SST2_SCHPO
ID SST2_SCHPO Reviewed; 435 AA.
AC Q9P371;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=AMSH-like protease sst2;
DE EC=3.4.19.-;
DE AltName: Full=Suppressor of ste12 deletion protein 2;
GN Name=sst2; ORFNames=SPAC19B12.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION.
RX PubMed=17660439; DOI=10.1099/mic.0.2007/006072-0;
RA Iwaki T., Onishi M., Ikeuchi M., Kita A., Sugiura R., Giga-Hama Y.,
RA Fukui Y., Takegawa K.;
RT "Essential roles of class E Vps proteins for sorting into multivesicular
RT bodies in Schizosaccharomyces pombe.";
RL Microbiology 153:2753-2764(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-192, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-
CC linked polyubiquitin chains. Does not cleave 'Lys-48'-linked
CC polyubiquitin chains (By similarity). Plays a role in the
CC multivesicular body (MVB) sorting pathway. Required for ubiquitin-
CC dependent sorting of proteins into the endosome and subsequent
CC trafficking to the vacuole. May regulate MVB sorting through
CC deubiquitination of ubiquitinated ESCRT proteins. {ECO:0000250,
CC ECO:0000269|PubMed:17660439}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Endosome
CC {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The JAMM motif is essential for the protease activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67C family. {ECO:0000305}.
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DR EMBL; CU329670; CAC00558.1; -; Genomic_DNA.
DR RefSeq; NP_594773.1; NM_001020200.2.
DR PDB; 4JXE; X-ray; 1.45 A; A/B=245-435.
DR PDB; 4K1R; X-ray; 1.63 A; A/C=245-435.
DR PDB; 4MS7; X-ray; 1.67 A; A/B=245-435.
DR PDB; 4MSD; X-ray; 1.90 A; A/B=245-435.
DR PDB; 4MSJ; X-ray; 1.80 A; A/B/C=245-435.
DR PDB; 4MSM; X-ray; 1.74 A; A/C=245-435.
DR PDB; 4MSQ; X-ray; 1.95 A; A/C=245-435.
DR PDB; 4NQL; X-ray; 2.30 A; A=221-435.
DR PDB; 4PQT; X-ray; 2.05 A; A=245-435.
DR PDB; 4ZD4; X-ray; 1.63 A; A/B=245-435.
DR PDB; 4ZD5; X-ray; 2.07 A; A/B=245-435.
DR PDB; 4ZFR; X-ray; 1.72 A; A=245-435.
DR PDB; 4ZFT; X-ray; 2.30 A; A/C=245-435.
DR PDB; 7LM3; X-ray; 2.70 A; A/B=245-435.
DR PDBsum; 4JXE; -.
DR PDBsum; 4K1R; -.
DR PDBsum; 4MS7; -.
DR PDBsum; 4MSD; -.
DR PDBsum; 4MSJ; -.
DR PDBsum; 4MSM; -.
DR PDBsum; 4MSQ; -.
DR PDBsum; 4NQL; -.
DR PDBsum; 4PQT; -.
DR PDBsum; 4ZD4; -.
DR PDBsum; 4ZD5; -.
DR PDBsum; 4ZFR; -.
DR PDBsum; 4ZFT; -.
DR PDBsum; 7LM3; -.
DR AlphaFoldDB; Q9P371; -.
DR SMR; Q9P371; -.
DR BioGRID; 279060; 5.
DR STRING; 4896.SPAC19B12.10.1; -.
DR MEROPS; M67.A14; -.
DR iPTMnet; Q9P371; -.
DR MaxQB; Q9P371; -.
DR PaxDb; Q9P371; -.
DR PRIDE; Q9P371; -.
DR EnsemblFungi; SPAC19B12.10.1; SPAC19B12.10.1:pep; SPAC19B12.10.
DR PomBase; SPAC19B12.10; sst2.
DR VEuPathDB; FungiDB:SPAC19B12.10; -.
DR eggNOG; KOG2880; Eukaryota.
DR HOGENOM; CLU_023304_4_0_1; -.
DR InParanoid; Q9P371; -.
DR OMA; RQNAFFI; -.
DR PhylomeDB; Q9P371; -.
DR Reactome; R-SPO-5689901; Metalloprotease DUBs.
DR PRO; PR:Q9P371; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:PomBase.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IDA:PomBase.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IDA:PomBase.
DR GO; GO:0043130; F:ubiquitin binding; IPI:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IDA:PomBase.
DR GO; GO:0120113; P:cytoplasm to vacuole transport by the NVT pathway; IMP:PomBase.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:PomBase.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; EXP:PomBase.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:PomBase.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:PomBase.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:PomBase.
DR CDD; cd08066; MPN_AMSH_like; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR InterPro; IPR015063; USP8_dimer.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endosome; Hydrolase; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..435
FT /note="AMSH-like protease sst2"
FT /id="PRO_0000358323"
FT DOMAIN 262..392
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 162..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 341..354
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 286
FT /note="Indirect zinc-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 192
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:4JXE"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:4JXE"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:4JXE"
FT STRAND 299..307
FT /evidence="ECO:0007829|PDB:4JXE"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:4K1R"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:4K1R"
FT HELIX 323..331
FT /evidence="ECO:0007829|PDB:4JXE"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:4JXE"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:4JXE"
FT HELIX 352..364
FT /evidence="ECO:0007829|PDB:4JXE"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:4JXE"
FT TURN 375..378
FT /evidence="ECO:0007829|PDB:4JXE"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:4JXE"
FT HELIX 389..396
FT /evidence="ECO:0007829|PDB:4JXE"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:4K1R"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:4JXE"
FT TURN 416..419
FT /evidence="ECO:0007829|PDB:4JXE"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:4JXE"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:4JXE"
SQ SEQUENCE 435 AA; 49349 MW; 94A674F36234A18B CRC64;
MNILQGSEAP LSYEEIASRA GAFDFNKNIP LKNWLRTSTT ISKQAHVYVS EHDYSNGVFL
LFRYCELFMK CQKHPDAAAY KKELFDYYQG VRNALEEIEL IKPIVKEQYE QYQCQKNDLD
DLKKLSMKDS QPSLEKPVSY VDEPILEQWA LSDLQILPPS STDLLSPDSQ KLSKSSSDLP
QFDYPSLNSS PTFNSNLPIS SSRFEKTSLS DSKLVSPEPL DDNKDIQFIK KPIYTRTSEP
RPKPAGTFKI HAYTEGGKPL RTIYLPKLLK KVFLDVVKPN TKKNLETCGI LCGKLRQNAF
FITHLVIPLQ EATSDTCGTT DEASLFEFQD KHNLLTLGWI HTHPTQTCFM SSVDLHTHCS
YQLMLPEAIA IVMAPSKNTS GIFRLLDPEG LQTIVKCRKP GLFHPHEGKV YTMVAQPGHV
REINSKLQVV DLRVK
