MMP1_YEAST
ID MMP1_YEAST Reviewed; 583 AA.
AC Q12372; D6VXU8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=S-methylmethionine permease 1;
GN Name=MMP1; OrderedLocusNames=YLL061W; ORFNames=L0555;
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=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 [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 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-23, 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).
CC -!- FUNCTION: High-affinity S-methylmethionine (SMM) permease, required for
CC utilization of S-methylmethionine 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 -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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; Z73166; CAA97514.1; -; Genomic_DNA.
DR EMBL; Z47973; CAA87996.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09264.1; -; Genomic_DNA.
DR PIR; S50959; S50959.
DR RefSeq; NP_013039.1; NM_001181881.1.
DR AlphaFoldDB; Q12372; -.
DR SMR; Q12372; -.
DR BioGRID; 31255; 44.
DR DIP; DIP-8952N; -.
DR IntAct; Q12372; 2.
DR MINT; Q12372; -.
DR STRING; 4932.YLL061W; -.
DR TCDB; 2.A.3.10.16; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; Q12372; -.
DR MaxQB; Q12372; -.
DR PaxDb; Q12372; -.
DR PRIDE; Q12372; -.
DR EnsemblFungi; YLL061W_mRNA; YLL061W; YLL061W.
DR GeneID; 850665; -.
DR KEGG; sce:YLL061W; -.
DR SGD; S000003984; MMP1.
DR VEuPathDB; FungiDB:YLL061W; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000176823; -.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; Q12372; -.
DR OMA; QYLFNIC; -.
DR BioCyc; YEAST:G3O-32158-MON; -.
DR PRO; PR:Q12372; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12372; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0000100; F:S-methylmethionine transmembrane transporter activity; IMP:SGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015806; P:S-methylmethionine transport; IMP:SGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR Pfam; PF00324; AA_permease; 1.
DR TIGRFAMs; TIGR00913; 2A0310; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..583
FT /note="S-methylmethionine permease 1"
FT /id="PRO_0000054157"
FT TOPO_DOM 1..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..356
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..428
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..505
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08986"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 583 AA; 64218 MW; AF88AB299957C5AA CRC64;
MDEFESTKLS KVQFSTSVLS TPSNEGNNLI HRFKNSFKRN DSPAIQEGLL YSELSEEEKI
QWDLANQPYK KVLDQRHLTM IAIGGTLGTG LFIGLGESLA SGPASLLIGF LLVGASMLCV
VQCGAELSCQ YPVSGSYALH ASRFIDPSVG FSIGINYLLM WLISYPSELV GCSLTISYWA
PSVNPAAWVA IAFVLSMLLN LFGARGFAES EFYMSIFKIV ALFIFIIIGI VLIAGGGPDS
TGYIGTKYWH DPGSFAVPVF KNLCNTFVSA AYSFSGTEMV VLTSTEARSV SSVSRAAKGT
FWRIIIFYIV TVIIIGCLVP YNDPRLISGS SSEDITASPF VIALSNTGAM GTRVSHFMNA
VILIAVFSVC NSCVYASSRL IQGLATAGQL PKICAYMDRN GRPLVGMAIC GAFGLLGFLV
VSKNQGTVFT WLFALCSISF FTTWFCICFC QVRFRMAMKA QGRSKDDIIY RSTLGIYGGI
FGCILNVLLV IGEIYVSAAP VGSPSSAANF FEYCMSIPIM IAVYIGHRIY RRDWRHWYIK
RMDIDLDSGH SLEDFEATKL ERDEDKKYVS SKPLYYRIYR FFC
