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   27-MAR-2024, entry version 155.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 188.
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; 4932-YML067C; -.
DR   PeptideAtlas; Q04651; -.
DR   EnsemblFungi; YML067C_mRNA; YML067C; YML067C.
DR   GeneID; 854935; -.
DR   KEGG; sce:YML067C; -.
DR   AGR; SGD:S000004532; -.
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; EDTWWEL; -.
DR   OrthoDB; 8790at2759; -.
DR   BioCyc; YEAST:G3O-32662-MONOMER; -.
DR   BioGRID-ORCS; 854935; 4 hits in 10 CRISPR screens.
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:SGD.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0061852; C:retrograde 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; ENDOPLASMIC RETICULUM-GOLGI INTERMEDIATE COMPARTMENT PROTEIN; 1.
DR   PANTHER; PTHR10984:SF30; ENDOPLASMIC RETICULUM-GOLGI INTERMEDIATE COMPARTMENT PROTEIN 2; 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
//