MGA2_YEAST
ID MGA2_YEAST Reviewed; 1113 AA.
AC P40578; D6VVW4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Protein MGA2;
GN Name=MGA2; OrderedLocusNames=YIR033W;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [5]
RP IDENTIFICATION BY 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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP 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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z38061; CAA86193.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08580.1; -; Genomic_DNA.
DR PIR; S48495; S48495.
DR RefSeq; NP_012299.1; NM_001179555.1.
DR AlphaFoldDB; P40578; -.
DR SMR; P40578; -.
DR BioGRID; 35024; 516.
DR DIP; DIP-6689N; -.
DR IntAct; P40578; 21.
DR MINT; P40578; -.
DR STRING; 4932.YIR033W; -.
DR iPTMnet; P40578; -.
DR MaxQB; P40578; -.
DR PaxDb; P40578; -.
DR PRIDE; P40578; -.
DR EnsemblFungi; YIR033W_mRNA; YIR033W; YIR033W.
DR GeneID; 854851; -.
DR KEGG; sce:YIR033W; -.
DR SGD; S000001472; MGA2.
DR VEuPathDB; FungiDB:YIR033W; -.
DR eggNOG; KOG3836; Eukaryota.
DR HOGENOM; CLU_004311_0_0_1; -.
DR InParanoid; P40578; -.
DR OMA; CIARQKF; -.
DR BioCyc; YEAST:G3O-31448-MON; -.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P40578; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40578; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0048255; P:mRNA stabilization; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061399; P:positive regulation of transcription from RNA polymerase II promoter in response to cobalt ion; IMP:SGD.
DR GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IMP:SGD.
DR GO; GO:0036086; P:positive regulation of transcription from RNA polymerase II promoter in response to iron ion starvation; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IGI:SGD.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01833; TIG; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW ANK repeat; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1113
FT /note="Protein MGA2"
FT /id="PRO_0000067074"
FT TRANSMEM 1037..1054
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 530..610
FT /note="IPT/TIG"
FT REPEAT 719..748
FT /note="ANK 1"
FT REPEAT 752..781
FT /note="ANK 2"
FT REGION 91..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
SQ SEQUENCE 1113 AA; 127055 MW; EC8A6D46C01CF917 CRC64;
MQQNSEFLTE TPGSDPHISQ LHANSVMESQ LLDDFLLNGS PMYQDDSMAH INIDEGANFQ
NFIKTDEGDS PNLLSFEGIG NNTHVNQNVS TPLEEEMESN RALKEEEEDE HENKVFNEKN
IGNPAHDEIV FGRKETIQSV YINPLDYLKV NAAQLPLDVE VSGLPQVSRV ENQLKLKVKI
TSETPLNQSM LYLPSDSISR EKFYLKKNIE DFSEDFKKNL LYINAFVLCA VSNRTTNVCT
KCVKREQRRA ARRKSGIADN LLWCNNINRR LVVFNNKQVF PIMKTFDNVK EFELTTRLVC
YCRHHKANNG FVILFTITDW QNRLLGKFTT TPIMITDRKP ANMDTTKFNN TTTSSRRQLT
EEESTTEYYS TDNNQLSKDE NMPFQYTYQH NPYDNDSQMN NIPLKDKNVP FPYSISQQTD
LLQNNNLSLN LSLPNQHIPS PTSMSEEGSE SFNYHHRDND NPVRTISLTN IEQQSQLNQR
KRARNNLEND IGKPLFKHSF SNSISATNTM NPALHSMQDF SMKNNNNNLP SINRVIPSQG
PINGGIEVTL LGCNFKDGLS VKFGSNLALS TQCWSETTIV TYLPPAAYAG QVFVSITDTN
NENNNDDLPQ EIEINDNKKA IFTYVDDTDR QLIELALQIV GLKMNGKLED ARNIAKRIVG
NDSPDSGTNG NSCSKSTGPS PNQHSMNLNT SVLYSDEVLI QKVIKSLNIN SNISICDSLG
RTLLHLACLK NYSSLVYTLI KKGARVNDID SFGLTPLHFA CISGDPKIIK MLLNCKVNYS
LRSHNGLTAR EVFIANHIHS KEIDKKQDNR DNHKFVHNDT YISEVLSLFE EFQNGTKFTD
SVETDSNYSI SRKYSQSSFN SSLLDNESLN ENLFESQSMI NPTSMEIQHP TLQLFENSSY
SEYDQSDFEE DGDEDLFVTD EVEKPGVACR EEQSELLDIG SSANEPEEDN GSTSLWNRVL
HRINDDLPKY EDLFPLSWGK DDKLKTTNQD SIVEQSASNI ENSENSEEED YEEEEEFLKK
QFNRFFQNKQ NFRNDKMLIF FWIPLTLLLL TWFIMYKFGN QDSSINHISE LISEYLRIAL
AKFLLGNERM KTAFRSKLSN LQTTRMLNDL IVS
