MSO1_YEAST
ID MSO1_YEAST Reviewed; 210 AA.
AC P53604; D6W1M4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein MSO1;
GN Name=MSO1; OrderedLocusNames=YNR049C; ORFNames=N3457;
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 208353 / W303-1A;
RX PubMed=9207091; DOI=10.1073/pnas.94.14.7331;
RA Aalto M.K., Jantti J., Ostling J., Keranen S., Ronne H.;
RT "Mso1p: a yeast protein that functions in secretion and interacts
RT physically and genetically with Sec1p.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7331-7336(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
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 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, ACETYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in secretion. Component of the secretory vesicle
CC docking complex.
CC -!- SUBUNIT: Interacts physically with SEC1.
CC -!- INTERACTION:
CC P53604; P30619: SEC1; NbExp=3; IntAct=EBI-2086543, EBI-16833;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P53604-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53604-2; Sequence=VSP_058125;
CC -!- MISCELLANEOUS: Present with 1380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U56416; AAB01212.1; -; Genomic_DNA.
DR EMBL; Z71664; CAA96330.1; -; Genomic_DNA.
DR EMBL; AY558423; AAS56749.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10590.1; -; Genomic_DNA.
DR PIR; S63380; S63380.
DR RefSeq; NP_014447.3; NM_001183226.3. [P53604-1]
DR AlphaFoldDB; P53604; -.
DR BioGRID; 35874; 139.
DR DIP; DIP-2499N; -.
DR IntAct; P53604; 4.
DR MINT; P53604; -.
DR STRING; 4932.YNR049C; -.
DR iPTMnet; P53604; -.
DR MaxQB; P53604; -.
DR PaxDb; P53604; -.
DR PRIDE; P53604; -.
DR EnsemblFungi; YNR049C_mRNA; YNR049C; YNR049C. [P53604-1]
DR GeneID; 855785; -.
DR KEGG; sce:YNR049C; -.
DR SGD; S000005332; MSO1.
DR VEuPathDB; FungiDB:YNR049C; -.
DR eggNOG; ENOG502S4R3; Eukaryota.
DR HOGENOM; CLU_082503_0_0_1; -.
DR InParanoid; P53604; -.
DR OMA; WNKFTKS; -.
DR BioCyc; YEAST:G3O-33356-MON; -.
DR PRO; PR:P53604; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53604; protein.
DR GO; GO:0033101; C:cellular bud membrane; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0031201; C:SNARE complex; IDA:SGD.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:SGD.
DR GO; GO:0061025; P:membrane fusion; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IDA:SGD.
DR InterPro; IPR028095; Mso1_N_dom.
DR Pfam; PF14475; Mso1_Sec1_bdg; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..210
FT /note="Protein MSO1"
FT /id="PRO_0000096600"
FT REGION 88..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT VAR_SEQ 1
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_058125"
FT INIT_MET P53604-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES P53604-2:2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 210 AA; 23351 MW; C51AC383A149DA46 CRC64;
MMSQVSHSQE GSGRFWNKFK SSTKSLSTSL AHLSIKAEKD GDTVNTTLVH KGLVKFYENQ
HPFQGFPGWL GEKEDLPNER KILDTQVKHD MKKQNSRHFS PSFSNRRKAS SEDPMGTPSS
NGNTPEYTPA SKSFQDIYNN HTSSSSATPR RASSRPTRPS AGQEFRASLG RSKTSNSFNT
SSTPTPPPDA SSGVMAMKDR LKRRNNDYGF
