MST28_YEAST
ID MST28_YEAST Reviewed; 234 AA.
AC P39552; D6VPN3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Multicopy suppressor of SEC21 protein 28;
DE AltName: Full=DUP240 protein MST28;
GN Name=MST28; OrderedLocusNames=YAR033W; ORFNames=FUN59;
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 204511 / S288c / AB972;
RA Bussey H., Keng T., Storms R.K., Vo D., Zhong W., Fortin N., Barton A.B.,
RA Kaback D.B., Clark M.W.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 52
RT Kbp CDC15-FLO1-PHO11-YAR074 region.";
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=12101299; DOI=10.1099/00221287-148-7-2111;
RA Poirey R., Despons L., Leh V., Lafuente M.-J., Potier S., Souciet J.-L.,
RA Jauniaux J.-C.;
RT "Functional analysis of the Saccharomyces cerevisiae DUP240 multigene
RT family reveals membrane-associated proteins that are not essential for cell
RT viability.";
RL Microbiology 148:2111-2123(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MST27.
RX PubMed=12925749; DOI=10.1091/mbc.e02-11-0736;
RA Sandmann T., Herrmann J.M., Dengjel J., Schwarz H., Spang A.;
RT "Suppression of coatomer mutants by a new protein family with COPI and
RT COPII binding motifs in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 14:3097-3113(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Involved in protein trafficking vesicle formation, probably
CC by stabilizing of coatomer at the Golgi membrane and thus allowing the
CC efficient formation of COPI coated vesicles.
CC {ECO:0000269|PubMed:12925749}.
CC -!- SUBUNIT: Interacts with MST27. Binds to coatomer proteins of COPI and
CC SEC23/SEC24 of COPII coated vesicles. {ECO:0000269|PubMed:12925749}.
CC -!- INTERACTION:
CC P39552; P53176: MST27; NbExp=4; IntAct=EBI-20785, EBI-6205;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:12101299, ECO:0000269|PubMed:12925749}. Golgi
CC apparatus {ECO:0000269|PubMed:12925749}. Cytoplasmic vesicle, COPI-
CC coated vesicle membrane {ECO:0000269|PubMed:12925749}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12925749}. Cytoplasmic vesicle,
CC COPII-coated vesicle membrane {ECO:0000269|PubMed:12925749}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12925749}.
CC -!- MISCELLANEOUS: Members of the DUP240 multigene family are specific to
CC S.cerevisiae sensu strictu. Cells lacking all 10 DUP240 proteins show
CC no obvious alterations in mating, sporulation and cell growth.
CC -!- SIMILARITY: Belongs to the DUP/COS family. {ECO:0000305}.
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DR EMBL; L28920; AAC09494.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA07003.1; -; Genomic_DNA.
DR PIR; S53484; S53484.
DR RefSeq; NP_009419.1; NM_001178225.1.
DR AlphaFoldDB; P39552; -.
DR BioGRID; 31810; 58.
DR ComplexPortal; CPX-1303; MST27-MST28 vesicle formation complex.
DR DIP; DIP-1853N; -.
DR IntAct; P39552; 6.
DR MINT; P39552; -.
DR STRING; 4932.YAR033W; -.
DR iPTMnet; P39552; -.
DR MaxQB; P39552; -.
DR PaxDb; P39552; -.
DR PRIDE; P39552; -.
DR EnsemblFungi; YAR033W_mRNA; YAR033W; YAR033W.
DR GeneID; 851284; -.
DR KEGG; sce:YAR033W; -.
DR SGD; S000000079; MST28.
DR VEuPathDB; FungiDB:YAR033W; -.
DR eggNOG; ENOG502SSNW; Eukaryota.
DR GeneTree; ENSGT00940000176285; -.
DR HOGENOM; CLU_081384_0_1_1; -.
DR InParanoid; P39552; -.
DR BioCyc; YEAST:G3O-28882-MON; -.
DR PRO; PR:P39552; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39552; protein.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IDA:ComplexPortal.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016050; P:vesicle organization; IDA:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR001142; DUP/COS.
DR Pfam; PF00674; DUP; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..234
FT /note="Multicopy suppressor of SEC21 protein 28"
FT /id="PRO_0000207526"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..72
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 231..234
FT /note="COPI binding"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 234 AA; 27091 MW; B23AAD4D26831319 CRC64;
MQTPPESTDV KLDTLNEPSA HLIEKNVALP KDIFRSYLSY WIYEIARYTP VMILSLVIGV
LVLLIIFFND NEACVFNSAI FAFTSLVGLL IILSDGNPKL VSRRNFRTEL LVDVITRKPA
VEGKEWRIIT YNMNQYLFNH GQWHTPYYFY SDEDCYRYFL RLVEGVTPKK QTATSIGNSP
VTAKPEDAIE SASPSSRLNY QNFLLKAAEI ERQAQENYWR RRHPNIDALL KKTE
