NESP1_SCHPO
ID NESP1_SCHPO Reviewed; 420 AA.
AC O42980; P78807;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=NEDD8-specific protease 1;
DE EC=3.4.22.-;
GN Name=nep1; ORFNames=SPBC17D11.01, SPBC20F10.11;
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 [MRNA], FUNCTION, INTERACTION WITH CSN5, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15769255; DOI=10.1042/bj20041991;
RA Zhou L., Watts F.Z.;
RT "Nep1, a Schizosaccharomyces pombe deneddylating enzyme.";
RL Biochem. J. 389:307-314(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-340 AND SER-351, AND
RP IDENTIFICATION BY 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: Protease that catalyzes two essential functions in the NEDD8
CC pathway: processing of full-length NEDD8 to its mature form and
CC deconjugation of NEDD8 from targeted proteins such as the pcu1, pcu2
CC and pcu4 cullins and other proteins. {ECO:0000269|PubMed:15769255}.
CC -!- SUBUNIT: Interacts with csn1. It is, however, not a component of the
CC signalosome. {ECO:0000269|PubMed:15769255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15769255}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; D89156; BAA13818.1; -; mRNA.
DR EMBL; CU329671; CAA16851.1; -; Genomic_DNA.
DR PIR; T39712; T39712.
DR PIR; T42516; T42516.
DR RefSeq; NP_596375.2; NM_001022296.2.
DR AlphaFoldDB; O42980; -.
DR SMR; O42980; -.
DR BioGRID; 276358; 11.
DR STRING; 4896.SPBC17D11.01.1; -.
DR MEROPS; C48.025; -.
DR iPTMnet; O42980; -.
DR SwissPalm; O42980; -.
DR MaxQB; O42980; -.
DR PaxDb; O42980; -.
DR PRIDE; O42980; -.
DR EnsemblFungi; SPBC17D11.01.1; SPBC17D11.01.1:pep; SPBC17D11.01.
DR GeneID; 2539808; -.
DR KEGG; spo:SPBC17D11.01; -.
DR PomBase; SPBC17D11.01; nep1.
DR VEuPathDB; FungiDB:SPBC17D11.01; -.
DR eggNOG; KOG3246; Eukaryota.
DR HOGENOM; CLU_054090_0_0_1; -.
DR InParanoid; O42980; -.
DR PhylomeDB; O42980; -.
DR PRO; PR:O42980; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0019784; F:deNEDDylase activity; IDA:PomBase.
DR GO; GO:0000338; P:protein deneddylation; IDA:PomBase.
DR InterPro; IPR044613; Nep1/2-like.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR PANTHER; PTHR46468; PTHR46468; 1.
DR Pfam; PF02902; Peptidase_C48; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease.
FT CHAIN 1..420
FT /note="NEDD8-specific protease 1"
FT /id="PRO_0000101735"
FT REGION 257..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 57
FT /note="L -> W (in Ref. 2; BAA13818)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="F -> FGCYTCVV (in Ref. 2; BAA13818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 47258 MW; 2125D94D9A2D9E87 CRC64;
MSSSPTVLEL FDVCFKQEDV DSLKKPNWFT DVSIDYVDEL IEHLWFPSYP NQANEILLLR
PSLVFLLAEA AISPEELKVA LPKKLMNCKY LFMPINDLDK HAAGSGGSHW SLMVASIPDG
QCYYYDSLSN GKTKDCRSAL ARVSDLFKKK FTIECMPVQQ QRNGYDCGAH VCAFTLELVR
RLLHSPMPTS SMWNLSTFQP DVTAIREQLS RCLDHIINSL GTRVSGDFDE DFPTGTVFFD
LESHLPLLDV ALPVLPKSSD SSETSHESSN SNLKKSSESG STNHHNNHES DKDLHHEGHH
HHHHHHHHHH SHDDDPSSPA EKKQNHVPSP SEKIQDHVPS PSEKKQDRVP SPSNNKEDHL
PLLSDEKLDK SAIDKIEPTP LPSVHMNSHI AKGELPKFHN STDNPFLTPP EELVSGDFPF
