ULP1_SCHPO
ID ULP1_SCHPO Reviewed; 568 AA.
AC O42957;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Ubiquitin-like-specific protease 1;
DE EC=3.4.22.-;
GN Name=ulp1; ORFNames=SPBC19G7.09;
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 FUNCTION, AND GENE NAME.
RA Watts F.;
RL Submitted (MAR-2001) to UniProtKB.
CC -!- FUNCTION: A cysteine protease that proteolytically removes the C-
CC terminus of pmt3. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAA17063.1; -; Genomic_DNA.
DR PIR; T39840; T39840.
DR RefSeq; NP_595975.1; NM_001021883.2.
DR AlphaFoldDB; O42957; -.
DR SMR; O42957; -.
DR BioGRID; 277257; 40.
DR STRING; 4896.SPBC19G7.09.1; -.
DR MEROPS; C48.A19; -.
DR iPTMnet; O42957; -.
DR SwissPalm; O42957; -.
DR MaxQB; O42957; -.
DR PaxDb; O42957; -.
DR EnsemblFungi; SPBC19G7.09.1; SPBC19G7.09.1:pep; SPBC19G7.09.
DR GeneID; 2540734; -.
DR KEGG; spo:SPBC19G7.09; -.
DR PomBase; SPBC19G7.09; ulp1.
DR VEuPathDB; FungiDB:SPBC19G7.09; -.
DR eggNOG; KOG0778; Eukaryota.
DR HOGENOM; CLU_512061_0_0_1; -.
DR InParanoid; O42957; -.
DR OMA; WDSLAGS; -.
DR PhylomeDB; O42957; -.
DR BRENDA; 3.4.22.68; 5613.
DR Reactome; R-SPO-3065679; SUMO is proteolytically processed.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:O42957; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0016929; F:deSUMOylase activity; IDA:PomBase.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; IDA:PomBase.
DR GO; GO:0016926; P:protein desumoylation; IDA:PomBase.
DR GO; GO:0016485; P:protein processing; IDA:PomBase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR Pfam; PF02902; Peptidase_C48; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..568
FT /note="Ubiquitin-like-specific protease 1"
FT /id="PRO_0000101733"
FT REGION 64..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 463
FT /evidence="ECO:0000250"
FT ACT_SITE 480
FT /evidence="ECO:0000250"
FT ACT_SITE 527
FT /evidence="ECO:0000250"
SQ SEQUENCE 568 AA; 64941 MW; AAF9771440302D9F CRC64;
MIGKRNASKR TRQDDCITYE EYQRKRKKTF LNTFVNICSR TVTYAKLFLT KTPISELDRI
AGEAIPSNSN STNSKLEPST KAPESRFSHI NSKTERGYVT VESDMSSHNT LDRNSKPTVS
HSYTNSSKDE KFLDPIALQN LFSPASDTHS QNIHDEALSP SSFRVSRSRY FPRPHRSSKN
LSVSNRLQLA VFKETTSSTL SHGNSVEADE INSFNPTPFS SSPLHFTNSS PNPNSDIVTP
DKQLDVVSEH ARYKHLPFTA TLRKKSPHDS TSRKASFRFV QSDQQPARNI VTSDIQNEKS
LLLLIRDLKE KQTESFQDWN EVDFLQLKGL EISPPPTRPK FIPELEFPDN ARKRALKYLN
QSNSVSSSEP IITKFNIPIT LKDLHTLRNR QWLNDEVINF YMNLISERSK IDSSLPRVHG
FNTFFYTSLQ RRGYAGVRRW AKKARVNIAD MDAVFIPVHL DVHWCMAVIN KSKKRFEYWD
SLAGSPGKVF DLLRDYYIAE TKGAVDVSDW ENFMDDNSPR QRNGHDCGVF ACKTAECVSR
NVPVQFSQND MPELRIKMAA SIIDAQIY
