ERP2_YEAST
ID ERP2_YEAST Reviewed; 215 AA.
AC P39704; D6VPL1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protein ERP2;
DE Flags: Precursor;
GN Name=ERP2; OrderedLocusNames=YAL007C; ORFNames=FUN54;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(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 CHARACTERIZATION.
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 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 [7]
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: Involved in vesicular protein trafficking.
CC -!- SUBUNIT: Associates with EMP24, ERV25 and ERP1.
CC -!- INTERACTION:
CC P39704; P32803: EMP24; NbExp=3; IntAct=EBI-6587, EBI-6431;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 26300 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; L22015; AAC04951.1; -; Genomic_DNA.
DR EMBL; AY558166; AAS56492.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06981.1; -; Genomic_DNA.
DR PIR; S43448; S43448.
DR RefSeq; NP_009395.1; NM_001178152.1.
DR AlphaFoldDB; P39704; -.
DR SMR; P39704; -.
DR BioGRID; 31759; 134.
DR ComplexPortal; CPX-1698; EMP24 complex.
DR DIP; DIP-5808N; -.
DR IntAct; P39704; 26.
DR MINT; P39704; -.
DR STRING; 4932.YAL007C; -.
DR MaxQB; P39704; -.
DR PaxDb; P39704; -.
DR PRIDE; P39704; -.
DR TopDownProteomics; P39704; -.
DR EnsemblFungi; YAL007C_mRNA; YAL007C; YAL007C.
DR GeneID; 851226; -.
DR KEGG; sce:YAL007C; -.
DR SGD; S000000005; ERP2.
DR VEuPathDB; FungiDB:YAL007C; -.
DR eggNOG; KOG1693; Eukaryota.
DR GeneTree; ENSGT00940000166069; -.
DR HOGENOM; CLU_066963_4_2_1; -.
DR InParanoid; P39704; -.
DR OMA; FATGGRM; -.
DR BioCyc; YEAST:G3O-28820-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:P39704; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39704; protein.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA: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: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 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 Endoplasmic reticulum; ER-Golgi transport; Membrane; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..215
FT /note="Protein ERP2"
FT /id="PRO_0000010409"
FT TOPO_DOM 26..182
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..123
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
SQ SEQUENCE 215 AA; 24064 MW; 82560055D590954F CRC64;
MIKSTIALPS FFIVLILALV NSVAASSSYA PVAISLPAFS KECLYYDMVT EDDSLAVGYQ
VLTGGNFEID FDITAPDGSV ITSEKQKKYS DFLLKSFGVG KYTFCFSNNY GTALKKVEIT
LEKEKTLTDE HEADVNNDDI IANNAVEEID RNLNKITKTL NYLRAREWRN MSTVNSTESR
LTWLSILIII IIAVISIAQV LLIQFLFTGR QKNYV
