CSN6_NEUCR
ID CSN6_NEUCR Reviewed; 497 AA.
AC Q7S8C8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=COP9 signalosome complex subunit 6;
DE Short=Signalosome subunit 6;
GN Name=csn-6; ORFNames=NCU07019;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE COP9 SIGNALOSOME
RP COMPLEX, AND FUNCTION OF THE COP9 SIGNALOSOME COMPLEX.
RX PubMed=15961524; DOI=10.1101/gad.1322205;
RA He Q., Cheng P., He Q., Liu Y.;
RT "The COP9 signalosome regulates the Neurospora circadian clock by
RT controlling the stability of the SCFFWD-1 complex.";
RL Genes Dev. 19:1518-1531(2005).
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 (By similarity). The CSN complex is involved
CC in the regulation of the circadian clock through its control of the
CC stability of the SCF(FWD1) complex. {ECO:0000250,
CC ECO:0000269|PubMed:15961524}.
CC -!- SUBUNIT: Component of the COP9 signalosome (CSN) complex.
CC {ECO:0000269|PubMed:15961524}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN6 subfamily.
CC {ECO:0000305}.
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DR EMBL; CM002239; EAA32604.1; -; Genomic_DNA.
DR RefSeq; XP_961840.1; XM_956747.2.
DR AlphaFoldDB; Q7S8C8; -.
DR STRING; 5141.EFNCRP00000007086; -.
DR EnsemblFungi; EAA32604; EAA32604; NCU07019.
DR GeneID; 3877988; -.
DR KEGG; ncr:NCU07019; -.
DR VEuPathDB; FungiDB:NCU07019; -.
DR HOGENOM; CLU_027018_2_0_1; -.
DR InParanoid; Q7S8C8; -.
DR OMA; DLVGWYT; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0000338; P:protein deneddylation; IEA:InterPro.
DR CDD; cd08063; MPN_CSN6; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR033859; MPN_CSN6.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Signalosome.
FT CHAIN 1..497
FT /note="COP9 signalosome complex subunit 6"
FT /id="PRO_0000314735"
FT DOMAIN 21..162
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 230..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 54044 MW; 58E34A83970A7061 CRC64;
MAAATVNPLM STLKSDSSLQ VALHPLPILE ISDYITRSYL RGYKGAIVGA LIGQQNGRQI
TIEHSFSVKT EHTGQNYKVD SEWFTARLDQ MKAVHKDRAL DFVGWYTLVP KSGPTDAHLP
IHSYFYSQNE SAVLLGFHIH EILNPVAGDP LPLTIYESNL EIVDGTEAST VEVEGEDREM
KDVTAEPSRS IKFRELPYTT ETGEAEMIAL EFVREGGSAN VTTTATNITA TEDEGSDKPL
MKKVVDTNKG SKRRAVSSDD AAAEAPTTSS AAKGTATDKN RDANLTKAEL DYMSALQAKY
NAVQMMKKRL DTVISYLQRL PPDYLSSGDA SSQQQQQQQQ QQQTEGLDQP QYTVPSNKIL
RQIQALVTNV QLVMSNSTSG QGQGQGERDT DLGALEKELL KETNDVKLVE LIADLMSSVK
DMKEVGKKFH VVETAKNSKR REQASHGGGE RFNPHHPYPG GGGGSSMMRE HAGLVGEGSA
SGSGGSGPAG DLARFDH
