EMP46_YEAST
ID EMP46_YEAST Reviewed; 444 AA.
AC Q12396; D6VY80;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein EMP46;
DE AltName: Full=46 kDa endomembrane protein;
DE Flags: Precursor;
GN Name=EMP46; OrderedLocusNames=YLR080W;
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 PROTEIN SEQUENCE OF 47-56, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH
RP COP1; SEC21 AND SEC23, AND MUTAGENESIS OF TYR-429; PHE-432;
RP 440-LYS--LYS-442; 440-LYS--LEU-444 AND 443-LEU-LEU-444.
RX PubMed=12134087; DOI=10.1091/mbc.e02-01-0027;
RA Sato K., Nakano A.;
RT "Emp47p and its close homolog Emp46p have a tyrosine-containing endoplasmic
RT reticulum exit signal and function in glycoprotein secretion in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 13:2518-2532(2002).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12206772; DOI=10.1016/s0022-2836(02)00652-6;
RA Teixeira M.T., Dujon B., Fabre E.;
RT "Genome-wide nuclear morphology screen identifies novel genes involved in
RT nuclear architecture and gene-silencing in Saccharomyces cerevisiae.";
RL J. Mol. Biol. 321:551-561(2002).
RN [5]
RP INTERACTION WITH EMP47, AND SUBCELLULAR LOCATION.
RX PubMed=12857885; DOI=10.1091/mbc.e03-02-0115;
RA Sato K., Nakano A.;
RT "Oligomerization of a cargo receptor directs protein sorting into COPII-
RT coated transport vesicles.";
RL Mol. Biol. Cell 14:3055-3063(2003).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=14627716; DOI=10.1074/jbc.c300457200;
RA Sato K., Nakano A.;
RT "Reconstitution of coat protein complex II (COPII) vesicle formation from
RT cargo-reconstituted proteoliposomes reveals the potential role of GTP
RT hydrolysis by Sar1p in protein sorting.";
RL J. Biol. Chem. 279:1330-1335(2004).
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 X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 52-275, POTASSIUM-BINDING, AND
RP MUTAGENESIS OF TYR-177.
RX PubMed=16439369; DOI=10.1074/jbc.m512258200;
RA Satoh T., Sato K., Kanoh A., Yamashita K., Yamada Y., Igarashi N., Kato R.,
RA Nakano A., Wakatsuki S.;
RT "Structures of the carbohydrate recognition domain of Ca2+-independent
RT cargo receptors Emp46p and Emp47p.";
RL J. Biol. Chem. 281:10410-10419(2006).
CC -!- FUNCTION: Involved in the secretion of glycoproteins and in nucleus
CC architecture and gene silencing. {ECO:0000269|PubMed:12134087,
CC ECO:0000269|PubMed:12206772, ECO:0000269|PubMed:14627716}.
CC -!- SUBUNIT: Interacts with EMP47 in the endoplasmic reticulum membrane in
CC order to be transported to the Golgi apparatus. Interacts with the
CC coatomer proteins COP1, SEC21 and SEC23. {ECO:0000269|PubMed:12134087,
CC ECO:0000269|PubMed:12857885}.
CC -!- INTERACTION:
CC Q12396; P43555: EMP47; NbExp=3; IntAct=EBI-38641, EBI-6439;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type I
CC membrane protein. Endoplasmic reticulum membrane; Single-pass type I
CC membrane protein.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EMP46/EMP47 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; Z73252; CAA97639.1; -; Genomic_DNA.
DR EMBL; U53880; AAB67584.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09396.1; -; Genomic_DNA.
DR PIR; S64912; S64912.
DR RefSeq; NP_013181.1; NM_001181967.1.
DR PDB; 2A6V; X-ray; 1.52 A; A/B=52-275.
DR PDB; 2A6W; X-ray; 1.75 A; A/B=52-275.
DR PDB; 2A6X; X-ray; 1.55 A; A/B=52-275.
DR PDBsum; 2A6V; -.
DR PDBsum; 2A6W; -.
DR PDBsum; 2A6X; -.
DR AlphaFoldDB; Q12396; -.
DR SMR; Q12396; -.
DR BioGRID; 31353; 103.
DR DIP; DIP-4209N; -.
DR IntAct; Q12396; 1.
DR STRING; 4932.YLR080W; -.
DR UniLectin; Q12396; -.
DR MaxQB; Q12396; -.
DR PaxDb; Q12396; -.
DR PRIDE; Q12396; -.
DR EnsemblFungi; YLR080W_mRNA; YLR080W; YLR080W.
DR GeneID; 850769; -.
DR KEGG; sce:YLR080W; -.
DR SGD; S000004070; EMP46.
DR VEuPathDB; FungiDB:YLR080W; -.
DR eggNOG; ENOG502QR1C; Eukaryota.
DR GeneTree; ENSGT00940000176827; -.
DR HOGENOM; CLU_050572_0_0_1; -.
DR InParanoid; Q12396; -.
DR OMA; GKIMAND; -.
DR BioCyc; YEAST:G3O-32231-MON; -.
DR Reactome; R-SCE-9013106; RHOC GTPase cycle.
DR EvolutionaryTrace; Q12396; -.
DR PRO; PR:Q12396; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12396; protein.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IPI:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IDA:SGD.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IGI:SGD.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd06903; lectin_EMP46_EMP47; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016710; Emp46/Emp47.
DR InterPro; IPR035661; EMP46/EMP47_N.
DR InterPro; IPR005052; Lectin_leg.
DR Pfam; PF03388; Lectin_leg-like; 1.
DR PIRSF; PIRSF018136; L-type_lectin_fungi; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51328; L_LECTIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Golgi apparatus; Lectin; Membrane; Metal-binding;
KW Potassium; Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..46
FT /evidence="ECO:0000269|PubMed:12134087"
FT CHAIN 47..444
FT /note="Protein EMP46"
FT /id="PRO_0000239645"
FT TOPO_DOM 47..408
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 52..269
FT /note="L-type lectin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT REGION 429..432
FT /note="Mediates the interactions with COPI and COPII coat
FT complexes"
FT MOTIF 440..444
FT /note="Di-lysine motif"
FT BINDING 177
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT DISULFID 196..230
FT MUTAGEN 177
FT /note="Y->F: Impairs potassium-binding."
FT /evidence="ECO:0000269|PubMed:16439369"
FT MUTAGEN 429
FT /note="Y->A: Impairs interaction with COP1, SEC21 and SEC23
FT and loss of reticulum endoplasmic exit."
FT /evidence="ECO:0000269|PubMed:12134087"
FT MUTAGEN 432
FT /note="F->A: Impairs interaction with COP1, SEC21 and SEC23
FT and loss of reticulum endoplasmic exit."
FT /evidence="ECO:0000269|PubMed:12134087"
FT MUTAGEN 440..444
FT /note="Missing: Loss of endoplasmic reticulum exit."
FT /evidence="ECO:0000269|PubMed:12134087"
FT MUTAGEN 440..442
FT /note="KVK->SVS,RVR: Impairs interaction with COP1 and
FT SEC21 and mislocalizes to the vacuole."
FT /evidence="ECO:0000269|PubMed:12134087"
FT MUTAGEN 443..444
FT /note="LL->AA: Loss of endoplasmic reticulum exit."
FT /evidence="ECO:0000269|PubMed:12134087"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2A6V"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2A6V"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:2A6V"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 115..125
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:2A6V"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:2A6V"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 171..183
FT /evidence="ECO:0007829|PDB:2A6V"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:2A6V"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:2A6V"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:2A6V"
FT STRAND 258..269
FT /evidence="ECO:0007829|PDB:2A6V"
SQ SEQUENCE 444 AA; 50947 MW; 9B83B61667814DBE CRC64;
MTTRKTASSL QLLGKITGTK AGTKQKKMNF INGLIWLYMC VWMVHGKVTQ KDELKWNKGY
SLPNLLEVTD QQKELSQWTL GDKVKLEEGR FVLTPGKNTK GSLWLKPEYS IKDAMTIEWT
FRSFGFRGST KGGLAFWLKQ GNEGDSTELF GGSSKKFNGL MILLRLDDKL GESVTAYLND
GTKDLDIESS PYFASCLFQY QDSMVPSTLR LTYNPLDNHL LKLQMDNRVC FQTRKVKFMG
SSPFRIGTSA INDASKESFE ILKMKLYDGV IEDSLIPNVN PMGQPRVVTK VINSQTGEES
FREKMPFSDK EESITSNELF EKMNKLEGKI MANDIDPLLR KMNKIVENER ELIQRLRPLL
DLKKTAISDD SFQDFLSMNA NLDRLIKEQE KIRQDAKLYG KQTKGHDEIF SKISVWLALL
IFIMITLAYY MFRINQDIKK VKLL
