ID   TMEDA_YEAST             Reviewed;         211 AA.
AC   P54837; D6VZG2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Endoplasmic reticulum vesicle protein 25;
DE   Flags: Precursor;
GN   Name=ERV25; OrderedLocusNames=YML012W; ORFNames=YM9571.06;
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=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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 21-36, FUNCTION, INTERACTION WITH EMP24, SUBCELLULAR
RP   LOCATION, AND LACK OF GLYCOSYLATION.
RX   PubMed=8900179; DOI=10.1074/jbc.271.43.26939;
RA   Belden W.J., Barlowe C.;
RT   "Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p
RT   that is required for efficient endoplasmic reticulum to Golgi transport.";
RL   J. Biol. Chem. 271:26939-26946(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 21-25, AND SUBCELLULAR LOCATION.
RX   PubMed=10713261; DOI=10.1016/s0014-5793(00)01268-0;
RA   Cho J.-H., Noda Y., Yoda K.;
RT   "Proteins in the early Golgi compartment of Saccharomyces cerevisiae
RT   immunoisolated by Sed5p.";
RL   FEBS Lett. 469:151-154(2000).
RN   [5]
RP   INTERACTION WITH EMP24; ERP1 AND ERP2.
RX   PubMed=10359606; DOI=10.1091/mbc.10.6.1923;
RA   Marzioch M., Henthorn D.C., Herrmann J.M., Wilson R., Thomas D.Y.,
RA   Bergeron J.J.M., Solari R.C., Rowley A.;
RT   "Erp1p and Erp2p, partners for Emp24p and Erv25p in a yeast p24 complex.";
RL   Mol. Biol. Cell 10:1923-1938(1999).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 206-LYS--LYS-208.
RX   PubMed=11560939; DOI=10.1074/jbc.m108113200;
RA   Belden W.J., Barlowe C.;
RT   "Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in
RT   transport between the endoplasmic reticulum and Golgi complex.";
RL   J. Biol. Chem. 276:43040-43048(2001).
RN   [7]
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   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16107716; DOI=10.1128/mcb.25.17.7696-7710.2005;
RA   Inadome H., Noda Y., Adachi H., Yoda K.;
RT   "Immunoisolation of the yeast Golgi subcompartments and characterization of
RT   a novel membrane protein, Svp26, discovered in the Sed5-containing
RT   compartments.";
RL   Mol. Cell. Biol. 25:7696-7710(2005).
CC   -!- FUNCTION: Constituent of COPII-coated endoplasmic reticulum-derived
CC       transport vesicles. Required for efficient transport of a subset of
CC       secretory proteins to the Golgi. Possesses a C-terminal dilysine motif
CC       that interacts with COPI coat subunits. Facilitates retrograde
CC       transport from the Golgi to the endoplasmic reticulum.
CC       {ECO:0000269|PubMed:11560939, ECO:0000269|PubMed:8900179}.
CC   -!- SUBUNIT: Associates with EMP24, ERP1 and ERP2.
CC   -!- INTERACTION:
CC       P54837; P32803: EMP24; NbExp=3; IntAct=EBI-6642, EBI-6431;
CC       P54837; Q05359: ERP1; NbExp=5; IntAct=EBI-6642, EBI-6581;
CC       P54837; P38819: ERP5; NbExp=3; IntAct=EBI-6642, EBI-6603;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC       I membrane protein. Golgi apparatus membrane; Single-pass type I
CC       membrane protein. Note=Recycles between endoplasmic reticulum and
CC       Golgi.
CC   -!- MISCELLANEOUS: Present with 51700 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR   EMBL; Z49810; CAA89940.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09886.1; -; Genomic_DNA.
DR   PIR; S55107; S55107.
DR   RefSeq; NP_013701.1; NM_001182369.1.
DR   AlphaFoldDB; P54837; -.
DR   SMR; P54837; -.
DR   BioGRID; 35157; 333.
DR   ComplexPortal; CPX-1698; EMP24 complex.
DR   DIP; DIP-2134N; -.
DR   IntAct; P54837; 68.
DR   MINT; P54837; -.
DR   STRING; 4932.YML012W; -.
DR   PaxDb; 4932-YML012W; -.
DR   PeptideAtlas; P54837; -.
DR   EnsemblFungi; YML012W_mRNA; YML012W; YML012W.
DR   GeneID; 854997; -.
DR   KEGG; sce:YML012W; -.
DR   AGR; SGD:S000004473; -.
DR   SGD; S000004473; ERV25.
DR   VEuPathDB; FungiDB:YML012W; -.
DR   eggNOG; KOG1691; Eukaryota.
DR   GeneTree; ENSGT00550000074954; -.
DR   HOGENOM; CLU_066963_3_0_1; -.
DR   InParanoid; P54837; -.
DR   OMA; GWQIMYL; -.
DR   OrthoDB; 1090443at2759; -.
DR   BioCyc; YEAST:G3O-32616-MONOMER; -.
DR   Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   BioGRID-ORCS; 854997; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P54837; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P54837; Protein.
DR   GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:ComplexPortal.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005798; C:Golgi-associated vesicle; NAS:ComplexPortal.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IPI:SGD.
DR   GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0006900; P:vesicle budding from membrane; NAS:ComplexPortal.
DR   InterPro; IPR015720; Emp24-like.
DR   InterPro; IPR009038; GOLD_dom.
DR   PANTHER; PTHR22811; TRANSMEMBRANE EMP24 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22811:SF184; TRANSMEMBRANE EMP24 DOMAIN-CONTAINING PROTEIN 10; 1.
DR   Pfam; PF01105; EMP24_GP25L; 1.
DR   SMART; SM01190; EMP24_GP25L; 1.
DR   PROSITE; PS50866; GOLD; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW   Golgi apparatus; Membrane; Protein transport; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:10713261,
FT                   ECO:0000269|PubMed:8900179"
FT   CHAIN           21..211
FT                   /note="Endoplasmic reticulum vesicle protein 25"
FT                   /id="PRO_0000010414"
FT   TOPO_DOM        21..180
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..211
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          33..121
FT                   /note="GOLD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT   MUTAGEN         206..208
FT                   /note="KTK->ATA: Decrease in COPI-binding."
FT                   /evidence="ECO:0000269|PubMed:11560939"
SQ   SEQUENCE   211 AA;  24106 MW;  8E5ECE0336B1F885 CRC64;
     MQVLQLWLTT LISLVVAVQG LHFDIAASTD PEQVCIRDFV TEGQLVVADI HSDGSVGDGQ
     KLNLFVRDSV GNEYRRKRDF AGDVRVAFTA PSSTAFDVCF ENQAQYRGRS LSRAIELDIE
     SGAEARDWNK ISANEKLKPI EVELRRVEEI TDEIVDELTY LKNREERLRD TNESTNRRVR
     NFSILVIIVL SSLGVWQVNY LKNYFKTKHI I
//