ID   UBP6_SCHPO              Reviewed;         468 AA.
AC   Q92353;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 6;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 6;
DE   AltName: Full=Ubiquitin thiollesterase 6;
DE   AltName: Full=Ubiquitin-specific-processing protease 6;
GN   Name=ubp6; ORFNames=SPAC6G9.08;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   FUNCTION, INTERACTION WITH RPN1, AND SUBCELLULAR LOCATION.
RX   PubMed=15533439; DOI=10.1016/j.jmb.2004.09.057;
RA   Stone M., Hartmann-Petersen R., Seeger M., Bech-Otschir D., Wallace M.,
RA   Gordon C.;
RT   "Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S
RT   proteasome in fission yeast.";
RL   J. Mol. Biol. 344:697-706(2004).
RN   [4]
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).
CC   -!- FUNCTION: Ubiquitin-protein hydrolase is involved both in the
CC       processing of ubiquitin precursors and of ubiquitinated proteins. This
CC       enzyme is a thiol protease that recognizes and hydrolyzes a peptide
CC       bond at the C-terminal glycine of ubiquitin.
CC       {ECO:0000269|PubMed:15533439}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12;
CC   -!- SUBUNIT: Component of the 26S proteasome. Interacts with rpn1.
CC       {ECO:0000269|PubMed:15533439}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15533439,
CC       ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP14/UBP6 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAB03610.2; -; Genomic_DNA.
DR   PIR; T39070; T39070.
DR   RefSeq; NP_594117.2; NM_001019541.2.
DR   AlphaFoldDB; Q92353; -.
DR   SMR; Q92353; -.
DR   BioGRID; 278310; 63.
DR   STRING; 284812.Q92353; -.
DR   MEROPS; C19.A60; -.
DR   iPTMnet; Q92353; -.
DR   SwissPalm; Q92353; -.
DR   MaxQB; Q92353; -.
DR   PaxDb; 4896-SPAC6G9-08-1; -.
DR   EnsemblFungi; SPAC6G9.08.1; SPAC6G9.08.1:pep; SPAC6G9.08.
DR   GeneID; 2541819; -.
DR   KEGG; spo:SPAC6G9.08; -.
DR   PomBase; SPAC6G9.08; ubp6.
DR   VEuPathDB; FungiDB:SPAC6G9.08; -.
DR   eggNOG; KOG1872; Eukaryota.
DR   HOGENOM; CLU_017549_2_1_1; -.
DR   InParanoid; Q92353; -.
DR   OMA; RKVQFPF; -.
DR   Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR   PRO; PR:Q92353; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005654; C:nucleoplasm; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; HDA:PomBase.
DR   GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:PomBase.
DR   GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR   CDD; cd02657; Peptidase_C19A; 1.
DR   CDD; cd16104; Ubl_USP14_like; 1.
DR   Gene3D; 6.10.140.1140; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF1; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..468
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 6"
FT                   /id="PRO_0000080607"
FT   DOMAIN          1..71
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          101..465
FT                   /note="USP"
FT   ACT_SITE        110
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        415
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
SQ   SEQUENCE   468 AA;  52316 MW;  D54D44B8D76D2F31 CRC64;
     MMIPIAIRWQ GKKYDLEIEP NETGSTLKHQ LYSLTQVPPE RQKVIVKGGQ LKDDVLLGSV
     GIKPNATLLM MGTAGELPTA MPIPAVESVE QEESEDDGYP SGLINLGNTC YMNSTVQMLR
     AIPELSDAVS QFNSSGGLVA EYRTLLNSMQ SNAPVTPMRF LQSLRMEYPQ FAEMSRETGG
     YAQQDAEECW SFLLSVLQRS LSSEWVQKNM AGKLLSTMKC DENEVQEQPS ISHDTFLSLP
     CHISMHTSYM TQGILEGLTQ KISKHSDVLN RDAMYSKISR ISRLPNYLTV NFVRFYWKAS
     IGKKAKILRK VKFPFELDAV EFCTPELSQK LIPVRDKLRE IEKNDEEHER AAKRIKIQPS
     EDEKEAEAEC RLTQVATCQS LVDPELADDE GANPTGLYDL VGVLSHAGAS ASSGHYQAWI
     RNSNNRAEWF RFNDAKVSIV PAEKIETLDG GGEADSAYIL LYKAKDIA
//