UCC1_YEAST
ID UCC1_YEAST Reviewed; 369 AA.
AC Q05947; D6VYM4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=F-box protein UCC1;
DE AltName: Full=Ubiquitination of citrate synthase in the glyoxylate cycle protein 1;
GN Name=UCC1; OrderedLocusNames=YLR224W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP DOMAIN F-BOX, AND FUNCTION PREDICTION.
RX PubMed=10582239; DOI=10.1098/rstb.1999.0497;
RA Willems A.R., Goh T., Taylor L., Chernushevich I., Shevchenko A., Tyers M.;
RT "SCF ubiquitin protein ligases and phosphorylation-dependent proteolysis.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 354:1533-1550(1999).
RN [4]
RP INTERACTION WITH SKP1, AND DOMAIN F-BOX.
RX PubMed=11283612; DOI=10.1038/35070067;
RA Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.;
RT "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-
RT ATPase assembly.";
RL Nat. Cell Biol. 3:384-391(2001).
RN [5]
RP INTERACTION WITH SKP1, RECONSTITUTION OF THE SCF(YLR224W) COMPLEX, AND
RP MONOUBIQUITINATION.
RX PubMed=14747994; DOI=10.1002/prot.10620;
RA Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.;
RT "Functional interaction of 13 yeast SCF complexes with a set of yeast E2
RT enzymes in vitro.";
RL Proteins 54:455-467(2004).
RN [6]
RP FUNCTION, INTERACTION WITH CIT2, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25982115; DOI=10.1016/j.molcel.2015.04.013;
RA Nakatsukasa K., Nishimura T., Byrne S.D., Okamoto M.,
RA Takahashi-Nakaguchi A., Chibana H., Okumura F., Kamura T.;
RT "The ubiquitin ligase SCF(Ucc1) acts as a metabolic switch for the
RT glyoxylate cycle.";
RL Mol. Cell 59:22-34(2015).
CC -!- FUNCTION: Substrate recognition component of the SKP1-CUL1-F-box
CC protein E3 ubiquitin-protein ligase complex SCF(UCC1) which mediates
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins (PubMed:10582239, PubMed:25982115). The SCF(UCC1) complex acts
CC as a metabolic switch for the glyoxylate cycle and regulates the level
CC of CIT2 protein to maintain citrate homeostasis (PubMed:25982115).
CC {ECO:0000269|PubMed:10582239, ECO:0000269|PubMed:25982115}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the SCF(UCC1) E3 ubiquitin-protein ligase complex
CC composed of CDC53, SKP1, RBX1 and UCC1 (PubMed:11283612,
CC PubMed:14747994). Interacts with CIT2 (PubMed:25982115).
CC {ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:14747994,
CC ECO:0000269|PubMed:25982115}.
CC -!- INTERACTION:
CC Q05947; P52286: SKP1; NbExp=4; IntAct=EBI-33647, EBI-4090;
CC -!- INDUCTION: Expression is down-regulated by the presence of C2-compounds
CC such as acetate. {ECO:0000269|PubMed:25982115}.
CC -!- PTM: Monoubiquitinated by UBC4.
CC -!- DISRUPTION PHENOTYPE: Leads to poor ubiquitination of CIT2 and
CC accumulation of citrate in the cells. {ECO:0000269|PubMed:25982115}.
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DR EMBL; U19027; AAB67408.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09540.1; -; Genomic_DNA.
DR PIR; S51447; S51447.
DR RefSeq; NP_013325.1; NM_001182111.1.
DR AlphaFoldDB; Q05947; -.
DR BioGRID; 31491; 130.
DR DIP; DIP-1630N; -.
DR IntAct; Q05947; 3.
DR MINT; Q05947; -.
DR STRING; 4932.YLR224W; -.
DR iPTMnet; Q05947; -.
DR MaxQB; Q05947; -.
DR PaxDb; Q05947; -.
DR PRIDE; Q05947; -.
DR EnsemblFungi; YLR224W_mRNA; YLR224W; YLR224W.
DR GeneID; 850921; -.
DR KEGG; sce:YLR224W; -.
DR SGD; S000004214; UCC1.
DR VEuPathDB; FungiDB:YLR224W; -.
DR eggNOG; ENOG502S61D; Eukaryota.
DR HOGENOM; CLU_063944_0_0_1; -.
DR InParanoid; Q05947; -.
DR OMA; VWIYLED; -.
DR BioCyc; YEAST:G3O-32338-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q05947; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05947; protein.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISA:SGD.
DR GO; GO:0071406; P:cellular response to methylmercury; IMP:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:SGD.
PE 1: Evidence at protein level;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..369
FT /note="F-box protein UCC1"
FT /id="PRO_0000269758"
FT DOMAIN 8..45
FT /note="F-box"
SQ SEQUENCE 369 AA; 42754 MW; 4C9FA5962E3A9851 CRC64;
MNQSDSSLMD LPLEIHLSLL EYVPNELRAV NKYFYVLHNH SYKEKSLAWI AEDNYIWAVV
KHSLCLYVKS LDPLRQHARE IIQETKEPGF NVPLCMTKYI ADSWYIVYNA LQYPGKIINM
GWDKYTKSQD SNGSDSTSNF NSRPKERTLM QSLTALPVNF WSRRKDEPTP VNVWFYVKNA
HVARYIPKII TEIGICNYGP KQIVASAGYI NELITSEGIY CVNLGHLPRL YDEQIFEGTG
TTHLPLELKA IDRTDSDVCI NGDLVLLGYD FIPYQISKPW LLFRIEPVNS IEAIFNYSEC
SFSYQFAWSL ACLQSEEKIS FPRDTIIGHG LPYKPSKLIR IFVYKHPEQK QDLGQEIALP
NWNTPYLRR
