SOP4_YEAST
ID SOP4_YEAST Reviewed; 234 AA.
AC P39543; D6VVZ9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein SOP4;
DE AltName: Full=Suppressor of PMA1-7 protein 4;
DE Flags: Precursor;
GN Name=SOP4; OrderedLocusNames=YJL192C; ORFNames=J0351;
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 204508 / S288c;
RX PubMed=7754713; DOI=10.1002/yea.320100912;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of a 36 kb segment on the left arm of yeast chromosome X
RT identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6,
RT CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two
RT homologues to chromosome III genes.";
RL Yeast 10:1235-1249(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 FUNCTION.
RX PubMed=9265642; DOI=10.1083/jcb.138.4.731;
RA Luo W.-J., Chang A.;
RT "Novel genes involved in endosomal traffic in yeast revealed by suppression
RT of a targeting-defective plasma membrane ATPase mutant.";
RL J. Cell Biol. 138:731-746(1997).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12230471; DOI=10.1034/j.1600-0854.2002.31005.x;
RA Luo W.J., Gong X.H., Chang A.;
RT "An ER membrane protein, Sop4, facilitates ER export of the yeast plasma
RT membrane [H+]ATPase, Pma1.";
RL Traffic 3:730-739(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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).
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:0000269|PubMed:12230471,
CC ECO:0000269|PubMed:9265642}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12230471, ECO:0000269|PubMed:14562095}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:12230471,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SOP4 family. {ECO:0000305}.
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DR EMBL; X77688; CAA54768.1; -; Genomic_DNA.
DR EMBL; Z49467; CAA89487.1; -; Genomic_DNA.
DR EMBL; AY693041; AAT93060.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08615.1; -; Genomic_DNA.
DR PIR; S46642; S46642.
DR RefSeq; NP_012343.1; NM_001181625.1.
DR PDB; 6WB9; EM; 3.00 A; 7=1-234.
DR PDB; 7KRA; EM; 3.20 A; G=1-234.
DR PDB; 7KTX; EM; 4.30 A; G=1-234.
DR PDBsum; 6WB9; -.
DR PDBsum; 7KRA; -.
DR PDBsum; 7KTX; -.
DR AlphaFoldDB; P39543; -.
DR SMR; P39543; -.
DR BioGRID; 33571; 87.
DR DIP; DIP-5094N; -.
DR IntAct; P39543; 13.
DR MINT; P39543; -.
DR STRING; 4932.YJL192C; -.
DR MaxQB; P39543; -.
DR PaxDb; P39543; -.
DR PRIDE; P39543; -.
DR EnsemblFungi; YJL192C_mRNA; YJL192C; YJL192C.
DR GeneID; 853247; -.
DR KEGG; sce:YJL192C; -.
DR SGD; S000003728; SOP4.
DR VEuPathDB; FungiDB:YJL192C; -.
DR eggNOG; ENOG502RXGD; Eukaryota.
DR HOGENOM; CLU_102669_0_0_1; -.
DR InParanoid; P39543; -.
DR OMA; PYITVEL; -.
DR BioCyc; YEAST:G3O-31624-MON; -.
DR PRO; PR:P39543; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P39543; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR031395; Sop4.
DR Pfam; PF17081; SOP4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..234
FT /note="Protein SOP4"
FT /id="PRO_0000014332"
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"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:7KRA"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 89..99
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:7KRA"
SQ SEQUENCE 234 AA; 26598 MW; A29CA99FA3741A41 CRC64;
MFSQIVLLLS AFIYVASATA RRGTIKGRLD LAASNITGFV STRTSFKLYQ IGNFSTEYPY
TSTTMFQDDE GNFEFANLPL NDGVNETTYY VMYPASMDFN LKPNRILIEF KNLENGTLQL
NAFKNFFGRE YFPSKDITYP EKLQSMKVHP YITVELLHKA PIRSYLQARN VSIFSTGIVG
NILNSRWKLA GVITLIALVV FPIIVEKLDP ETARAIREEA KRKQREKYAA VASK
