PSG1_YEAST
ID PSG1_YEAST Reviewed; 392 AA.
AC P36081; D6VXL0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=PMA1 stabilization in the Golgi protein 1 {ECO:0000303|PubMed:28727280};
DE Contains:
DE RecName: Full=PSG1-N' {ECO:0000303|PubMed:28727280};
DE Contains:
DE RecName: Full=PSG1-C' {ECO:0000303|PubMed:28727280};
DE Flags: Precursor;
GN Name=PSG1 {ECO:0000303|PubMed:28727280}; OrderedLocusNames=YKL077W;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 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).
RN [4]
RP CLEAVAGE BY KEX2.
RX PubMed=17210951; DOI=10.1083/jcb.200609182;
RA Heiman M.G., Engel A., Walter P.;
RT "The Golgi-resident protease Kex2 acts in conjunction with Prm1 to
RT facilitate cell fusion during yeast mating.";
RL J. Cell Biol. 176:209-222(2007).
RN [5]
RP GLYCOSYLATION AT THR-34; THR-35; SER-36; THR-45; SER-49; THR-55; THR-57;
RP THR-63; SER-65; THR-71; SER-80; THR-89; THR-99; SER-107; THR-108; THR-112;
RP SER-114; SER-115; THR-117; SER-119; SER-148; THR-156; SER-171; THR-176;
RP SER-181; THR-188; THR-192; THR-195; THR-199; SER-203 AND SER-215.
RX PubMed=26764011; DOI=10.1074/mcp.m115.057505;
RA Neubert P., Halim A., Zauser M., Essig A., Joshi H.J., Zatorska E.,
RA Larsen I.S., Loibl M., Castells-Ballester J., Aebi M., Clausen H.,
RA Strahl S.;
RT "Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae.";
RL Mol. Cell. Proteomics 15:1323-1337(2016).
RN [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH PSG1; EPS1; CDC48; UBX2; SSM4; TLG1;
RP TLG2 AND VTI1, DISRUPTION PHENOTYPE, TOPOLOGY, CLEAVAGE BY KEX2, AND
RP GLYCOSYLATION.
RX PubMed=28727280; DOI=10.1111/tra.12503;
RA Geva Y., Crissman J., Arakel E.C., Gomez-Navarro N., Chuartzman S.G.,
RA Stahmer K.R., Schwappach B., Miller E.A., Schuldiner M.;
RT "Two novel effectors of trafficking and maturation of the yeast plasma
RT membrane H+ -ATPase.";
RL Traffic 18:672-682(2017).
CC -!- FUNCTION: With EXP1, the specific cargo receptor protein for the plasma
CC membrane ATPase PMA1, is involved in the transport and/or maturation of
CC PMA1 (PubMed:28727280). EXP1 and PSG1 probably act sequentially to
CC promote PMA1 sorting between the ER and the Golgi, with EXP1 promoting
CC PMA1 export from the ER to the Golgi while PSG1 has a role in PMA1
CC maturation or quality control in the Golgi (PubMed:28727280). PSG1
CC might also couple PMA1 sorting and maturation in the early secretory
CC pathway with the glycosylation machinery (Probable).
CC {ECO:0000269|PubMed:28727280, ECO:0000305|PubMed:28727280}.
CC -!- FUNCTION: PSG1 is cleaved by KEX2 in two stable peptides, PSG1-N' and
CC PSG1-C', the former supporting a role in maturation quality control,
CC the latter having a role in modulating vesicular trafficking.
CC {ECO:0000269|PubMed:28727280}.
CC -!- SUBUNIT: Interacts with EXP1 (PubMed:28727280). PSG1-N' interacts with
CC ERAD-related proteins involved in PMA1 quality control including EPS1,
CC CDC48, UBX2 and SSM4 (PubMed:28727280). PSG1-C' interacts with the
CC TLG1/2 SNARE complex proteins TLG1, TLG2 and VTI1 (PubMed:28727280).
CC {ECO:0000269|PubMed:28727280}.
CC -!- SUBCELLULAR LOCATION: [PSG1-N']: Golgi apparatus lumen
CC {ECO:0000269|PubMed:28727280}.
CC -!- SUBCELLULAR LOCATION: [PSG1-C']: Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000269|PubMed:28727280}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- PTM: The precursor protein is cleaved into two polypeptide chains,
CC PSG1-N' and PSG1-C'. The cleavage is performed in the Golgi apparatus
CC by Ca(+)-dependent serine protease KEX2 between Arg-229 and Asp-230.
CC {ECO:0000269|PubMed:17210951, ECO:0000269|PubMed:28727280}.
CC -!- PTM: PSG1-N' is highly O-mannosylated. {ECO:0000269|PubMed:26764011,
CC ECO:0000269|PubMed:28727280}.
CC -!- DISRUPTION PHENOTYPE: Leads to enhanced degradation of PMA1 in the
CC vacuole. {ECO:0000269|PubMed:28727280}.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z28077; CAA81914.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09080.1; -; Genomic_DNA.
DR PIR; S37902; S37902.
DR RefSeq; NP_012846.1; NM_001179643.1.
DR AlphaFoldDB; P36081; -.
DR BioGRID; 34055; 225.
DR DIP; DIP-5003N; -.
DR IntAct; P36081; 1.
DR STRING; 4932.YKL077W; -.
DR iPTMnet; P36081; -.
DR MaxQB; P36081; -.
DR PaxDb; P36081; -.
DR PRIDE; P36081; -.
DR TopDownProteomics; P36081; -.
DR EnsemblFungi; YKL077W_mRNA; YKL077W; YKL077W.
DR GeneID; 853785; -.
DR KEGG; sce:YKL077W; -.
DR SGD; S000001560; YKL077W.
DR VEuPathDB; FungiDB:YKL077W; -.
DR eggNOG; ENOG502QVDR; Eukaryota.
DR HOGENOM; CLU_041040_0_0_1; -.
DR InParanoid; P36081; -.
DR OMA; RCTPDRY; -.
DR BioCyc; YEAST:G3O-31872-MON; -.
DR PRO; PR:P36081; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36081; protein.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0005796; C:Golgi lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051604; P:protein maturation; IMP:SGD.
DR GO; GO:0006605; P:protein targeting; IMP:SGD.
DR InterPro; IPR028000; Pma1.
DR Pfam; PF14610; Psg1; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..392
FT /note="PMA1 stabilization in the Golgi protein 1"
FT /id="PRO_0000203168"
FT CHAIN 23..229
FT /note="PSG1-N'"
FT /evidence="ECO:0000269|PubMed:28727280"
FT /id="PRO_0000448535"
FT CHAIN 230..392
FT /note="PSG1-C'"
FT /evidence="ECO:0000269|PubMed:28727280"
FT /id="PRO_0000448536"
FT TOPO_DOM 230..317
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:28727280"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28727280"
FT SITE 229..230
FT /note="Cleavage; by KEX2"
FT /evidence="ECO:0000269|PubMed:17210951,
FT ECO:0000269|PubMed:28727280"
FT CARBOHYD 34
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 35
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 36
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 45
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 49
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 55
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 57
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 63
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 65
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 71
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 80
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 89
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 99
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 107
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 108
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 112
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 114
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 115
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 117
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 119
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 148
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 156
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 171
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 176
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 181
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 188
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 192
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 195
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 199
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 203
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
FT CARBOHYD 215
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:26764011"
SQ SEQUENCE 392 AA; 46036 MW; 8EEC795903D5D540 CRC64;
MRFHDSILIF FSLASLYQHV HGARQVVRPK EKMTTSEEVK PWLRTVYGSQ KELVTPTVIA
GVTFSEKPEE TPNPLKPWVS LEHDGRPKTI KPEINKGRTK KGRPDYSTYF KTVSSHTYSY
EELKAHNMGP NEVFVEEEYI DEDDTYVSLN PIVRCTPNLY FNKGLAKDIR SEPFCTPYEN
SRWKVDKTYF VTWYTRFFTD ENSGKVADKV RVHLSYVKEN PVEKGNYKRD IPATFFSSEW
IDNDNGLMPV EVRDEWLQDQ FDRRIVVSVQ PIYISDEDFD PLQYGILLYI TKGSKVFKPT
KEQLALDDAG ITNDQWYYVA LSIPTVVVVF FVFMYFFLYV NGKNRDFTDV TRKALNKKRR
VLGKFSEMKK FKNMKNHKYT ELPSYKKTSK QN
