EMP24_YEAST
ID EMP24_YEAST Reviewed; 203 AA.
AC P32803; D6VTV4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Endosomal protein P24B;
DE AltName: Full=24 kDa endomembrane protein;
DE AltName: Full=Basic 24 kDa late endocytic intermediate component;
DE Flags: Precursor;
GN Name=EMP24; OrderedLocusNames=YGL200C; ORFNames=G1271;
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].
RX PubMed=7729411; DOI=10.1002/j.1460-2075.1995.tb07119.x;
RA Schimmoeller F., Singer-Krueger B., Schroeder S., Krueger U., Barlowe C.,
RA Riezman H.;
RT "The absence of Emp24p, a component of ER-derived COPII-coated vesicles,
RT causes a defect in transport of selected proteins to the Golgi.";
RL EMBO J. 14:1329-1339(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bjourson A.J., McReynolds A.D.K., Wright L.F.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-169.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046087;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<55::aid-yea48>3.0.co;2-9;
RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT from Saccharomyces cerevisiae.";
RL Yeast 13:55-64(1997).
RN [6]
RP PROTEIN SEQUENCE OF 21-37.
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 [7]
RP INTERACTION WITH ERV25.
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 [8]
RP INTERACTION WITH ERV25; 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 [9]
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SAR1; SEC23 AND SEC24, AND
RP MUTAGENESIS OF 202-LYS-VAL-203.
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 [11]
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 [12]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
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. {ECO:0000269|PubMed:11560939}.
CC -!- SUBUNIT: Associates with ERV25, ERP1 and ERP2. Interacts also with
CC SAR1, SEC23 and SEC24. {ECO:0000269|PubMed:10359606,
CC ECO:0000269|PubMed:11560939, ECO:0000269|PubMed:8900179}.
CC -!- INTERACTION:
CC P32803; P39704: ERP2; NbExp=3; IntAct=EBI-6431, EBI-6587;
CC P32803; Q12450: ERP4; NbExp=3; IntAct=EBI-6431, EBI-6598;
CC P32803; P54837: ERV25; NbExp=3; IntAct=EBI-6431, EBI-6642;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10713261}; Single-pass type I membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:11560939};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Recycles
CC between endoplasmic reticulum and Golgi (PubMed:11560939).
CC {ECO:0000269|PubMed:11560939}.
CC -!- MISCELLANEOUS: Present with 26800 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; X67317; CAA47731.1; -; Genomic_DNA.
DR EMBL; Z72722; CAA96912.1; -; Genomic_DNA.
DR EMBL; X91837; CAA62944.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07915.1; -; Genomic_DNA.
DR PIR; S25109; S25109.
DR RefSeq; NP_011315.3; NM_001181065.3.
DR AlphaFoldDB; P32803; -.
DR SMR; P32803; -.
DR BioGRID; 33058; 215.
DR ComplexPortal; CPX-1698; EMP24 complex.
DR DIP; DIP-2856N; -.
DR ELM; P32803; -.
DR IntAct; P32803; 22.
DR MINT; P32803; -.
DR STRING; 4932.YGL200C; -.
DR MaxQB; P32803; -.
DR PaxDb; P32803; -.
DR PRIDE; P32803; -.
DR TopDownProteomics; P32803; -.
DR EnsemblFungi; YGL200C_mRNA; YGL200C; YGL200C.
DR GeneID; 852675; -.
DR KEGG; sce:YGL200C; -.
DR SGD; S000003168; EMP24.
DR VEuPathDB; FungiDB:YGL200C; -.
DR eggNOG; KOG1692; Eukaryota.
DR GeneTree; ENSGT00940000175999; -.
DR HOGENOM; CLU_066963_4_0_1; -.
DR InParanoid; P32803; -.
DR OMA; WNLFVIG; -.
DR BioCyc; YEAST:G3O-30680-MON; -.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:P32803; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32803; protein.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
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; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP: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:0006621; P:protein retention in ER lumen; IMP:SGD.
DR GO; GO:0006900; P:vesicle budding from membrane; IC:ComplexPortal.
DR GO; GO:0016050; P:vesicle organization; IMP:SGD.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR SUPFAM; SSF101576; SSF101576; 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:8314797"
FT CHAIN 21..203
FT /note="Endosomal protein P24B"
FT /id="PRO_0000010407"
FT TOPO_DOM 21..172
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..118
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT MUTAGEN 202..203
FT /note="LV->AA: No change in COPII-binding."
FT /evidence="ECO:0000269|PubMed:11560939"
FT CONFLICT 32
FT /note="C -> H (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 23332 MW; 9B9E46982FA62B07 CRC64;
MASFATKFVI ACFLFFSASA HNVLLPAYGR RCFFEDLSKG DELSISFQFG DRNPQSSSQL
TGDFIIYGPE RHEVLKTVRD TSHGEITLSA PYKGHFQYCF LNENTGIETK DVTFNIHGVV
YVDLDDPNTN TLDSAVRKLS KLTREVKDEQ SYIVIRERTH RNTAESTNDR VKWWSIFQLG
VVIANSLFQI YYLRRFFEVT SLV
