ALR1_YEAST
ID ALR1_YEAST Reviewed; 859 AA.
AC Q08269; D6W1T8; Q02811;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Magnesium transporter ALR1;
DE AltName: Full=Aluminum resistance protein 1;
GN Name=ALR1; OrderedLocusNames=YOL130W;
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 96604 / S288c / FY1679;
RX PubMed=8896265;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1013::aid-yea980%3e3.0.co;2-5;
RA Casamayor A., Khalid H., Balcells L., Aldea M., Casas C., Herrero E.,
RA Arino J.;
RT "Sequence analysis of a 13.4 kbp fragment from the left arm of chromosome
RT XV reveals a malate dehydrogenase gene, a putative Ser/Thr protein kinase,
RT the ribosomal L25 gene and four new open reading frames.";
RL Yeast 12:1013-1020(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 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 FUNCTION.
RX PubMed=9430719; DOI=10.1074/jbc.273.3.1727;
RA MacDiarmid C.W., Gardner R.C.;
RT "Overexpression of the Saccharomyces cerevisiae magnesium transport system
RT confers resistance to aluminum ion.";
RL J. Biol. Chem. 273:1727-1732(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-77; SER-220; SER-221; SER-236
RP AND THR-242, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-850, AND IDENTIFICATION BY
RP 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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-185 AND SER-188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Plasma membrane magnesium transporter.
CC {ECO:0000269|PubMed:9430719}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9430719};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC family. {ECO:0000305}.
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DR EMBL; U41293; AAC49462.1; -; Genomic_DNA.
DR EMBL; Z74872; CAA99150.1; -; Genomic_DNA.
DR EMBL; Z74871; CAA99149.1; -; Genomic_DNA.
DR EMBL; AY692762; AAT92781.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10654.1; -; Genomic_DNA.
DR PIR; S66827; S66827.
DR RefSeq; NP_014511.1; NM_001183384.1.
DR AlphaFoldDB; Q08269; -.
DR BioGRID; 34245; 47.
DR DIP; DIP-1184N; -.
DR IntAct; Q08269; 12.
DR MINT; Q08269; -.
DR STRING; 4932.YOL130W; -.
DR TCDB; 1.A.35.2.1; the cora metal ion transporter (mit) family.
DR iPTMnet; Q08269; -.
DR MaxQB; Q08269; -.
DR PaxDb; Q08269; -.
DR PRIDE; Q08269; -.
DR EnsemblFungi; YOL130W_mRNA; YOL130W; YOL130W.
DR GeneID; 853990; -.
DR KEGG; sce:YOL130W; -.
DR SGD; S000005490; ALR1.
DR VEuPathDB; FungiDB:YOL130W; -.
DR eggNOG; ENOG502QPTQ; Eukaryota.
DR GeneTree; ENSGT00940000176664; -.
DR HOGENOM; CLU_007127_6_0_1; -.
DR InParanoid; Q08269; -.
DR OMA; AHSMPHQ; -.
DR BioCyc; YEAST:G3O-33525-MON; -.
DR BRENDA; 7.2.2.14; 984.
DR PRO; PR:Q08269; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08269; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IMP:SGD.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006812; P:cation transport; IMP:SGD.
DR GO; GO:0010961; P:cellular magnesium ion homeostasis; IBA:GO_Central.
DR GO; GO:0015693; P:magnesium ion transport; IDA:SGD.
DR CDD; cd12829; Alr1p-like; 1.
DR InterPro; IPR044089; Alr1-like.
DR InterPro; IPR045861; CorA_cytoplasmic_dom.
DR InterPro; IPR045863; CorA_TM1_TM2.
DR InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR Pfam; PF01544; CorA; 2.
DR SUPFAM; SSF143865; SSF143865; 1.
DR SUPFAM; SSF144083; SSF144083; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Magnesium; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..859
FT /note="Magnesium transporter ALR1"
FT /id="PRO_0000201535"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 77
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 13
FT /note="N -> Y (in Ref. 1; AAC49462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 95869 MW; 6DA44CA70EFA2693 CRC64;
MSSSSSSSES SPNLSRSNSL ANTMVSMKTE DHTGLYDHRQ HPDSLPVRHQ PPTLKNKEIA
KSTKPSIPKE QKSATRYNSH VDVGSVPSRG RMDFEDEGQG MDETVAHHQL RASAILTSNA
RPSRLAHSMP HQRQLYVESN IHTPPKDVGV KRDYTMSSST ASSGNKSKLS ASSSASPITK
VRKSSLVSPV LEIPHESKSD THSKLAKPKK RTYSTTSAHS SINPAVLLTK STSQKSDADD
DTLERKPVRM NTRASFDSDV SQASRDSQET EEDVCFPMPP QLHTRVNGID FDELEEYAQF
ANAEKSQFLA SLQVPNEQKY SNVSQDIGFT SSTSTSGSSA ALKYTPRVSQ TGEKSESTNE
TEIHEKKEDE HEKIKPSLHP GISFGKNKVE GEENENIPSN DPAYCSYQGT DFQIPNRFSF
FCSESDETVH ASDIPSLVSE GQTFYELFRG GEPTWWLDCS CPTDDEMRCI AKAFGIHPLT
AEDIRMQETR EKVELFKSYY FVCFHTFEND KESEDFLEPI NVYIVVCRSG VLTFHFGPIS
HCANVRRRVR QLRDYVNVNS DWLCYALIDD ITDSFAPVIQ SIEYEADAIE DSVFMARDMD
FAAMLQRIGE SRRKTMTLMR LLSGKADVIK MFAKRCQDEA NGIGPALTSQ INIANLQARQ
DNASHIKNNS STTVPNNYAP TTSQPRGDIA LYLGDIQDHL LTMFQNLLAY EKIFSRSHTN
YLAQLQVESF NSNNKVTEML GKVTMIGTML VPLNVITGLF GMNVKVPGEN SSIAWWFGIL
GVLLLLAVLG WFLASYWIKR IDPPATLNEA AESGAKSVIS SFLPKRNKRF NDRSKNINVR
AGPSNKSVAS LPSRYSRYD
