga-Hama Y., Fukui Y., Takegawa K. Microbiology 153:2753-2764(2007) [PubMed: 17660439] [Abstract] Cited for: FUNCTION.
[4]	"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-192, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAC00558.1.
RefSeq	NP_594773.1.
3D structure databases
SMR	Q9P371. Positions 12-136, 260-392.
ModBase	Search...
Genome annotation databases
GeneID	2542606.
GenomeReviews	Gene locus sst2 in contig CU329670_GR.
KEGG	spo:SPAC19B12.10.
NMPDR	fig|4896.1.peg.4743.
Organism-specific databases
GeneDB_Spombe	SPAC19B12.10.
Phylogenomic databases
eggNOG	fuNOG07638.
HOGENOM	HBG318399.
OrthoDB	EOG9HB036.
PhylomeDB	Q9P371.
Gene expression databases
ArrayExpress	Q9P371.
Family and domain databases
InterPro	IPR000555. Mov34_MPN_PAD1. [Graphical view]
Pfam	PF01398. Mov34. 1 hit. [Graphical view]
SMART	SM00232. JAB_MPN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SST2_SCHPO

Accession

Primary (citable) accession number: Q9P371

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 1, 2000
Last modified:	January 19, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)