CSN3_SCHPO
ID CSN3_SCHPO Reviewed; 338 AA.
AC Q9UT51; Q9UTD9;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=COP9 signalosome complex subunit 3;
DE Short=CSN complex subunit 3;
DE Short=SGN3;
GN Name=csn3; ORFNames=SPAC222.16c, SPAC821.02c;
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).
CC -!- FUNCTION: Component of the COP9 signalosome (CSN) complex that acts as
CC an regulator of the ubiquitin (Ubl) conjugation pathway by mediating
CC the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-
CC protein ligase complexes. {ECO:0000250}.
CC -!- SUBUNIT: Component of the COP9 signalosome (CSN) complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CSN3 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; CU329670; CAB60708.3; -; Genomic_DNA.
DR PIR; T41713; T41713.
DR PIR; T50156; T50156.
DR RefSeq; NP_593155.3; NM_001018552.3.
DR AlphaFoldDB; Q9UT51; -.
DR SMR; Q9UT51; -.
DR BioGRID; 278402; 39.
DR STRING; 4896.SPAC222.16c.1; -.
DR MaxQB; Q9UT51; -.
DR PaxDb; Q9UT51; -.
DR EnsemblFungi; SPAC222.16c.1; SPAC222.16c.1:pep; SPAC222.16c.
DR GeneID; 2541912; -.
DR KEGG; spo:SPAC222.16c; -.
DR PomBase; SPAC222.16c; csn3.
DR VEuPathDB; FungiDB:SPAC222.16c; -.
DR eggNOG; KOG2582; Eukaryota.
DR HOGENOM; CLU_816744_0_0_1; -.
DR InParanoid; Q9UT51; -.
DR OMA; YHCLGNN; -.
DR Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR PRO; PR:Q9UT51; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0008180; C:COP9 signalosome; ISS:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005628; C:prospore membrane; HDA:PomBase.
DR GO; GO:0000338; P:protein deneddylation; TAS:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR037753; CSN3.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR10758:SF1; PTHR10758:SF1; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Reference proteome; Signalosome.
FT CHAIN 1..338
FT /note="COP9 signalosome complex subunit 3"
FT /id="PRO_0000120986"
FT DOMAIN 137..306
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 338 AA; 38950 MW; 578A3ACFCB07E0E1 CRC64;
MVANMEFQGT LPFHPLEDPE TLLLKFTDFV HQHSVEQCNQ LSMYIIASVN SLAEAFYGSH
PEKYNIVFQS VEYAAHSPAI SVMHVCYLKE LLRQGQYATS LKSFNDLEVS KHIPGSILLQ
YCMYAAYHCL GNNDLDSAKV WYFSILYIPT TTLTSFHEEA YYSFLLLYII TTGKKFQLDS
ATSSNVLPLK RHMVPYEEFL DAYLKDVNTL RTVIKEHWSR FLKDNSTAFI LFALEVYPMH
RLKKWRKTFS SLKLEYIAKQ LAISQDVAKE IIQKFDNKTN FTVANGEIFL TFNALDDVSP
EMHSDLCQQL IEASKNFEAS IRLKSVIYSK IMAKKLNA
