TMN1_YEAST
ID TMN1_YEAST Reviewed; 667 AA.
AC P32802; D6VY83; Q12101;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Transmembrane 9 superfamily member 1;
DE AltName: Full=70 kDa endomembrane protein;
DE AltName: Full=Endomembrane protein EMP70;
DE Contains:
DE RecName: Full=Protein p24a;
DE AltName: Full=Acidic 24 kDa late endocytic intermediate component;
DE Flags: Precursor;
GN Name=EMP70; Synonyms=TMN1; OrderedLocusNames=YLR083C;
GN ORFNames=L2385, L9449.11;
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=MH 145-4B;
RA Singer-Krueger B., Krueger U., Riezman H.;
RT "Molecular characterization of putative markers for early and late
RT endosomes.";
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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 PROTEIN SEQUENCE OF 23-42, AND SUBCELLULAR LOCATION.
RC STRAIN=RH732;
RX PubMed=8314797; DOI=10.1016/s0021-9258(19)85250-x;
RA Singer-Krueger B., Frank R., Crausaz F., Riezman H.;
RT "Partial purification and characterization of early and late endosomes from
RT yeast. Identification of four novel proteins.";
RL J. Biol. Chem. 268:14376-14386(1993).
RN [5]
RP PROBABLE CLEAVAGE BY KEX2.
RX PubMed=9729438; DOI=10.1016/s0378-1119(98)00349-7;
RA Schimmoeller F., Diaz E., Muehlbauer B., Pfeffer S.R.;
RT "Characterization of a 76 kDa endosomal, multispanning membrane protein
RT that is highly conserved throughout evolution.";
RL Gene 216:311-318(1998).
RN [6]
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 [7]
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 [8]
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 TMN2 and TMN3, 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: Endosome membrane {ECO:0000269|PubMed:8314797};
CC Multi-pass membrane protein. Vacuole membrane
CC {ECO:0000269|PubMed:20681974}; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
CC {ECO:0000305}.
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DR EMBL; X67316; CAA47730.1; -; Genomic_DNA.
DR EMBL; U53880; AAB67587.1; -; Genomic_DNA.
DR EMBL; Z73255; CAA97643.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09399.1; -; Genomic_DNA.
DR PIR; S25110; S25110.
DR PIR; S64915; S64915.
DR RefSeq; NP_013184.1; NM_001181970.1.
DR AlphaFoldDB; P32802; -.
DR BioGRID; 31356; 82.
DR DIP; DIP-4700N; -.
DR IntAct; P32802; 6.
DR MINT; P32802; -.
DR STRING; 4932.YLR083C; -.
DR iPTMnet; P32802; -.
DR MaxQB; P32802; -.
DR PaxDb; P32802; -.
DR PRIDE; P32802; -.
DR TopDownProteomics; P32802; -.
DR EnsemblFungi; YLR083C_mRNA; YLR083C; YLR083C.
DR GeneID; 850772; -.
DR KEGG; sce:YLR083C; -.
DR SGD; S000004073; EMP70.
DR VEuPathDB; FungiDB:YLR083C; -.
DR eggNOG; KOG1278; Eukaryota.
DR GeneTree; ENSGT00940000172441; -.
DR HOGENOM; CLU_010714_4_1_1; -.
DR InParanoid; P32802; -.
DR OMA; TILITYH; -.
DR BioCyc; YEAST:G3O-32234-MON; -.
DR PRO; PR:P32802; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32802; protein.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA: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:0006878; P:cellular copper ion homeostasis; IMP:SGD.
DR GO; GO:0016197; P:endosomal transport; IMP:SGD.
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 Direct protein sequencing; Endosome; Glycoprotein; Ion transport; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport;
KW Vacuole.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:8314797"
FT CHAIN 23..667
FT /note="Transmembrane 9 superfamily member 1"
FT /id="PRO_0000034371"
FT CHAIN 23..250
FT /note="Protein p24a"
FT /id="PRO_0000034372"
FT TOPO_DOM 23..302
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..405
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..474
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..560
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..635
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..667
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 250..251
FT /note="Cleavage; by KEX2"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 207
FT /note="R -> C (in Ref. 1; CAA47730)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="G -> E (in Ref. 1; CAA47730)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="L -> S (in Ref. 1; CAA47730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 75963 MW; B5B8AA6876C548CA CRC64;
MIYKMAHVQL LLLYFFVSTV KAFYLPGVAP TTYRENDNIP LLVNHLTPSM NYQHKDEDGN
NVSGDKENFL YSYDYYYNRF HFCQPEKVEK QPESLGSVIF GDRIYNSPFQ LNMLQEKECE
SLCKTVIPGD DAKFINKLIK NGFFQNWLID GLPAAREVYD GRTKTSFYGA GFNLGFVQVT
QGTDIEATPK GAETTDKDVE LETRNDRNMV KTYELPYFAN HFDIMIEYHD RGEGNYRVVG
VIVEPVSIKR SSPGTCETTG SPLMLDEGND NEVYFTYSVK FNESATSWAT RWDKYLHVYD
PSIQWFSLIN FSLVVVLLSS VVIHSLLRAL KSDFARYNEL NLDDDFQEDS GWKLNHGDVF
RSPSQSLTLS ILVGSGVQLF LMVTCSIFFA ALGFLSPSSR GSLATVMFIL YALFGFVGSY
TSMGIYKFFN GPYWKANLIL TPLLVPGAIL LIIIALNFFL MFVHSSGVIP ASTLFFMVFL
WFLFSIPLSF AGSLIARKRC HWDEHPTKTN QIARQIPFQP WYLKTIPATL IAGIFPFGSI
AVELYFIYTS LWFNKIFYMF GFLFFSFLLL TLTSSLVTIL ITYHSLCLEN WKWQWRGFII
GGAGCALYVF IHSILFTKFK LGGFTTIVLY VGYSSVISLL CCLVTGSIGF ISSMLFVRKI
YSSIKVD
