HRT3_YEAST
ID HRT3_YEAST Reviewed; 344 AA.
AC Q12347; D6VY97;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=F-box protein HRT3;
DE AltName: Full=High level expression reduces Ty3 transposition protein 3;
GN Name=HRT3; OrderedLocusNames=YLR097C;
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 INTERACTION WITH SKP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [4]
RP INTERACTION WITH SKP1, RECONSTITUTION OF THE SCF(HRT3) COMPLEX, AND
RP FUNCTION.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Probably recognizes and binds to phosphorylated target
CC proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:14747994}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with SKP1. Component of the probable SCF(HRT3)
CC complex containing CDC53, SKP1, RBX1 and HRT3.
CC {ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:14747994}.
CC -!- INTERACTION:
CC Q12347; P52286: SKP1; NbExp=5; IntAct=EBI-30029, EBI-4090;
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; Z73269; CAA97660.1; -; Genomic_DNA.
DR EMBL; U53876; AAB67541.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09413.1; -; Genomic_DNA.
DR PIR; S64931; S64931.
DR RefSeq; NP_013198.1; NM_001181984.1.
DR AlphaFoldDB; Q12347; -.
DR SMR; Q12347; -.
DR BioGRID; 31370; 66.
DR ComplexPortal; CPX-3255; SCF-Hrt3 ubiquitin ligase complex.
DR DIP; DIP-1629N; -.
DR IntAct; Q12347; 20.
DR MINT; Q12347; -.
DR STRING; 4932.YLR097C; -.
DR MaxQB; Q12347; -.
DR PaxDb; Q12347; -.
DR PRIDE; Q12347; -.
DR EnsemblFungi; YLR097C_mRNA; YLR097C; YLR097C.
DR GeneID; 850786; -.
DR KEGG; sce:YLR097C; -.
DR SGD; S000004087; HRT3.
DR VEuPathDB; FungiDB:YLR097C; -.
DR eggNOG; KOG2997; Eukaryota.
DR GeneTree; ENSGT00390000014256; -.
DR HOGENOM; CLU_017706_1_0_1; -.
DR InParanoid; Q12347; -.
DR OMA; DEFRENW; -.
DR BioCyc; YEAST:G3O-32247-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q12347; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12347; 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; IGI:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR045118; FBXO9/FBXO48.
DR InterPro; IPR045464; Hrt3/FBXO9_C.
DR PANTHER; PTHR12874; PTHR12874; 1.
DR Pfam; PF19270; FBO_C; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 1: Evidence at protein level;
KW Reference proteome; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..344
FT /note="F-box protein HRT3"
FT /id="PRO_0000245842"
FT REPEAT 14..47
FT /note="TPR"
FT DOMAIN 98..148
FT /note="F-box"
SQ SEQUENCE 344 AA; 40475 MW; C2AF89147E313D93 CRC64;
MIVDYEKDPR AKEAIAIWEK GVLKEKDGSM SDAINFYRSA LKIHDNVESL YRKKILDEWM
LHKKLSGLSM TTDAPDEQNE TGKDDLSVEE NAELQPCWIL EILPDDILLR IIKKVILMSG
ESWVNLSMTC STFSKLCFHD SVPFKTFAKY IYSKQIYDKM AMDLNGITDI NTFEKEIWRG
DDYRMLRERP YIKFEGVYIS VVNYVRYGSN AESSLSLLKP VHMITYYRYF RFYENGQCLR
LLSTDEPSAV VKHFSKENKP RHSHMCYWSL GFDYDFGHLK ITRSDEKYTF IEEFQIKNQG
NKRYQRLKWL SSIVVDKEGN ASNCSLRNEK SFFFSRVKSF KDPG