SAM3_YEAST
ID SAM3_YEAST Reviewed; 587 AA.
AC Q08986; D6W396; Q7LGU1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=S-adenosylmethionine permease SAM3;
DE AltName: Full=S-adenosylmethionine metabolism protein 3;
GN Name=SAM3; OrderedLocusNames=YPL274W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 FUNCTION.
RX PubMed=10497160; DOI=10.1074/jbc.274.40.28096;
RA Rouillon A., Surdin-Kerjan Y., Thomas D.;
RT "Transport of sulfonium compounds. Characterization of the s-
RT adenosylmethionine and s-methylmethionine permeases from the yeast
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:28096-28105(1999).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: High-affinity S-adenosylmethionine permease, required for
CC utilization of S-adenosylmethionine as a sulfur source.
CC {ECO:0000269|PubMed:10497160}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14562095}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:14562095}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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DR EMBL; Z73629; CAA98010.1; -; Genomic_DNA.
DR EMBL; Z73630; CAA98011.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11162.1; -; Genomic_DNA.
DR PIR; S65307; S65307.
DR RefSeq; NP_015049.1; NM_001184088.1.
DR AlphaFoldDB; Q08986; -.
DR SMR; Q08986; -.
DR BioGRID; 35939; 72.
DR DIP; DIP-8874N; -.
DR STRING; 4932.YPL274W; -.
DR TCDB; 2.A.3.10.15; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; Q08986; -.
DR SwissPalm; Q08986; -.
DR MaxQB; Q08986; -.
DR PaxDb; Q08986; -.
DR PRIDE; Q08986; -.
DR EnsemblFungi; YPL274W_mRNA; YPL274W; YPL274W.
DR GeneID; 855854; -.
DR KEGG; sce:YPL274W; -.
DR SGD; S000006195; SAM3.
DR VEuPathDB; FungiDB:YPL274W; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000176823; -.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; Q08986; -.
DR OMA; TFWRIAI; -.
DR BioCyc; YEAST:G3O-34155-MON; -.
DR PRO; PR:Q08986; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08986; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015489; F:putrescine transmembrane transporter activity; IDA:SGD.
DR GO; GO:0000095; F:S-adenosyl-L-methionine transmembrane transporter activity; IMP:SGD.
DR GO; GO:0015606; F:spermidine transmembrane transporter activity; IDA:SGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015847; P:putrescine transport; IDA:SGD.
DR GO; GO:0015805; P:S-adenosyl-L-methionine transport; IMP:SGD.
DR GO; GO:0015848; P:spermidine transport; IDA:SGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR TIGRFAMs; TIGR00913; 2A0310; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..587
FT /note="S-adenosylmethionine permease SAM3"
FT /id="PRO_0000054163"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..360
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..509
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12372"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 587 AA; 64354 MW; 6ADEA30F9763B92F CRC64;
MDILKRGNES DKFTKIETES TTIPNDSDRS GSLIRRMKDS FKQSNLHVIP EDLENSEQTE
QEKIQWKLAS QPYQKVLSQR HLTMIAIGGT LGTGLFIGLG YSLASGPAAL LIGFLLVGTS
MFCVVQSAAE LSCQFPVSGS YATHVSRFID ESVGFTVATN YALAWLISFP SELIGCALTI
SYWNQTVNPA VWVAIFYVFI MVLNLFGVRG FAETEFALSI IKVIAIFIFI IIGIVLIAGG
GPNSTGYIGA KYWHDPGAFA KPVFKNLCNT FVSAAFSFGG SELVLLTSTE SKNISAISRA
AKGTFWRIAI FYITTVVIIG CLVPYNDPRL LSGSNSEDVS ASPFVIALSN TGSMGAKVSN
FMNVVILVAV VSVCNSCVYA SSRLIQALGA SGQLPSVCSY MDRKGRPLVG IGISGAFGLL
GFLVASKKED EVFTWLFALC SISSFFTWFC ICMSQIRFRM ALKAQGRSND EIAYKSILGV
YGGILGCVLN ALLIAGEIYV SAAPVGSPSS AEAFFEYCLS IPIMIVVYFA HRFYRRDWKH
FYIKRSEIDL DTGCSVENLE LFKAQKEAEE QLIASKPFYY KIYRFWC
