LAG2_YEAST
ID LAG2_YEAST Reviewed; 660 AA.
AC Q92325; D6W240; Q08175;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cullin-associated NEDD8-dissociated protein 1 homolog;
DE AltName: Full=CAND1 homolog;
DE AltName: Full=Longevity-assurance protein 2;
GN Name=LAG2; OrderedLocusNames=YOL025W;
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].
RC STRAIN=SP1;
RX PubMed=8760941; DOI=10.1099/13500872-142-8-2289;
RA Childress A.M., Franklin D.S., Pinswasdi C., Kale S.P., Jazwinski S.M.;
RT "LAG2, a gene that determines yeast longevity.";
RL Microbiology 142:2289-2297(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP INTERACTION WITH CDC53.
RX PubMed=19763088; DOI=10.1038/emboj.2009.268;
RA Liu Y., Mimura S., Kishi T., Kamura T.;
RT "A longevity protein, Lag2, interacts with SCF complex and regulates SCF
RT function.";
RL EMBO J. 28:3366-3377(2009).
RN [6]
RP INTERACTION WITH CDC53, AND MUTAGENESIS OF LYS-16; 17-ASP--MET-23 AND
RP 551-GLY-ASN-552.
RX PubMed=19942853; DOI=10.1038/emboj.2009.354;
RA Siergiejuk E., Scott D.C., Schulman B.A., Hofmann K., Kurz T., Peter M.;
RT "Cullin neddylation and substrate-adaptors counteract SCF inhibition by the
RT CAND1-like protein Lag2 in Saccharomyces cerevisiae.";
RL EMBO J. 28:3845-3856(2009).
CC -!- FUNCTION: Assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC ligase complexes that promotes the exchange of the substrate-
CC recognition F-box subunit in SCF complexes, thereby playing a key role
CC in the cellular repertoire of SCF complexes. Acts as a F-box protein
CC exchange factor (By similarity). Involved in the aging process.
CC Longevity-assurance protein. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with unneddylated cullin CDC53.
CC {ECO:0000269|PubMed:19763088, ECO:0000269|PubMed:19942853}.
CC -!- INTERACTION:
CC Q92325; Q12018: CDC53; NbExp=10; IntAct=EBI-2045650, EBI-4321;
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed in young cells.
CC -!- PTM: Neddylated at Lys-16.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- CAUTION: Acts as an inhibitor of cullin neddylation and SCF complex
CC assembly in vitro (PubMed:19942853). However in vivo experiments in
CC other organisms strongly suggest that it acts as an essential regulator
CC of SCF complex assembly. {ECO:0000305|PubMed:19942853}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB16890.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U50334; AAB16890.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z74767; CAA99025.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10756.1; -; Genomic_DNA.
DR RefSeq; NP_014617.1; NM_001183279.1.
DR AlphaFoldDB; Q92325; -.
DR BioGRID; 34376; 70.
DR IntAct; Q92325; 8.
DR MINT; Q92325; -.
DR STRING; 4932.YOL025W; -.
DR MaxQB; Q92325; -.
DR PaxDb; Q92325; -.
DR PRIDE; Q92325; -.
DR EnsemblFungi; YOL025W_mRNA; YOL025W; YOL025W.
DR GeneID; 854133; -.
DR KEGG; sce:YOL025W; -.
DR SGD; S000005385; LAG2.
DR VEuPathDB; FungiDB:YOL025W; -.
DR eggNOG; ENOG502S2GH; Eukaryota.
DR HOGENOM; CLU_026649_0_0_1; -.
DR InParanoid; Q92325; -.
DR OMA; ICERRIR; -.
DR BioCyc; YEAST:G3O-33441-MON; -.
DR PRO; PR:Q92325; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q92325; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IMP:SGD.
PE 1: Evidence at protein level;
KW Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..660
FT /note="Cullin-associated NEDD8-dissociated protein 1
FT homolog"
FT /id="PRO_0000084352"
FT REGION 339..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT MUTAGEN 16
FT /note="K->R: Does not affect interaction with CDC53."
FT /evidence="ECO:0000269|PubMed:19942853"
FT MUTAGEN 17..23
FT /note="DNDLKYM->ANALKAA: Decreased interaction with CDC53."
FT /evidence="ECO:0000269|PubMed:19942853"
FT MUTAGEN 551..552
FT /note="GN->AA: Decreased interaction with CDC53."
FT /evidence="ECO:0000269|PubMed:19942853"
FT CONFLICT 13
FT /note="R -> C (in Ref. 1; AAB16890)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..157
FT /note="QL -> HV (in Ref. 1; AAB16890)"
FT /evidence="ECO:0000305"
FT CONFLICT 486..491
FT /note="CTLAHT -> VSYAI (in Ref. 1; AAB16890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 75639 MW; C5B8483C3BD758C1 CRC64;
MSLHISKLIE QYRSTKDNDL KYMLLRQNFK INDIEDELAP LVNELLLPVL VEEQDMEILN
LVSFQVLPDL VLSMISDPAA AQLGWVISLI CDPLLNQSMI HANRSFVLIE TLRNVLQKIE
NSPHLDYHQP VNSSLEFISK FIVEMKRHMC DVDAAQLSHS LSESNMLIYI ESLNLLLKFS
FFSDAASPSV MVTLPFDILN DVFTIAQDYS ATNTNESIDR ITEKLLLTST QLTHPVDLEN
LCPKMKYNTL AAVSRIWYKF GPIVDKLFTN RLLPVLFPPQ MGEECNVEDV LEIVHNFHPY
FSIRRLKDNR PLLSDSTISQ LREGLFGMLS ILNDSLTRTQ NENDHGSDNL IDSDDGFGSD
NDPEQQAYLD ELVSEGYDEN MYDGDTDDED ADDINVEKND EATKDITETN KILLIFSELH
YPQEERFSEL LVELQTKIAI NTSLIDKILS KETTELPTHN GEIADLNEIL NEVKGNKPIR
KNVIFCTLAH TLSLQSGSEL SVLQLSIEVI DHLLVKNHSN NITRGEQFQL IKLILPHLKT
NKSFIDTLKA GNFTQKIDEG VTLRTMILSL LLQLFPLDYS MLGEILPTIA RYSVRDKDLG
VRDLSFQLLD QILRTYYNYL IGIDWEWYKD DFYQVLQETC IKKDINTNLL LQFPPYLPHD
