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RPN1_NEUCR
ID   RPN1_NEUCR              Reviewed;         902 AA.
AC   Q7S8R8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=26S proteasome regulatory subunit rpn-1;
GN   Name=rpn-1; ORFNames=NCU07721;
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).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S2 family. {ECO:0000305}.
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DR   EMBL; CM002239; EAA32735.2; -; Genomic_DNA.
DR   RefSeq; XP_961971.2; XM_956878.3.
DR   AlphaFoldDB; Q7S8R8; -.
DR   SMR; Q7S8R8; -.
DR   STRING; 5141.EFNCRP00000008058; -.
DR   PRIDE; Q7S8R8; -.
DR   EnsemblFungi; EAA32735; EAA32735; NCU07721.
DR   GeneID; 3878119; -.
DR   KEGG; ncr:NCU07721; -.
DR   VEuPathDB; FungiDB:NCU07721; -.
DR   HOGENOM; CLU_008705_1_0_1; -.
DR   InParanoid; Q7S8R8; -.
DR   OMA; KTVYKHM; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:1905754; C:ascospore-type prospore nucleus; IEA:EnsemblFungi.
DR   GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0031595; C:nuclear proteasome complex; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR   GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR016643; 26S_Psome_Rpn1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR   InterPro; IPR041433; RPN1_C.
DR   InterPro; IPR040892; RPN1_N.
DR   PANTHER; PTHR10943:SF1; PTHR10943:SF1; 1.
DR   Pfam; PF01851; PC_rep; 2.
DR   Pfam; PF18051; RPN1_C; 1.
DR   Pfam; PF17781; RPN1_RPN2_N; 1.
DR   PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Proteasome; Reference proteome; Repeat.
FT   CHAIN           1..902
FT                   /note="26S proteasome regulatory subunit rpn-1"
FT                   /id="PRO_0000173813"
FT   REPEAT          415..448
FT                   /note="PC 1"
FT   REPEAT          449..487
FT                   /note="PC 2"
FT   REPEAT          488..522
FT                   /note="PC 3"
FT   REPEAT          525..559
FT                   /note="PC 4"
FT   REPEAT          568..601
FT                   /note="PC 5"
FT   REPEAT          645..680
FT                   /note="PC 6"
FT   REPEAT          681..715
FT                   /note="PC 7"
FT   REPEAT          716..750
FT                   /note="PC 8"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   902 AA;  100251 MW;  75816FF842D13F19 CRC64;
     MAQESDLSKT ADKGKGKAVD DEKKHQDVDG KTPANGKKEE EQNASEELSE EDQQLKSELE
     MLVERLTESD ATLYKPALEA MKNSIKTSTS SMTAVPKPLK FLRPHYETMT KLYDEWPAGD
     DKSSLADVLS VIGMTYSDED RQDTLKYRLL SPTQDIGSWG HEYVRHLALE IGEVYAKRIA
     NDEPTQELVD LALVLVPLFL KSNAEADAVD LMSELEIIEE LPKFLDENTY SRVCLYMVSM
     VNLLTYPDNE TFLRVAHSIY KKYNQHTQAM VLAIRLNDLG LIEKDFEAAD EDPALRKQLA
     FLIARQGIPL EFERSNDDDE KIYECLSNQK LSEYFKSLGK ELNILEPKTT EDIYKSHLES
     SRVAGMTNFD SARHNLAAGF VNAFVNAGFG SDKMMLVGKD KDSWVWKTKD EGMMSTVASL
     GTLLLWDVEN GLDHVDKYTY LEEEQIQAGA YLAIGIMNTN VRTDSEPAMA LLADPDKLAH
     KNPLIRVATI MGLGLAYAGS CKEELLSFLV NIISDPEESM QVSAMAALAC GMIFVGSSNS
     EVSEAIVTTL LDEESGSRLN DKWSRFLALG LGLLYFGRQE QVDVILETLK AVEHPMAKPT
     AVLAEICAWA GTGAVLKIQE LLHICNEHIE DGEEKKGEEL LQAYAVLGIG LIAMGEDVGQ
     EMVLRHFGHL MHYGEANIRR AVPLAMGLIS PSNPQMKVYD TLSRYSHDND NEVAINAIFA
     MGLLGAGTNN ARLAQLLRQL ASYYHRDQES LFMVRIAQGL LHMGKGTLSV SPFHTDRQVL
     SNVATAGLLA VLVAMIDAKQ FITSKSHYLL YWIVTAMHPR MLVTLDEDLK PLTVNVRVGQ
     AVDVVGQAGR PKTITGWQTQ STPVLLGYGE RAELEDDQYI SLSSTLEGLV ILRKNPDWEG
     EK
 
 
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