ERV46_YEAST
ID ERV46_YEAST Reviewed; 415 AA.
AC P39727; D6VPH4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ER-derived vesicles protein ERV46;
GN Name=ERV46; OrderedLocusNames=YAL042W; ORFNames=FUN9;
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=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 [2]
RP SEQUENCE REVISION TO 405.
RA Vo D.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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 INTERACTION WITH ERV41, 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 ERV41, 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 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. The C-terminal Phe-Tyr motif is
CC required for exit from the endoplasmic reticulum. Facilitates
CC retrograde transport from the Golgi to the endoplasmic reticulum.
CC {ECO:0000269|PubMed:11157978, ECO:0000269|PubMed:12426381}.
CC -!- SUBUNIT: Interacts with ERV41. {ECO:0000269|PubMed:11157978,
CC ECO:0000269|PubMed:11758914}.
CC -!- INTERACTION:
CC P39727; Q04651: ERV41; NbExp=5; IntAct=EBI-20659, EBI-27850;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC protein. Note=Recycles between endoplasmic reticulum and Golgi. Resides
CC in the endoplasmic and Golgi compartments, and then packaged into
CC endoplasmic reticulum derived vesicles.
CC -!- SIMILARITY: Belongs to the ERGIC family. {ECO:0000305}.
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DR EMBL; U12980; AAC04989.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06944.1; -; Genomic_DNA.
DR PIR; S51977; S51977.
DR RefSeq; NP_009358.1; NM_001178187.1.
DR AlphaFoldDB; P39727; -.
DR BioGRID; 31785; 132.
DR ComplexPortal; CPX-1045; ERV41-ERV46 retrograde receptor complex.
DR DIP; DIP-3792N; -.
DR IntAct; P39727; 5.
DR MINT; P39727; -.
DR STRING; 4932.YAL042W; -.
DR MaxQB; P39727; -.
DR PaxDb; P39727; -.
DR PRIDE; P39727; -.
DR EnsemblFungi; YAL042W_mRNA; YAL042W; YAL042W.
DR GeneID; 851256; -.
DR KEGG; sce:YAL042W; -.
DR SGD; S000000040; ERV46.
DR VEuPathDB; FungiDB:YAL042W; -.
DR eggNOG; KOG2667; Eukaryota.
DR GeneTree; ENSGT00530000063113; -.
DR HOGENOM; CLU_034705_1_0_1; -.
DR InParanoid; P39727; -.
DR OMA; IGNFHIA; -.
DR BioCyc; YEAST:G3O-28850-MON; -.
DR PRO; PR:P39727; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39727; 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; IDA:ComplexPortal.
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: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 Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..415
FT /note="ER-derived vesicles protein ERV46"
FT /id="PRO_0000202419"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 402..403
FT /note="Phenylalanine-tyrosine motif"
SQ SEQUENCE 415 AA; 46235 MW; FB7BC171B88BB5EA CRC64;
MKRSTLLSLD AFAKTEEDVR VRTRAGGLIT LSCILTTLFL LVNEWGQFNS VVTRPQLVVD
RDRHAKLELN MDVTFPSMPC DLVNLDIMDD SGEMQLDILD AGFTMSRLNS EGRPVGDATE
LHVGGNGDGT APVNNDPNYC GPCYGAKDQS QNENLAQEEK VCCQDCDAVR SAYLEAGWAF
FDGKNIEQCE REGYVSKINE HLNEGCRIKG SAQINRIQGN LHFAPGKPYQ NAYGHFHDTS
LYDKTSNLNF NHIINHLSFG KPIQSHSKLL GNDKRHGGAV VATSPLDGRQ VFPDRNTHFH
QFSYFAKIVP TRYEYLDNVV IETAQFSATF HSRPLAGGRD KDHPNTLHVR GGIPGMFVFF
EMSPLKVINK EQHGQTWSGF ILNCITSIGG VLAVGTVMDK LFYKAQRSIW GKKSQ