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Protein EMP46 (46 kDa endomembrane protein)

 EMP46_YEAST             Reviewed;         444 AA.
Q12396; D6VY80;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 128.
RecName: Full=Protein EMP46;
AltName: Full=46 kDa endomembrane protein;
Flags: Precursor;
Name=EMP46; OrderedLocusNames=YLR080W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
PROTEIN SEQUENCE OF 47-56, FUNCTION, SUBCELLULAR LOCATION, INTERACTION
WITH COP1; SEC21 AND SEC23, AND MUTAGENESIS OF TYR-429; PHE-432;
440-LYS--LYS-442; 440-LYS--LEU-444 AND 443-LEU-LEU-444.
PubMed=12134087; DOI=10.1091/mbc.E02-01-0027;
Sato K., Nakano A.;
"Emp47p and its close homolog Emp46p have a tyrosine-containing
endoplasmic reticulum exit signal and function in glycoprotein
secretion in Saccharomyces cerevisiae.";
Mol. Biol. Cell 13:2518-2532(2002).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12206772; DOI=10.1016/S0022-2836(02)00652-6;
Teixeira M.T., Dujon B., Fabre E.;
"Genome-wide nuclear morphology screen identifies novel genes involved
in nuclear architecture and gene-silencing in Saccharomyces
cerevisiae.";
J. Mol. Biol. 321:551-561(2002).
[5]
INTERACTION WITH EMP47, AND SUBCELLULAR LOCATION.
PubMed=12857885; DOI=10.1091/mbc.E03-02-0115;
Sato K., Nakano A.;
"Oligomerization of a cargo receptor directs protein sorting into
COPII-coated transport vesicles.";
Mol. Biol. Cell 14:3055-3063(2003).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
FUNCTION.
PubMed=14627716; DOI=10.1074/jbc.C300457200;
Sato K., Nakano A.;
"Reconstitution of coat protein complex II (COPII) vesicle formation
from cargo-reconstituted proteoliposomes reveals the potential role of
GTP hydrolysis by Sar1p in protein sorting.";
J. Biol. Chem. 279:1330-1335(2004).
[8]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[9]
X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 52-275, POTASSIUM-BINDING,
AND MUTAGENESIS OF TYR-177.
PubMed=16439369; DOI=10.1074/jbc.M512258200;
Satoh T., Sato K., Kanoh A., Yamashita K., Yamada Y., Igarashi N.,
Kato R., Nakano A., Wakatsuki S.;
"Structures of the carbohydrate recognition domain of Ca2+-independent
cargo receptors Emp46p and Emp47p.";
J. Biol. Chem. 281:10410-10419(2006).
-!- FUNCTION: Involved in the secretion of glycoproteins and in
nucleus architecture and gene silencing.
{ECO:0000269|PubMed:12134087, ECO:0000269|PubMed:12206772,
ECO:0000269|PubMed:14627716}.
-!- SUBUNIT: Interacts with EMP47 in the endoplasmic reticulum
membrane in order to be transported to the Golgi apparatus.
Interacts with the coatomer proteins COP1, SEC21 and SEC23.
{ECO:0000269|PubMed:12134087, ECO:0000269|PubMed:12857885}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type I
membrane protein. Endoplasmic reticulum membrane; Single-pass type
I membrane protein.
-!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
localization for type I membrane proteins. {ECO:0000250}.
-!- SIMILARITY: Belongs to the EMP46/EMP47 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z73252; CAA97639.1; -; Genomic_DNA.
EMBL; U53880; AAB67584.1; -; Genomic_DNA.
EMBL; BK006945; DAA09396.1; -; Genomic_DNA.
PIR; S64912; S64912.
RefSeq; NP_013181.1; NM_001181967.1.
PDB; 2A6V; X-ray; 1.52 A; A/B=52-275.
PDB; 2A6W; X-ray; 1.75 A; A/B=52-275.
PDB; 2A6X; X-ray; 1.55 A; A/B=52-275.
PDBsum; 2A6V; -.
PDBsum; 2A6W; -.
PDBsum; 2A6X; -.
ProteinModelPortal; Q12396; -.
SMR; Q12396; -.
BioGrid; 31353; 100.
DIP; DIP-4209N; -.
IntAct; Q12396; 1.
STRING; 4932.YLR080W; -.
UniLectin; Q12396; -.
MaxQB; Q12396; -.
PaxDb; Q12396; -.
PRIDE; Q12396; -.
EnsemblFungi; YLR080W; YLR080W; YLR080W.
GeneID; 850769; -.
KEGG; sce:YLR080W; -.
EuPathDB; FungiDB:YLR080W; -.
SGD; S000004070; EMP46.
GeneTree; ENSGT00510000053646; -.
HOGENOM; HOG000112365; -.
InParanoid; Q12396; -.
KO; K10080; -.
OMA; GKIMAND; -.
OrthoDB; EOG092C4CI2; -.
BioCyc; YEAST:G3O-32231-MONOMER; -.
EvolutionaryTrace; Q12396; -.
PRO; PR:Q12396; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IPI:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IGI:SGD.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
CDD; cd06903; lectin_EMP46_EMP47; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR016710; Emp46/Emp47.
InterPro; IPR035661; EMP46/EMP47_N.
InterPro; IPR005052; Lectin_leg.
Pfam; PF03388; Lectin_leg-like; 1.
PIRSF; PIRSF018136; L-type_lectin_fungi; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51328; L_LECTIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Golgi apparatus; Lectin;
Membrane; Metal-binding; Potassium; Protein transport;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Transport.
SIGNAL 1 46 {ECO:0000269|PubMed:12134087}.
CHAIN 47 444 Protein EMP46.
/FTId=PRO_0000239645.
TOPO_DOM 47 408 Lumenal. {ECO:0000255}.
TRANSMEM 409 429 Helical. {ECO:0000255}.
TOPO_DOM 430 444 Cytoplasmic. {ECO:0000255}.
DOMAIN 52 269 L-type lectin-like. {ECO:0000255|PROSITE-
ProRule:PRU00658}.
REGION 429 432 Mediates the interactions with COPI and
COPII coat complexes.
MOTIF 440 444 Di-lysine motif.
METAL 177 177 Potassium.
DISULFID 196 230
MUTAGEN 177 177 Y->F: Impairs potassium-binding.
{ECO:0000269|PubMed:16439369}.
MUTAGEN 429 429 Y->A: Impairs interaction with COP1,
SEC21 and SEC23 and loss of reticulum
endoplasmic exit.
{ECO:0000269|PubMed:12134087}.
MUTAGEN 432 432 F->A: Impairs interaction with COP1,
SEC21 and SEC23 and loss of reticulum
endoplasmic exit.
{ECO:0000269|PubMed:12134087}.
MUTAGEN 440 444 Missing: Loss of endoplasmic reticulum
exit. {ECO:0000269|PubMed:12134087}.
MUTAGEN 440 442 KVK->SVS,RVR: Impairs interaction with
COP1 and SEC21 and mislocalizes to the
vacuole. {ECO:0000269|PubMed:12134087}.
MUTAGEN 443 444 LL->AA: Loss of endoplasmic reticulum
exit. {ECO:0000269|PubMed:12134087}.
HELIX 58 60 {ECO:0000244|PDB:2A6V}.
TURN 65 67 {ECO:0000244|PDB:2A6V}.
HELIX 71 74 {ECO:0000244|PDB:2A6V}.
TURN 75 77 {ECO:0000244|PDB:2A6V}.
STRAND 78 82 {ECO:0000244|PDB:2A6V}.
STRAND 85 87 {ECO:0000244|PDB:2A6V}.
STRAND 90 93 {ECO:0000244|PDB:2A6V}.
STRAND 100 107 {ECO:0000244|PDB:2A6V}.
STRAND 115 125 {ECO:0000244|PDB:2A6V}.
STRAND 133 139 {ECO:0000244|PDB:2A6V}.
TURN 150 152 {ECO:0000244|PDB:2A6V}.
STRAND 158 167 {ECO:0000244|PDB:2A6V}.
TURN 168 170 {ECO:0000244|PDB:2A6V}.
STRAND 171 183 {ECO:0000244|PDB:2A6V}.
TURN 187 189 {ECO:0000244|PDB:2A6V}.
STRAND 193 197 {ECO:0000244|PDB:2A6V}.
STRAND 207 214 {ECO:0000244|PDB:2A6V}.
HELIX 215 217 {ECO:0000244|PDB:2A6V}.
STRAND 219 225 {ECO:0000244|PDB:2A6V}.
STRAND 228 234 {ECO:0000244|PDB:2A6V}.
HELIX 238 240 {ECO:0000244|PDB:2A6V}.
STRAND 244 251 {ECO:0000244|PDB:2A6V}.
STRAND 258 269 {ECO:0000244|PDB:2A6V}.
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


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