TMN3_YEAST
ID TMN3_YEAST Reviewed; 706 AA.
AC P40071; D3DM19;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Transmembrane 9 superfamily member 3;
DE Flags: Precursor;
GN Name=TMN3; OrderedLocusNames=YER113C;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 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 [4]
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 [5]
RP FUNCTION.
RX PubMed=18178563; DOI=10.1074/jbc.m704484200;
RA Froquet R., Cherix N., Birke R., Benghezal M., Cameroni E., Letourneur F.,
RA Moesch H.-U., De Virgilio C., Cosson P.;
RT "Control of cellular physiology by TM9 proteins in yeast and
RT Dictyostelium.";
RL J. Biol. Chem. 283:6764-6772(2008).
RN [6]
RP FUNCTION.
RX PubMed=20681974; DOI=10.1111/j.1399-3054.2010.01404.x;
RA Hegelund J.N., Jahn T.P., Baekgaard L., Palmgren M.G., Schjoerring J.K.;
RT "Transmembrane nine proteins in yeast and Arabidopsis affect cellular metal
RT contents without changing vacuolar morphology.";
RL Physiol. Plantarum 140:355-367(2010).
CC -!- FUNCTION: With EMP70 and TMN2, plays a critical role in the late stages
CC of a nutrient-controlled pathway notably regulating FLO11 gene
CC expression. Acts downstream of RAS2 and TOR. Essential for cell
CC adhesion and filamentous growth. May play a role as effector of
CC cellular copper homeostasis. {ECO:0000269|PubMed:18178563,
CC ECO:0000269|PubMed:20681974}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
CC {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; U18916; AAC03211.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07773.1; -; Genomic_DNA.
DR PIR; S50616; S50616.
DR RefSeq; NP_011038.3; NM_001179003.3.
DR AlphaFoldDB; P40071; -.
DR BioGRID; 36858; 69.
DR DIP; DIP-849N; -.
DR IntAct; P40071; 7.
DR MINT; P40071; -.
DR STRING; 4932.YER113C; -.
DR iPTMnet; P40071; -.
DR MaxQB; P40071; -.
DR PaxDb; P40071; -.
DR PRIDE; P40071; -.
DR EnsemblFungi; YER113C_mRNA; YER113C; YER113C.
DR GeneID; 856849; -.
DR KEGG; sce:YER113C; -.
DR SGD; S000000915; TMN3.
DR VEuPathDB; FungiDB:YER113C; -.
DR eggNOG; KOG1278; Eukaryota.
DR HOGENOM; CLU_010714_4_0_1; -.
DR InParanoid; P40071; -.
DR OMA; CPGASKD; -.
DR BioCyc; YEAST:G3O-30277-MON; -.
DR PRO; PR:P40071; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40071; protein.
DR GO; GO:0005794; C:Golgi apparatus; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:UniProtKB.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0072657; P:protein localization to membrane; IBA:GO_Central.
DR GO; GO:0007124; P:pseudohyphal growth; IGI:SGD.
DR GO; GO:0007034; P:vacuolar transport; IGI:SGD.
DR InterPro; IPR004240; EMP70.
DR PANTHER; PTHR10766; PTHR10766; 1.
DR Pfam; PF02990; EMP70; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Ion transport; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..706
FT /note="Transmembrane 9 superfamily member 3"
FT /id="PRO_0000034373"
FT TOPO_DOM 34..290
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..405
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..494
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 575..592
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 614..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..665
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 666..686
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 687..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 706 AA; 81546 MW; 8FD8A66E45B1BFC2 CRC64;
MRVRPKRSVI TLMAIVVVML ILRNQFYSSR TRGHGQEPVI SSSQKNLYDG WITPNFYRKG
DPLELIVNKV ESDLTQLPYA YYDLPFTCPP TMHKKPLHLS LNEIIRGDRK WESDYKLKFG
EDNPCETLCA RKTTKEGMQT LDKLVREGYV VQWLIDDELP AATTFISTTD HKKYYASGFP
LGFIDPDTDK TYLHNHVMLV IRFHASDNDK NTIVGFEVYP RSVSDYHCPG ASKNYEQYEI
VIPEDENELT YLPFTYSVYW REEFEVDWNH RWDYFLNAGE LSDEQSIQFH WMSLANSVGI
VLSISFITLI IYVRVMYTDK SNSKSPKYMI NIEGIETEDD LDDDKYGKYS VYTVAKDWIQ
NGRPNLFGLK VLILLVSFGV QFLFTIIGSL TISCSMNKLH NVRNSVLTMA ILFFVLGAFM
ASFVGTRLSM VTKTKRTKAN YLDDNRYLKD YKKFSPIFTI LCGSSLPGIV MVSTFLLNSI
VWAHDSTSAL PFKTIVFFMS IYFIVCIPLS LFGGIVANNI PLPQYWLSGI TKDESNSDGN
GLFVPKSRAK FNPLVYCGIY LCGIFPLLVI YVEMQYVYKS LWLEKTTFYY FYGFLFLSII
LLCVLTMEIS IIGSYLLMRF CFEDKVVRNN WRWKCFEMGF SGGVYMELYS LYYIFAVLNI
HGFSSILISI CYSLIFNVMC SLGLGALSYL TASWFINKIY HQKVNL
