ID   SKP1_NEUCR              Reviewed;         171 AA.
AC   Q8NK13; U9W3K7;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=E3 ubiquitin ligase complex SCF subunit scon-3;
DE   AltName: Full=Sulfur control protein 3;
DE   AltName: Full=Sulfur metabolite repression control scon-3;
GN   Name=scon-3; Synonyms=skp1; ORFNames=NCU08991;
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 [GENOMIC DNA], INDUCTION, AND INTERACTION WITH SCON-2.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12477788; DOI=10.1128/ec.1.6.875-883.2002;
RA   Sizemore S.T., Paietta J.V.;
RT   "Cloning and characterization of scon-3+, a new member of the Neurospora
RT   crassa sulfur regulatory system.";
RL   Eukaryot. Cell 1:875-883(2002).
RN   [2]
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   [3]
RP   FUNCTION.
RX   PubMed=6455895;
RA   Piotrowska M., Kruszewska A., Paszewski A.;
RT   "Effect of regulatory mutations of sulphur metabolism on the levels of
RT   cysteine- and homocysteine-synthesizing enzymes in Neurospora crassa.";
RL   Acta Biochim. Pol. 27:395-403(1980).
CC   -!- FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) E3
CC       ubiquitin ligase complexes, which mediate the ubiquitination and
CC       subsequent proteasomal degradation of target proteins. Controls sulfur
CC       metabolite repression, probably by mediating the inactivation or
CC       degradation of the metR transcription factor (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:6455895}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC       ligase complexes (By similarity). Interacts with scon-2. {ECO:0000250,
CC       ECO:0000269|PubMed:12477788}.
CC   -!- SIMILARITY: Belongs to the SKP1 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; AF402682; AAM90676.1; -; Genomic_DNA.
DR   EMBL; CM002238; ESA43406.1; -; Genomic_DNA.
DR   EMBL; CM002238; ESA43407.1; -; Genomic_DNA.
DR   RefSeq; XP_011393972.1; XM_011395670.1.
DR   RefSeq; XP_011393973.1; XM_011395671.1.
DR   AlphaFoldDB; Q8NK13; -.
DR   SMR; Q8NK13; -.
DR   STRING; 5141.EFNCRP00000008967; -.
DR   EnsemblFungi; ESA43406; ESA43406; NCU08991.
DR   EnsemblFungi; ESA43407; ESA43407; NCU08991.
DR   GeneID; 3875176; -.
DR   KEGG; ncr:NCU08991; -.
DR   VEuPathDB; FungiDB:NCU08991; -.
DR   HOGENOM; CLU_059252_6_1_1; -.
DR   InParanoid; Q8NK13; -.
DR   OMA; PLKSADM; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR016897; SKP1.
DR   InterPro; IPR001232; SKP1-like.
DR   InterPro; IPR036296; SKP1-like_dim_sf.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR016072; Skp1_comp_dimer.
DR   InterPro; IPR016073; Skp1_comp_POZ.
DR   PANTHER; PTHR11165; PTHR11165; 1.
DR   Pfam; PF01466; Skp1; 1.
DR   Pfam; PF03931; Skp1_POZ; 1.
DR   PIRSF; PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1.
DR   SMART; SM00512; Skp1; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF81382; SSF81382; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..171
FT                   /note="E3 ubiquitin ligase complex SCF subunit scon-3"
FT                   /id="PRO_0000397269"
FT   REGION          112..171
FT                   /note="Interaction with the F-box domain of F-box proteins"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   171 AA;  19910 MW;  E7B2F688A8CD6A1D CRC64;
     MAENDERALQ KVSLQSNDGQ IITVDRVVAE RSLLIKNLIE DLGDEAVMNE AIPLPNVNEP
     VLRKVVEWCE HHRKDPPQTT EDENDSRKKS TEIDEWDQKF MQVDQEMLFE IILAANYMDI
     KPLLDVGCKT VANMIKGKSP EEIRKTFNIT NDFTPEEEEQ IRRENEWAED R