ERV41_YEAST
ID ERV41_YEAST Reviewed; 352 AA.
AC Q04651; D6VZA6; E9PAD9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=ER-derived vesicles protein ERV41;
GN Name=ERV41; OrderedLocusNames=YML067C;
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 4-10, 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 [4]
RP INTERACTION WITH ERV46, AND SUBCELLULAR LOCATION.
RX PubMed=11758914; DOI=10.1271/bbb.65.2226;
RA Cho J.-H., Noda Y., Adachi H., Yoda K.;
RT "A novel membrane protein complex on the endoplasmic reticulum and early
RT Golgi compartments in the yeast Saccharomyces cerevisiae.";
RL Biosci. Biotechnol. Biochem. 65:2226-2232(2001).
RN [5]
RP FUNCTION, INTERACTION WITH ERV46, AND SUBCELLULAR LOCATION.
RX PubMed=11157978; DOI=10.1083/jcb.152.3.503;
RA Otte S., Belden W.J., Heidtman M., Liu J., Jensen O.N., Barlowe C.;
RT "Erv41p and Erv46p: new components of COPII vesicles involved in transport
RT between the ER and Golgi complex.";
RL J. Cell Biol. 152:503-518(2001).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12426381; DOI=10.1093/emboj/cdf598;
RA Otte S., Barlowe C.;
RT "The Erv41p-Erv46p complex: multiple export signals are required in trans
RT for COPII-dependent transport from the ER.";
RL EMBO J. 21:6095-6104(2002).
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).
RN [9] {ECO:0007744|PDB:3ZLC}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 49-297.
RX PubMed=23524136; DOI=10.1016/j.jmb.2013.03.024;
RA Biterova E.I., Svard M., Possner D.D., Guy J.E.;
RT "The crystal structure of the lumenal domain of Erv41p, a protein involved
RT in transport between the endoplasmic reticulum and Golgi apparatus.";
RL J. Mol. Biol. 425:2208-2218(2013).
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 (PubMed:11157978, PubMed:12426381). The
CC C-terminal Ile-Leu motif is required for exit from the endoplasmic
CC reticulum (PubMed:12426381). Facilitates retrograde transport from the
CC Golgi to the endoplasmic reticulum (PubMed:12426381).
CC {ECO:0000269|PubMed:11157978, ECO:0000269|PubMed:12426381}.
CC -!- SUBUNIT: Interacts with ERV46. {ECO:0000269|PubMed:11157978,
CC ECO:0000269|PubMed:11758914}.
CC -!- INTERACTION:
CC Q04651; Q04651: ERV41; NbExp=3; IntAct=EBI-27850, EBI-27850;
CC Q04651; P39727: ERV46; NbExp=5; IntAct=EBI-27850, EBI-20659;
CC Q04651; P41810: SEC26; NbExp=3; IntAct=EBI-27850, EBI-4869;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11758914, ECO:0000269|PubMed:12426381}; Multi-pass
CC membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:10713261, ECO:0000269|PubMed:11758914,
CC ECO:0000269|PubMed:12426381, ECO:0000269|PubMed:16107716}; Multi-pass
CC membrane protein. Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000269|PubMed:11157978, ECO:0000269|PubMed:12426381}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Recycles between endoplasmic
CC reticulum and Golgi. Resides in the endoplasmic and Golgi compartments,
CC and then packaged into endoplasmic reticulum derived vesicles.
CC {ECO:0000269|PubMed:12426381}.
CC -!- MISCELLANEOUS: Present with 3000 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ERGIC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA86253.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z38114; CAA86253.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z38114; CAA86254.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09830.1; -; Genomic_DNA.
DR PIR; S48331; S48331.
DR RefSeq; NP_013644.1; NM_001182426.1.
DR PDB; 3ZLC; X-ray; 2.00 A; A/B=49-297.
DR PDBsum; 3ZLC; -.
DR AlphaFoldDB; Q04651; -.
DR SMR; Q04651; -.
DR BioGRID; 35099; 162.
DR ComplexPortal; CPX-1045; ERV41-ERV46 retrograde receptor complex.
DR DIP; DIP-6791N; -.
DR IntAct; Q04651; 29.
DR MINT; Q04651; -.
DR STRING; 4932.YML067C; -.
DR iPTMnet; Q04651; -.
DR MaxQB; Q04651; -.
DR PaxDb; Q04651; -.
DR PRIDE; Q04651; -.
DR EnsemblFungi; YML067C_mRNA; YML067C; YML067C.
DR GeneID; 854935; -.
DR KEGG; sce:YML067C; -.
DR SGD; S000004532; ERV41.
DR VEuPathDB; FungiDB:YML067C; -.
DR eggNOG; KOG2667; Eukaryota.
DR GeneTree; ENSGT00530000063113; -.
DR HOGENOM; CLU_034705_2_1_1; -.
DR InParanoid; Q04651; -.
DR OMA; TYQYSVK; -.
DR BioCyc; YEAST:G3O-32662-MON; -.
DR PRO; PR:Q04651; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04651; 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; IDA:ComplexPortal.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IDA:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0061852; C:retrograte transporter complex, Golgi to ER; IPI:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IGI:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:ComplexPortal.
DR InterPro; IPR045888; Erv.
DR InterPro; IPR012936; Erv_C.
DR InterPro; IPR039542; Erv_N.
DR PANTHER; PTHR10984; PTHR10984; 1.
DR Pfam; PF07970; COPIIcoated_ERV; 1.
DR Pfam; PF13850; ERGIC_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Direct protein sequencing;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..352
FT /note="ER-derived vesicles protein ERV41"
FT /id="PRO_0000203251"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..311
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 349..350
FT /note="Isoleucine-leucine motif"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 63..75
FT /evidence="ECO:0007829|PDB:3ZLC"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:3ZLC"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3ZLC"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 162..181
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:3ZLC"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:3ZLC"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 233..245
FT /evidence="ECO:0007829|PDB:3ZLC"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:3ZLC"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:3ZLC"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:3ZLC"
SQ SEQUENCE 352 AA; 40706 MW; A9F002FB97666501 CRC64;
MAGLKTFDAF PKTEEQYKKK STKGGLTSLL TYLFLLFIAW TEFGEYFGGY IDQQYVVDSQ
VRDTVQINMD IYVNTKCDWL QINVRDQTMD RKLVLEELQL EEMPFFIPYD TKVNDINEII
TPELDEILGE AIPAEFREKL DTRSFFDESD PNKAHLPEFN GCHVFGSIPV NRVSGELQIT
AKSLGYVASR KAPLEELKFN HVINEFSFGD FYPYIDNPLD NTAQFNQDEP LTTYVYYTSV
VPTLFKKLGA EVDTNQYSVN DYRYLYKDVA AKGDKMPGIF FKYNFEPLSI VVSDVRLSFI
QFLVRLVAIC SFLVYCASWI FTLLDMALIT IMGPKWSLRY QPDDKTKGIL DR
