ERV29_YEAST
ID ERV29_YEAST Reviewed; 310 AA.
AC P53337; D6VV61; E9P8T4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ER-derived vesicles protein ERV29;
GN Name=ERV29; OrderedLocusNames=YGR284C;
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 96604 / S288c / FY1679;
RX PubMed=9090054;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<251::aid-yea63>3.0.co;2-r;
RA Volckaert G., Voet M., Robben J.;
RT "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right
RT arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus
RT reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2
RT genes and an ABC transporter gene.";
RL Yeast 13:251-259(1997).
RN [2]
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 [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 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.
RX PubMed=11711675; DOI=10.1126/science.1065224;
RA Belden W.J., Barlowe C.;
RT "Role of Erv29p in collecting soluble secretory proteins into ER-derived
RT transport vesicles.";
RL Science 294:1528-1531(2001).
RN [7]
RP FUNCTION.
RX PubMed=15516922; DOI=10.1038/ncb1195;
RA Otte S., Barlowe C.;
RT "Sorting signals can direct receptor-mediated export of soluble proteins
RT into COPII vesicles.";
RL Nat. Cell Biol. 6:1189-1194(2004).
RN [8]
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).
RN [9]
RP TOPOLOGY.
RX PubMed=17520482; DOI=10.1080/09687860601178518;
RA Foley D.A., Sharpe H.J., Otte S.;
RT "Membrane topology of the endoplasmic reticulum to Golgi transport factor
RT Erv29p.";
RL Mol. Membr. Biol. 24:259-268(2007).
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 di-lysine motif is
CC required for exit from the endoplasmic reticulum. Required directly for
CC packaging glycosylated pro-alpha-factor into COPII vesicles.
CC Facilitates retrograde transport from the Golgi to the endoplasmic
CC reticulum. {ECO:0000269|PubMed:11711675, ECO:0000269|PubMed:15516922}.
CC -!- INTERACTION:
CC P53337; P38353: SSH1; NbExp=3; IntAct=EBI-23662, EBI-18175;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11157978}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11157978}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250|UniProtKB:O15260}.
CC -!- SIMILARITY: Belongs to the SURF4 family. {ECO:0000305}.
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DR EMBL; Z73069; CAA97315.1; -; Genomic_DNA.
DR EMBL; AY557829; AAS56155.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08372.1; -; Genomic_DNA.
DR PIR; S64619; S64619.
DR RefSeq; NP_011800.3; NM_001181413.3.
DR AlphaFoldDB; P53337; -.
DR BioGRID; 33534; 295.
DR DIP; DIP-8110N; -.
DR IntAct; P53337; 45.
DR MINT; P53337; -.
DR STRING; 4932.YGR284C; -.
DR TCDB; 9.B.214.1.1; the er to golgi transport factor (er/g-tf) family.
DR iPTMnet; P53337; -.
DR MaxQB; P53337; -.
DR PaxDb; P53337; -.
DR PRIDE; P53337; -.
DR TopDownProteomics; P53337; -.
DR EnsemblFungi; YGR284C_mRNA; YGR284C; YGR284C.
DR GeneID; 853201; -.
DR KEGG; sce:YGR284C; -.
DR SGD; S000003516; ERV29.
DR VEuPathDB; FungiDB:YGR284C; -.
DR eggNOG; KOG3998; Eukaryota.
DR GeneTree; ENSGT00530000064123; -.
DR HOGENOM; CLU_056195_0_0_1; -.
DR InParanoid; P53337; -.
DR OMA; RHRHFPW; -.
DR BioCyc; YEAST:G3O-30946-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:P53337; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53337; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097020; F:COPII receptor activity; IMP:SGD.
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 InterPro; IPR045214; Surf1/Surf4.
DR InterPro; IPR002995; Surf4.
DR PANTHER; PTHR23427; PTHR23427; 1.
DR Pfam; PF02077; SURF4; 1.
DR PROSITE; PS01339; SURF4; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..310
FT /note="ER-derived vesicles protein ERV29"
FT /id="PRO_0000127671"
FT TOPO_DOM 1..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17520482"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..137
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:17520482"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17520482"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..245
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:17520482"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17520482"
FT REGION 11..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 307..310
FT /note="Di-lysine motif"
FT COMPBIAS 12..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 64
FT /note="Y -> C (in Ref. 4; AAS56155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 35013 MW; 6AE744904294DC76 CRC64;
MSYRGPIGNF GGMPMSSSQG PYSGGAQFRS NQNQSTSGIL KQWKHSFEKF ASRIEGLTDN
AVVYKLKPYI PSLSRFFIVA TFYEDSFRIL SQWSDQIFYL NKWKHYPYFF VVVFLVVVTV
SMLIGASLLV LRKQTNYATG VLCACVISQA LVYGLFTGSS FVLRNFSVIG GLLIAFSDSI
VQNKTTFGML PELNSKNDKA KGYLLFAGRI LIVLMFIAFT FSKSWFTVVL TIIGTICFAI
GYKTKFASIM LGLILTFYNI TLNNYWFYNN TKRDFLKYEF YQNLSIIGGL LLVTNTGAGE
LSVDEKKKIY
