EMP47_YEAST
ID EMP47_YEAST Reviewed; 445 AA.
AC P43555; D6VTI2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Protein EMP47;
DE AltName: Full=47 kDa endomembrane protein;
DE AltName: Full=Endosomal P44 protein;
DE Flags: Precursor;
GN Name=EMP47; OrderedLocusNames=YFL048C;
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], AND SUBCELLULAR LOCATION.
RX PubMed=7490292; DOI=10.1083/jcb.131.4.895;
RA Schroeder S., Schimmoeller F., Singer-Krueger B., Riezman H.;
RT "The Golgi-localization of yeast Emp47p depends on its di-lysine motif but
RT is not affected by the ret1-1 mutation in alpha-COP.";
RL J. Cell Biol. 131:895-912(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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 PROTEIN SEQUENCE OF 29-40.
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 [6]
RP FUNCTION, AND DOMAINS.
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 [7]
RP INTERACTION WITH EMP46, SUBUNIT, 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 [8]
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 [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1 ANGSTROMS) OF 29-282.
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. Required for the endoplasmic reticulum
CC exit of EMP46. {ECO:0000269|PubMed:12134087,
CC ECO:0000269|PubMed:14627716}.
CC -!- SUBUNIT: Homooligomers. Interacts with EMP46 in the endoplasmic
CC reticulum membrane. Interacts with the coatomer proteins COP1, SEC21
CC and SEC23. {ECO:0000269|PubMed:12857885}.
CC -!- INTERACTION:
CC P43555; Q12396: EMP46; NbExp=3; IntAct=EBI-6439, EBI-38641;
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 -!- MISCELLANEOUS: Present with 2900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EMP46/EMP47 family. {ECO:0000305}.
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DR EMBL; X87622; CAA60953.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09193.1; -; Genomic_DNA.
DR EMBL; AY693033; AAT93052.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12392.1; -; Genomic_DNA.
DR PIR; S56207; S56207.
DR RefSeq; NP_116606.1; NM_001179919.1.
DR PDB; 2A6Y; X-ray; 1.42 A; A=29-282.
DR PDB; 2A6Z; X-ray; 1.00 A; A=35-255.
DR PDB; 2A70; X-ray; 1.10 A; A/B=35-255.
DR PDB; 2A71; X-ray; 2.70 A; A/B/C/D=35-255.
DR PDBsum; 2A6Y; -.
DR PDBsum; 2A6Z; -.
DR PDBsum; 2A70; -.
DR PDBsum; 2A71; -.
DR AlphaFoldDB; P43555; -.
DR SMR; P43555; -.
DR BioGRID; 31099; 83.
DR DIP; DIP-7675N; -.
DR ELM; P43555; -.
DR IntAct; P43555; 38.
DR MINT; P43555; -.
DR STRING; 4932.YFL048C; -.
DR UniLectin; P43555; -.
DR MaxQB; P43555; -.
DR PaxDb; P43555; -.
DR PRIDE; P43555; -.
DR EnsemblFungi; YFL048C_mRNA; YFL048C; YFL048C.
DR GeneID; 850496; -.
DR KEGG; sce:YFL048C; -.
DR SGD; S000001846; EMP47.
DR VEuPathDB; FungiDB:YFL048C; -.
DR eggNOG; ENOG502QR1C; Eukaryota.
DR GeneTree; ENSGT00940000176827; -.
DR HOGENOM; CLU_050572_0_0_1; -.
DR InParanoid; P43555; -.
DR OMA; VMAYYTF; -.
DR BioCyc; YEAST:G3O-30417-MON; -.
DR Reactome; R-SCE-9013106; RHOC GTPase cycle.
DR EvolutionaryTrace; P43555; -.
DR PRO; PR:P43555; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43555; protein.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA: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:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:SGD.
DR GO; GO:0097367; F:carbohydrate derivative binding; IDA:SGD.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
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 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;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:8314797"
FT CHAIN 29..445
FT /note="Protein EMP47"
FT /id="PRO_0000021173"
FT TOPO_DOM 29..412
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..254
FT /note="L-type lectin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT REGION 430..433
FT /note="Mediates the interactions with COPI and COPII coat
FT complexes"
FT /evidence="ECO:0000250"
FT MOTIF 441..445
FT /note="Di-lysine motif"
FT DISULFID 179..213
FT CONFLICT 52
FT /note="A -> T (in Ref. 1; CAA60953)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="K -> N (in Ref. 1; CAA60953)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="V -> I (in Ref. 1; CAA60953)"
FT /evidence="ECO:0000305"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2A6Z"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2A6Y"
FT STRAND 96..106
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 152..164
FT /evidence="ECO:0007829|PDB:2A6Z"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:2A6Z"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 186..197
FT /evidence="ECO:0007829|PDB:2A6Z"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:2A6Z"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:2A6Z"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:2A6Z"
SQ SEQUENCE 445 AA; 50330 MW; 3978462BC2AFCD8A CRC64;
MMMLITMKST VLLSVFTVLA TWAGLLEAHP LGDTSDASKL SSDYSLPDLI NARKVPNNWQ
TGEQASLEEG RIVLTSKQNS KGSLWLKQGF DLKDSFTMEW TFRSVGYSGQ TDGGISFWFV
QDSNVPRDKQ LYNGPVNYDG LQLLVDNNGP LGPTLRGQLN DGQKPVDKTK IYDQSFASCL
MGYQDSSVPS TIRVTYDLED DNLLKVQVDN KVCFQTRKVR FPSGSYRIGV TAQNGAVNNN
AESFEIFKMQ FFNGVIEDSL IPNVNAMGQP KLITKYIDQQ TGKEKLIEKT AFDADKDKIT
NYELYKKLDR VEGKILANDI NALETKLNDV IKVQQELLSF MTTITKQLSS KPPANNEKGT
STDDAIAEDK ENFKDFLSIN QKLEKVLVEQ EKYREATKRH GQDGPQVDEI ARKLMIWLLP
LIFIMLVMAY YTFRIRQEII KTKLL
