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P43555

- EMP47_YEAST

UniProt

P43555 - EMP47_YEAST

Protein

Protein EMP47

Gene

EMP47

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Involved in the secretion of glycoproteins and in nucleus architecture and gene silencing. Required for the endoplasmic reticulum exit of EMP46.2 Publications

    GO - Molecular functioni

    1. glycoprotein binding Source: SGD

    GO - Biological processi

    1. ER to Golgi vesicle-mediated transport Source: SGD

    Keywords - Ligandi

    Lectin

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30417-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein EMP47
    Alternative name(s):
    47 kDa endomembrane protein
    Endosomal P44 protein
    Gene namesi
    Name:EMP47
    Ordered Locus Names:YFL048C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VI

    Organism-specific databases

    CYGDiYFL048c.
    SGDiS000001846. EMP47.

    Subcellular locationi

    GO - Cellular componenti

    1. ER to Golgi transport vesicle Source: SGD
    2. integral component of endoplasmic reticulum membrane Source: SGD
    3. integral component of Golgi membrane Source: SGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 28281 PublicationAdd
    BLAST
    Chaini29 – 445417Protein EMP47PRO_0000021173Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi179 ↔ 213

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP43555.
    PaxDbiP43555.
    PeptideAtlasiP43555.

    Expressioni

    Gene expression databases

    GenevestigatoriP43555.

    Interactioni

    Subunit structurei

    Homooligomers. Interacts with EMP46 in the endoplasmic reticulum membrane. Interacts with the coatomer proteins COP1, SEC21 and SEC23.1 Publication

    Protein-protein interaction databases

    BioGridi31099. 45 interactions.
    DIPiDIP-7675N.
    IntActiP43555. 38 interactions.
    MINTiMINT-1355466.
    STRINGi4932.YFL048C.

    Structurei

    Secondary structure

    1
    445
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi37 – 393
    Helixi42 – 443
    Beta strandi59 – 635
    Beta strandi66 – 683
    Beta strandi71 – 744
    Beta strandi81 – 888
    Beta strandi90 – 945
    Beta strandi96 – 10611
    Beta strandi114 – 1218
    Beta strandi123 – 1253
    Beta strandi139 – 1479
    Beta strandi152 – 16413
    Helixi168 – 1703
    Helixi171 – 1744
    Beta strandi176 – 1805
    Beta strandi186 – 19712
    Helixi198 – 2003
    Beta strandi201 – 2088
    Beta strandi211 – 2177
    Beta strandi223 – 23311
    Helixi237 – 2393
    Beta strandi243 – 25311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A6YX-ray1.42A29-282[»]
    2A6ZX-ray1.00A35-255[»]
    2A70X-ray1.10A/B35-255[»]
    2A71X-ray2.70A/B/C/D35-255[»]
    ProteinModelPortaliP43555.
    SMRiP43555. Positions 35-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43555.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 412384LumenalSequence AnalysisAdd
    BLAST
    Topological domaini434 – 44512CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei413 – 43321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 254219L-type lectin-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni430 – 4334Mediates the interactions with COPI and COPII coat complexesBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi441 – 4455Di-lysine motif

    Domaini

    The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.By similarity

    Sequence similaritiesi

    Belongs to the EMP46/EMP47 family.Curated
    Contains 1 L-type lectin-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG68488.
    GeneTreeiENSGT00510000053646.
    HOGENOMiHOG000112365.
    OMAiLVMAYYT.
    OrthoDBiEOG7N6414.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR016710. L-typ_lectin_fun.
    IPR005052. Lectin_leg.
    [Graphical view]
    PANTHERiPTHR12223. PTHR12223. 1 hit.
    PfamiPF03388. Lectin_leg-like. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018136. L-type_lectin_fungi. 1 hit.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS51328. L_LECTIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P43555-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMMLITMKST VLLSVFTVLA TWAGLLEAHP LGDTSDASKL SSDYSLPDLI    50
    NARKVPNNWQ TGEQASLEEG RIVLTSKQNS KGSLWLKQGF DLKDSFTMEW 100
    TFRSVGYSGQ TDGGISFWFV QDSNVPRDKQ LYNGPVNYDG LQLLVDNNGP 150
    LGPTLRGQLN DGQKPVDKTK IYDQSFASCL MGYQDSSVPS TIRVTYDLED 200
    DNLLKVQVDN KVCFQTRKVR FPSGSYRIGV TAQNGAVNNN AESFEIFKMQ 250
    FFNGVIEDSL IPNVNAMGQP KLITKYIDQQ TGKEKLIEKT AFDADKDKIT 300
    NYELYKKLDR VEGKILANDI NALETKLNDV IKVQQELLSF MTTITKQLSS 350
    KPPANNEKGT STDDAIAEDK ENFKDFLSIN QKLEKVLVEQ EKYREATKRH 400
    GQDGPQVDEI ARKLMIWLLP LIFIMLVMAY YTFRIRQEII KTKLL 445
    Length:445
    Mass (Da):50,330
    Last modified:November 1, 1995 - v1
    Checksum:i3978462BC2AFCD8A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521A → T in CAA60953. (PubMed:7490292)Curated
    Sequence conflicti77 – 771K → N in CAA60953. (PubMed:7490292)Curated
    Sequence conflicti125 – 1251V → I in CAA60953. (PubMed:7490292)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87622 Genomic DNA. Translation: CAA60953.1.
    D50617 Genomic DNA. Translation: BAA09193.1.
    AY693033 Genomic DNA. Translation: AAT93052.1.
    BK006940 Genomic DNA. Translation: DAA12392.1.
    PIRiS56207.
    RefSeqiNP_116606.1. NM_001179919.1.

    Genome annotation databases

    EnsemblFungiiYFL048C; YFL048C; YFL048C.
    GeneIDi850496.
    KEGGisce:YFL048C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87622 Genomic DNA. Translation: CAA60953.1 .
    D50617 Genomic DNA. Translation: BAA09193.1 .
    AY693033 Genomic DNA. Translation: AAT93052.1 .
    BK006940 Genomic DNA. Translation: DAA12392.1 .
    PIRi S56207.
    RefSeqi NP_116606.1. NM_001179919.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2A6Y X-ray 1.42 A 29-282 [» ]
    2A6Z X-ray 1.00 A 35-255 [» ]
    2A70 X-ray 1.10 A/B 35-255 [» ]
    2A71 X-ray 2.70 A/B/C/D 35-255 [» ]
    ProteinModelPortali P43555.
    SMRi P43555. Positions 35-255.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31099. 45 interactions.
    DIPi DIP-7675N.
    IntActi P43555. 38 interactions.
    MINTi MINT-1355466.
    STRINGi 4932.YFL048C.

    Proteomic databases

    MaxQBi P43555.
    PaxDbi P43555.
    PeptideAtlasi P43555.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YFL048C ; YFL048C ; YFL048C .
    GeneIDi 850496.
    KEGGi sce:YFL048C.

    Organism-specific databases

    CYGDi YFL048c.
    SGDi S000001846. EMP47.

    Phylogenomic databases

    eggNOGi NOG68488.
    GeneTreei ENSGT00510000053646.
    HOGENOMi HOG000112365.
    OMAi LVMAYYT.
    OrthoDBi EOG7N6414.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30417-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P43555.
    NextBioi 966182.

    Gene expression databases

    Genevestigatori P43555.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR016710. L-typ_lectin_fun.
    IPR005052. Lectin_leg.
    [Graphical view ]
    PANTHERi PTHR12223. PTHR12223. 1 hit.
    Pfami PF03388. Lectin_leg-like. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018136. L-type_lectin_fungi. 1 hit.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS51328. L_LECTIN_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the ret1-1 mutation in alpha-COP."
      Schroeder S., Schimmoeller F., Singer-Krueger B., Riezman H.
      J. Cell Biol. 131:895-912(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Partial purification and characterization of early and late endosomes from yeast. Identification of four novel proteins."
      Singer-Krueger B., Frank R., Crausaz F., Riezman H.
      J. Biol. Chem. 268:14376-14386(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-40.
      Strain: RH732.
    6. "Emp47p and its close homolog Emp46p have a tyrosine-containing endoplasmic reticulum exit signal and function in glycoprotein secretion in Saccharomyces cerevisiae."
      Sato K., Nakano A.
      Mol. Biol. Cell 13:2518-2532(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAINS.
    7. "Oligomerization of a cargo receptor directs protein sorting into COPII-coated transport vesicles."
      Sato K., Nakano A.
      Mol. Biol. Cell 14:3055-3063(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EMP46, SUBUNIT, SUBCELLULAR LOCATION.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "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."
      Sato K., Nakano A.
      J. Biol. Chem. 279:1330-1335(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p."
      Satoh T., Sato K., Kanoh A., Yamashita K., Yamada Y., Igarashi N., Kato R., Nakano A., Wakatsuki S.
      J. Biol. Chem. 281:10410-10419(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1 ANGSTROMS) OF 29-282.

    Entry informationi

    Entry nameiEMP47_YEAST
    AccessioniPrimary (citable) accession number: P43555
    Secondary accession number(s): D6VTI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2900 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VI
      Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

    External Data

    Dasty 3