YET2_YEAST
ID YET2_YEAST Reviewed; 160 AA.
AC Q04210; D6VZL5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Endoplasmic reticulum transmembrane protein 2;
GN Name=YET2; OrderedLocusNames=YMR040W; ORFNames=YM9532.05;
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 FUNCTION.
RA Toikkanen J.H., Fatal N., Hilden P., Makarow M., Kuismanen E.;
RT "YET1, YET2 and YET3 of Saccharomyces cerevisiae encode BAP31 homologs with
RT partially overlapping functions.";
RL J. Biol. Sci. (Faisalabad) 6:446-456(2006).
RN [4]
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: May play a role in anterograde transport of membrane proteins
CC from the endoplasmic reticulum to the Golgi. {ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family. {ECO:0000305}.
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DR EMBL; Z48502; CAA88406.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09939.1; -; Genomic_DNA.
DR PIR; S52889; S52889.
DR RefSeq; NP_013754.1; NM_001182537.1.
DR AlphaFoldDB; Q04210; -.
DR SMR; Q04210; -.
DR BioGRID; 35212; 53.
DR STRING; 4932.YMR040W; -.
DR PaxDb; Q04210; -.
DR EnsemblFungi; YMR040W_mRNA; YMR040W; YMR040W.
DR GeneID; 855056; -.
DR KEGG; sce:YMR040W; -.
DR SGD; S000004643; YET2.
DR VEuPathDB; FungiDB:YMR040W; -.
DR eggNOG; KOG1962; Eukaryota.
DR GeneTree; ENSGT00390000011863; -.
DR HOGENOM; CLU_087648_1_0_1; -.
DR InParanoid; Q04210; -.
DR OMA; EMAILFI; -.
DR BioCyc; YEAST:G3O-32745-MON; -.
DR PRO; PR:Q04210; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04210; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central.
DR InterPro; IPR008417; BAP29/BAP31.
DR InterPro; IPR040463; BAP29/BAP31_N.
DR PANTHER; PTHR12701; PTHR12701; 1.
DR Pfam; PF05529; Bap31; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; ER-Golgi transport; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..160
FT /note="Endoplasmic reticulum transmembrane protein 2"
FT /id="PRO_0000203275"
FT TOPO_DOM 1..2
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..103
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 157..160
FT /note="Di-lysine motif"
SQ SEQUENCE 160 AA; 19178 MW; D003EC7412559871 CRC64;
MGVYLAVLFS LLVIEMAILF ILVLPLPQRM RRWLYIRYSI ISTNKKFRTY MVGIMIFVGL
LFIDSWKRSQ IRVSTYRNQK NPYIINSVTP VDALASRAYN QRNVYISGFI IYFYICILTV
MSILRRIVEW NDKMKAGDDI LKEKLRRKQK YLEELQKKKF
