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   27-MAR-2024, entry version 187.
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; 138.
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; 4932-YFL048C; -.
DR   PeptideAtlas; P43555; -.
DR   EnsemblFungi; YFL048C_mRNA; YFL048C; YFL048C.
DR   GeneID; 850496; -.
DR   KEGG; sce:YFL048C; -.
DR   AGR; SGD:S000001846; -.
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   OrthoDB; 1332687at2759; -.
DR   BioCyc; YEAST:G3O-30417-MONOMER; -.
DR   BioGRID-ORCS; 850496; 9 hits in 10 CRISPR screens.
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; IDA:SGD.
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; 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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IGI:SGD.
DR   CDD; cd06903; lectin_EMP46_EMP47; 1.
DR   Gene3D; 2.60.120.200; -; 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   PANTHER; PTHR12223:SF40; PROTEIN EMP46-RELATED; 1.
DR   PANTHER; PTHR12223; VESICULAR MANNOSE-BINDING LECTIN; 1.
DR   Pfam; PF03388; Lectin_leg-like; 1.
DR   PIRSF; PIRSF018136; L-type_lectin_fungi; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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
//