ID   SOP4_YEAS7              Reviewed;         234 AA.
AC   A6ZQE4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Protein SOP4;
DE   AltName: Full=Suppressor of PMA1-7 protein 4;
DE   Flags: Precursor;
GN   Name=SOP4; ORFNames=SCY_3105;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Involved in the export of PMA1, possibly through the
CC       monitoring or assisting of PMA1 folding and acquisition of competence
CC       to enter vesicles. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SOP4 family. {ECO:0000305}.
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DR   EMBL; AAFW02000044; EDN63196.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZQE4; -.
DR   SMR; A6ZQE4; -.
DR   PRIDE; A6ZQE4; -.
DR   EnsemblFungi; EDN63196; EDN63196; SCY_3105.
DR   HOGENOM; CLU_102669_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR031395; Sop4.
DR   Pfam; PF17081; SOP4; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Protein transport; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..234
FT                   /note="Protein SOP4"
FT                   /id="PRO_0000324499"
FT   TOPO_DOM        19..188
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..234
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   234 AA;  26626 MW;  2D4751F6438C7B38 CRC64;
     MFSQIVLLLS AFIYVVSATA RRGTIKGRLD LAASNITGFV STRTSFKLYQ IGNFSTEYPY
     TSTTMFQDDE GNFEFANLPL NDGVNETTYY VMYPASMDFN LKPNRILIEF KNLENGTLQL
     NAFKNFFGRE YFPSKDITYP EKLQSMKVHP YITVELLHKA PIRSYLQARN VSIFSTGIVG
     NILNSRWKLA GVITLIALVV FPIIVEKLDP ETARAIREEA KRKQREKYAA VASK