MAM3_YEAST
ID MAM3_YEAST Reviewed; 706 AA.
AC Q12296; D6W207;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein MAM3;
GN Name=MAM3; OrderedLocusNames=YOL060C;
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=8789261;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<67::aid-yea884>3.0.co;2-f;
RA Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
RT "Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
RL Yeast 12:67-76(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 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, AND SUBCELLULAR LOCATION.
RX PubMed=15498024; DOI=10.1042/bj20041582;
RA Yang M., Jensen L.T., Gardner A.J., Culotta V.C.;
RT "Manganese toxicity and Saccharomyces cerevisiae Mam3p, a member of the
RT ACDP (ancient conserved domain protein) family.";
RL Biochem. J. 386:479-487(2005).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; SER-447; SER-603;
RP TYR-604 AND THR-607, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Involved in metal homeostasis and more specially in manganese
CC sensitivity. {ECO:0000269|PubMed:15498024}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15498024}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15498024}.
CC -!- MISCELLANEOUS: Present with 2270 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ACDP family. {ECO:0000305}.
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DR EMBL; X91067; CAA62524.1; -; Genomic_DNA.
DR EMBL; Z74802; CAA99069.1; -; Genomic_DNA.
DR EMBL; AY692822; AAT92841.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10723.1; -; Genomic_DNA.
DR PIR; S61717; S61717.
DR RefSeq; NP_014581.1; NM_001183315.1.
DR AlphaFoldDB; Q12296; -.
DR SMR; Q12296; -.
DR BioGRID; 34341; 66.
DR IntAct; Q12296; 26.
DR STRING; 4932.YOL060C; -.
DR iPTMnet; Q12296; -.
DR MaxQB; Q12296; -.
DR PaxDb; Q12296; -.
DR PRIDE; Q12296; -.
DR TopDownProteomics; Q12296; -.
DR EnsemblFungi; YOL060C_mRNA; YOL060C; YOL060C.
DR GeneID; 854094; -.
DR KEGG; sce:YOL060C; -.
DR SGD; S000005421; MAM3.
DR VEuPathDB; FungiDB:YOL060C; -.
DR eggNOG; KOG2118; Eukaryota.
DR HOGENOM; CLU_011310_3_1_1; -.
DR InParanoid; Q12296; -.
DR OMA; DVFVDIH; -.
DR BioCyc; YEAST:G3O-33469-MON; -.
DR PRO; PR:Q12296; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12296; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IMP:SGD.
DR GO; GO:0010960; P:magnesium ion homeostasis; IEA:InterPro.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR045095; ACDP.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR PANTHER; PTHR12064; PTHR12064; 1.
DR Pfam; PF01595; DUF21; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..706
FT /note="Protein MAM3"
FT /id="PRO_0000255960"
FT TOPO_DOM 1..16
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..120
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..177
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 57..240
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 259..320
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 321..386
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 421..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 604
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 607
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 706 AA; 77712 MW; AAB3EA4CAD8E5F53 CRC64;
MSFLPLRSRS RSGAPHWVYI ILYHIFTIPK IYSLPLLSGS HVLNSRDVAD SGHSVGDEAS
VTTYYIISII LVLLGGVFAG LTLGLMGQDE VYLKVISTSG SNSEKKLAKR VLDLISRGKH
WVLVTLLLSN VITNETLPIV LDRCLGGGWQ AVVSSTILIV IFGEIIPQSV CVKYGLQVGA
FFCPFVLVLM YLMYPVAYPI ATLLDYMLGE DHGTMYKKSG LKTLVTLHRT MGVERLTKDE
VTIISAVLDL KAKRVEEIMT PIENVFTMSA DTILDDKTVE KIFNSGFSRI PIFLPNEPNN
FIGMLLVRVL ISYDPDDCLP ISHFPLATLP ETSPNTSCLN ILNYFQEGKA HMCVVSKEPG
SSHGAIGVLT LEDVIEELIG EEIVDESDVF VDMHQHIMRQ QPGPLSKRHI TSYLHHLYTS
SHKEHKAADQ ADESSPLLSP SNSNHPSEHP QQDLNNKSWK QKSNDGYDRS NAVLSPTPQV
TEHGTIIPSN LASNPLNVNK SFVTIKKPAN VPKIITTHTP HSSKEPSPAP HSNDKSLSAE
EQQLLSDHAE LSRQAVLHTQ RSGQPTQVTT STKTTRNSPD SISIPNSGAN HGNENQNVTI
STSYQNTKNG IVESVITVKG VPKTIIGPAK DWDESKSEYG NENINQENSN RSDDRESSSS
NASLFSSIKN KFKNENANNN DRSNFTDSLS RTSNYDANGS SSTIKR
