GRR1_YEAST
ID GRR1_YEAST Reviewed; 1151 AA.
AC P24814; D6VWQ8;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=SCF E3 ubiquitin ligase complex F-box protein GRR1;
DE AltName: Full=F-box and leucine-rich repeat protein GRR1;
DE AltName: Full=F-box/LRR-repeat protein GRR1;
GN Name=GRR1; Synonyms=CAT80, COT2; OrderedLocusNames=YJR090C; ORFNames=J1885;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP LEUCINE-RICH REPEATS.
RX PubMed=1922034; DOI=10.1128/mcb.11.10.5101-5112.1991;
RA Flick J.S., Johnston M.;
RT "GRR1 of Saccharomyces cerevisiae is required for glucose repression and
RT encodes a protein with leucine-rich repeats.";
RL Mol. Cell. Biol. 11:5101-5112(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP FUNCTION IN UBIQUITINATION OF CLN1 AND CLN2.
RX PubMed=7883165; DOI=10.1101/gad.9.4.399;
RA Barral Y., Jentsch S., Mann C.;
RT "G1 cyclin turnover and nutrient uptake are controlled by a common pathway
RT in yeast.";
RL Genes Dev. 9:399-409(1995).
RN [6]
RP FUNCTION IN UBIQUITINATION OF GIC2.
RX PubMed=9736614; DOI=10.1093/emboj/17.18.5360;
RA Jaquenoud M., Gulli M.P., Peter K., Peter M.;
RT "The Cdc42p effector Gic2p is targeted for ubiquitin-dependent degradation
RT by the SCFGrr1 complex.";
RL EMBO J. 17:5360-5373(1998).
RN [7]
RP IDENTIFICATION IN SCF COMPLEX, AND FUNCTION IN UBIQUITINATION OF CLN1.
RX PubMed=10213692; DOI=10.1126/science.284.5414.662;
RA Skowyra D., Koepp D.M., Kamura T., Conrad M.N., Conaway R.C., Conaway J.W.,
RA Elledge S.J., Harper J.W.;
RT "Reconstitution of G1 cyclin ubiquitination with complexes containing
RT SCFGrr1 and Rbx1.";
RL Science 284:662-665(1999).
RN [8]
RP INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(GRR1) COMPLEX.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-300, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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. Recognizes and directs ubiquitination of phosphorylated CLN1,
CC CLN2 and GIC2. Probably constitutes the primary response element
CC required for the generation or interpretation of the signal that
CC induces glucose repression. {ECO:0000269|PubMed:10213692,
CC ECO:0000269|PubMed:1922034, ECO:0000269|PubMed:7883165,
CC ECO:0000269|PubMed:9736614}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with SKP1. Component of the probable SCF(GRR1)
CC complex containing CDC53, SKP1, RBX1 and GRR1.
CC {ECO:0000269|PubMed:10213692, ECO:0000269|PubMed:14747994}.
CC -!- INTERACTION:
CC P24814; Q12018: CDC53; NbExp=9; IntAct=EBI-7898, EBI-4321;
CC P24814; P52286: SKP1; NbExp=9; IntAct=EBI-7898, EBI-4090;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:1922034}.
CC Note=Associated with the particulate fraction. Probably forms a complex
CC by protein-protein interactions via its leucine-rich segment.
CC -!- INDUCTION: Expressed constitutively at low levels.
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DR EMBL; M59247; AAA34652.1; -; Genomic_DNA.
DR EMBL; Z49590; CAA89617.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39313.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08874.1; -; Genomic_DNA.
DR PIR; A41529; A41529.
DR RefSeq; NP_012623.1; NM_001181747.1.
DR AlphaFoldDB; P24814; -.
DR SMR; P24814; -.
DR BioGRID; 33844; 105.
DR ComplexPortal; CPX-3241; SCF-Grr1 ubiquitin ligase complex.
DR DIP; DIP-1626N; -.
DR IntAct; P24814; 27.
DR MINT; P24814; -.
DR STRING; 4932.YJR090C; -.
DR iPTMnet; P24814; -.
DR MaxQB; P24814; -.
DR PaxDb; P24814; -.
DR PRIDE; P24814; -.
DR EnsemblFungi; YJR090C_mRNA; YJR090C; YJR090C.
DR GeneID; 853552; -.
DR KEGG; sce:YJR090C; -.
DR SGD; S000003850; GRR1.
DR VEuPathDB; FungiDB:YJR090C; -.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000170586; -.
DR HOGENOM; CLU_008058_0_0_1; -.
DR InParanoid; P24814; -.
DR OMA; VDFACCT; -.
DR BioCyc; YEAST:G3O-31717-MON; -.
DR Reactome; R-SCE-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SCE-8949613; Cristae formation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P24814; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P24814; protein.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:ComplexPortal.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0071406; P:cellular response to methylmercury; IMP:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000751; P:mitotic cell cycle G1 arrest in response to pheromone; IMP:SGD.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0000209; P:protein polyubiquitination; IMP:SGD.
DR GO; GO:0019222; P:regulation of metabolic process; IC:ComplexPortal.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IPI:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 11.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glucose metabolism; Leucine-rich repeat; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..1151
FT /note="SCF E3 ubiquitin ligase complex F-box protein GRR1"
FT /id="PRO_0000119968"
FT DOMAIN 314..361
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 399..423
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 424..449
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 450..475
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 476..501
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 502..527
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 528..553
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 554..582
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 583..608
FT /note="LRR 8"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 609..634
FT /note="LRR 9"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 635..660
FT /note="LRR 10"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 661..685
FT /note="LRR 11"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 686..714
FT /note="LRR 12"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REPEAT 715..740
FT /note="LRR 13"
FT /evidence="ECO:0000269|PubMed:1922034"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1151 AA; 132734 MW; 6BB6C46611E6F825 CRC64;
MDQDNNNHND SNRLHPPDIH PNLGPQLWLN SSGDFDDNNN NNNNNNNNNS TRPQMPSRTR
ETATSERNAS EVRDATLNNI FRFDSIQRET LLPTNNGQPL NQNFSLTFQP QQQTNALNGI
DINTVNTNLM NGVNVQIDQL NRLLPNLPEE ERKQIHEFKL IVGKKIQEFL VVIEKRRKKI
LNEIELDNLK LKELRIDNSP QAISYLHKLQ RMRLRALETE NMEIRNLRLK ILTIIEEYKK
SLYAYCHSKL RGQQVENPTD NFIIWINSID TTESSDLKEG LQDLSRYSRQ FINNVLSNPS
NQNICTSVTR RSPVFALNML PSEILHLILD KLNQKYDIVK FLTVSKLWAE IIVKILYYRP
HINKKSQLDL FLRTMKLTSE ETVFNYRLMI KRLNFSFVGD YMHDTELNYF VGCKNLERLT
LVFCKHITSV PISAVLRGCK FLQSVDITGI RDVSDDVFDT LATYCPRVQG FYVPQARNVT
FDSLRNFIVH SPMLKRIKIT ANNNMNDELV ELLANKCPLL VEVDITLSPN VTDSSLLKLL
TRLVQLREFR ITHNTNITDN LFQELSKVVD DMPSLRLIDL SGCENITDKT IESIVNLAPK
LRNVFLGKCS RITDASLFQL SKLGKNLQTV HFGHCFNITD NGVRALFHSC TRIQYVDFAC
CTNLTNRTLY ELADLPKLKR IGLVKCTQMT DEGLLNMVSL RGRNDTLERV HLSYCSNLTI
YPIYELLMSC PRLSHLSLTA VPSFLRPDIT MYCRPAPSDF SENQRQIFCV FSGKGVHKLR
HYLVNLTSPA FGPHVDVNDV LTKYIRSKNL IFNGETLEDA LRRIITDLNQ DSAAIIAATG
LNQINGLNND FLFQNINFER IDEVFSWYLN TFDGIRMSSE EVNSLLLQVN KTFCEDPFSD
VDDDQDYVVA PGVNREINSE MCHIVRKFHE LNDHIDDFEV NVASLVRVQF QFTGFLLHEM
TQTYMQMIEL NRQICLVQKT VQESGNIDYQ KGLLIWRLLF IDKFIMVVQK YKLSTVVLRL
YLKDNITLLT RQRELLIAHQ RSAWNNNNDN DANRNANNIV NIVSDAGAND TSNNETNNGN
DDNETENPNF WRQFGNRMQI SPDQMRNLQM GLRNQNMVRN NNNNTIDESM PDTAIDSQMD
EASGTPDEDM L
