YL126_YEAST
ID YL126_YEAST Reviewed; 251 AA.
AC Q12288; D6VYC1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Putative glutamine amidotransferase YLR126C;
DE EC=2.4.2.-;
GN OrderedLocusNames=YLR126C; ORFNames=L3105;
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=ATCC 90840 / EAY235 / FY23;
RX PubMed=9090053;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<241::aid-yea61>3.0.co;2-#;
RA Verhasselt P., Volckaert G.;
RT "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-
RT Arg3 and 23 new open reading frames, among which several homologies to
RT proteins involved in cell division control and to mammalian growth factors
RT and other animal proteins are found.";
RL Yeast 13:241-250(1997).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=14534306; DOI=10.1074/jbc.m212308200;
RA De Freitas J.M., Kim J.H., Poynton H., Su T., Wintz H., Fox T., Holman P.,
RA Loguinov A., Keles S., van der Laan M., Vulpe C.;
RT "Exploratory and confirmatory gene expression profiling of mac1Delta.";
RL J. Biol. Chem. 279:4450-4458(2004).
RN [8]
RP INDUCTION.
RX PubMed=15886332; DOI=10.1152/physiolgenomics.00055.2005;
RA van Bakel H., Strengman E., Wijmenga C., Holstege F.C.P.;
RT "Gene expression profiling and phenotype analyses of S. cerevisiae in
RT response to changing copper reveals six genes with new roles in copper and
RT iron metabolism.";
RL Physiol. Genomics 22:356-367(2005).
CC -!- FUNCTION: May have a role in copper and iron homeostasis.
CC {ECO:0000269|PubMed:14534306}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Induced upon copper deprivation.
CC {ECO:0000269|PubMed:15886332}.
CC -!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; X89514; CAA61704.1; -; Genomic_DNA.
DR EMBL; U53877; AAB82372.1; -; Genomic_DNA.
DR EMBL; X91258; CAA62637.1; -; Genomic_DNA.
DR EMBL; Z73298; CAA97695.1; -; Genomic_DNA.
DR EMBL; AY692709; AAT92728.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09437.1; -; Genomic_DNA.
DR PIR; S59314; S59314.
DR RefSeq; NP_013227.1; NM_001182013.1.
DR AlphaFoldDB; Q12288; -.
DR SMR; Q12288; -.
DR BioGRID; 31395; 30.
DR DIP; DIP-2566N; -.
DR STRING; 4932.YLR126C; -.
DR MEROPS; C26.A05; -.
DR MaxQB; Q12288; -.
DR PaxDb; Q12288; -.
DR PRIDE; Q12288; -.
DR EnsemblFungi; YLR126C_mRNA; YLR126C; YLR126C.
DR GeneID; 850817; -.
DR KEGG; sce:YLR126C; -.
DR SGD; S000004116; YLR126C.
DR VEuPathDB; FungiDB:YLR126C; -.
DR eggNOG; KOG3179; Eukaryota.
DR HOGENOM; CLU_054974_0_2_1; -.
DR OMA; RWILRLC; -.
DR BioCyc; YEAST:G3O-32268-MON; -.
DR PRO; PR:Q12288; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12288; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006875; P:cellular metal ion homeostasis; ISS:SGD.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01741; GATase1_1; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR044992; ChyE-like.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR PANTHER; PTHR42695; PTHR42695; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glutamine amidotransferase; Reference proteome; Transferase.
FT CHAIN 1..251
FT /note="Putative glutamine amidotransferase YLR126C"
FT /id="PRO_0000247340"
FT DOMAIN 48..232
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 112
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 198
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 200
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 251 AA; 28826 MW; FCC96A8B62880D5C CRC64;
MTVKKIAILY TDEDNEWSKP WGNFVDMAIK LLEQTRKLEC IAEDVEYEVF HVQKNVFPQL
SDLQKDEYLG IYITGSKYDS FDNEIEWIMK LRSFLNEMLT SKTEYPPVAG ICFGHQVIAA
ALGSSVGRNP KGFEGGVVSL KLNSVGQKLF GAQELNLSEV HSDCVFDVPE GYQNWASSEK
CQNQGFYRQN RVLTFQGHPE FNSDVAQKGL LKSQDKLTLE EFNRYERQCQ ELDNNGIQAA
RNIWRLFLQK I
