ID   SYS1_YEAST              Reviewed;         203 AA.
AC   P41544; D6VWH1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2026, entry version 159.
DE   RecName: Full=Protein SYS1;
GN   Name=SYS1; OrderedLocusNames=YJL004C; ORFNames=J1402, YJR83.17;
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].
RX   PubMed=7720878; DOI=10.1016/0014-5793(95)00253-6;
RA   Pathak R., Parker C.S., Imperiali B.;
RT   "The essential yeast NLT1 gene encodes the 64 kDa glycoprotein subunit of
RT   the oligosaccharyl transferase.";
RL   FEBS Lett. 362:229-234(1995).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-203.
RX   PubMed=3327602; DOI=10.1007/bf00418405;
RA   Masson P., Lenzen G., Jacquemin J.M., Danchin A.;
RT   "Yeast adenylate cyclase catalytic domain is carboxy terminal.";
RL   Curr. Genet. 10:343-352(1986).
RN   [6]
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   [7]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-15, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA   Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT   "A subset of membrane-associated proteins is ubiquitinated in response to
RT   mutations in the endoplasmic reticulum degradation machinery.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN   [8]
RP   INTERACTION WITH ARL3.
RX   PubMed=15077113; DOI=10.1038/ncb1120;
RA   Behnia R., Panic B., Whyte J.R.C., Munro S.;
RT   "Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal
RT   acetylation and the membrane protein Sys1p.";
RL   Nat. Cell Biol. 6:405-413(2004).
RN   [9]
RP   INTERACTION WITH ARL3.
RX   PubMed=15077114; DOI=10.1038/ncb1121;
RA   Setty S.R., Strochlic T.I., Tong A.H., Boone C., Burd C.G.;
RT   "Golgi targeting of ARF-like GTPase Arl3p requires its Nalpha-acetylation
RT   and the integral membrane protein Sys1p.";
RL   Nat. Cell Biol. 6:414-419(2004).
RN   [10]
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).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND IDENTIFICATION BY
RP   MASS 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: Necessary for the targeting of ARL3 to the Golgi. Involved in
CC       protein trafficking. May serve as a receptor for acetylated ARL3.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC       protein.
CC   -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SYS1 family. {ECO:0000305}.
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DR   EMBL; U22326; AAA85159.1; -; Genomic_DNA.
DR   EMBL; Z49279; CAA89294.1; -; Genomic_DNA.
DR   EMBL; X87611; CAA60918.1; -; Genomic_DNA.
DR   EMBL; AY558345; AAS56671.1; -; Genomic_DNA.
DR   EMBL; X03449; CAA27176.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08787.1; -; Genomic_DNA.
DR   PIR; S55184; S55184.
DR   RefSeq; NP_012530.1; NM_001181438.1.
DR   AlphaFoldDB; P41544; -.
DR   BioGRID; 33753; 398.
DR   DIP; DIP-2613N; -.
DR   FunCoup; P41544; 279.
DR   IntAct; P41544; 39.
DR   MINT; P41544; -.
DR   STRING; 4932.YJL004C; -.
DR   iPTMnet; P41544; -.
DR   PaxDb; 4932-YJL004C; -.
DR   PeptideAtlas; P41544; -.
DR   DNASU; 853453; -.
DR   EnsemblFungi; YJL004C_mRNA; YJL004C; YJL004C.
DR   GeneID; 853453; -.
DR   KEGG; sce:YJL004C; -.
DR   AGR; SGD:S000003541; -.
DR   SGD; S000003541; SYS1.
DR   VEuPathDB; FungiDB:YJL004C; -.
DR   eggNOG; KOG4697; Eukaryota.
DR   HOGENOM; CLU_081382_1_0_1; -.
DR   InParanoid; P41544; -.
DR   OMA; AACIWYN; -.
DR   OrthoDB; 542931at2759; -.
DR   BioCyc; YEAST:G3O-31483-MONOMER; -.
DR   Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   BioGRID-ORCS; 853453; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P41544; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P41544; protein.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR   GO; GO:0006895; P:Golgi to endosome transport; IGI:SGD.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:SGD.
DR   GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:SGD.
DR   InterPro; IPR019185; Integral_membrane_SYS1-rel.
DR   PANTHER; PTHR12952:SF0; PROTEIN SYS1 HOMOLOG; 1.
DR   PANTHER; PTHR12952; SYS1; 1.
DR   Pfam; PF09801; SYS1; 1.
PE   1: Evidence at protein level;
KW   Golgi apparatus; Isopeptide bond; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport; Ubl conjugation.
FT   CHAIN           1..203
FT                   /note="Protein SYS1"
FT                   /id="PRO_0000213942"
FT   TOPO_DOM        1..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..78
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..105
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..131
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        155..203
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         192
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CROSSLNK        15
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:14557538"
FT   CONFLICT        149..203
FT                   /note="GTWTTRWRELRDTFFEGLVDPNEGEVGLVTPSQQHSNHSELEQSPIQLKDLE
FT                   SQI -> ALT (in Ref. 1; AAA85159)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   203 AA;  23716 MW;  78D398E84713732F CRC64;
     MVSIRRYLRV PNELKPSQIF KQDSLSPSKI GLQIVLLQIF YYTTAIVLFY CWAKLAGYDL
     NIKEWLFSWE NIDFTNAYGL SISLLWLLDS LICVFFLTVI VGRSKLAWDF AITIHAINFI
     VVFLYTRKFP SFSWFFLQIL SSLILIFLGT WTTRWRELRD TFFEGLVDPN EGEVGLVTPS
     QQHSNHSELE QSPIQLKDLE SQI
//