VID27_YEAST
ID VID27_YEAST Reviewed; 782 AA.
AC P40157; D6W0X8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Vacuolar import and degradation protein 27;
GN Name=VID27; OrderedLocusNames=YNL212W; ORFNames=N1327;
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 96604 / S288c / FY1679;
RX PubMed=7762305; DOI=10.1002/yea.320110111;
RA Coster F., van Dyck L., Jonniaux J.-L., Purnelle B., Goffeau A.;
RT "The sequence of a 13.5 kb DNA segment from the left arm of yeast
RT chromosome XIV reveals MER1; RAP1; a new putative member of the DNA
RT replication complex and a new putative serine/threonine phosphatase gene.";
RL Yeast 11:85-91(1995).
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 FUNCTION.
RX PubMed=12686616; DOI=10.1091/mbc.e02-08-0456;
RA Regelmann J., Schuele T., Josupeit F.S., Horak J., Rose M., Entian K.-D.,
RA Thumm M., Wolf D.H.;
RT "Catabolite degradation of fructose-1,6-bisphosphatase in the yeast
RT Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID
RT genes and indicates the existence of two degradation pathways.";
RL Mol. Biol. Cell 14:1652-1663(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND THR-486, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-195 AND SER-196, AND
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).
CC -!- FUNCTION: Has a role in the negative regulation of gluconeogenesis.
CC Required for vacuolar catabolite degradation of fructose-1,6-
CC bisphosphatase (FBPase). {ECO:0000269|PubMed:12686616}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VID27 family. {ECO:0000305}.
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DR EMBL; X78898; CAA55496.1; -; Genomic_DNA.
DR EMBL; Z71488; CAA96114.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10344.1; -; Genomic_DNA.
DR PIR; S50719; S50719.
DR RefSeq; NP_014187.1; NM_001183050.1.
DR AlphaFoldDB; P40157; -.
DR BioGRID; 35624; 49.
DR DIP; DIP-4291N; -.
DR IntAct; P40157; 20.
DR STRING; 4932.YNL212W; -.
DR iPTMnet; P40157; -.
DR MaxQB; P40157; -.
DR PaxDb; P40157; -.
DR PRIDE; P40157; -.
DR EnsemblFungi; YNL212W_mRNA; YNL212W; YNL212W.
DR GeneID; 855509; -.
DR KEGG; sce:YNL212W; -.
DR SGD; S000005156; VID27.
DR VEuPathDB; FungiDB:YNL212W; -.
DR eggNOG; KOG2395; Eukaryota.
DR HOGENOM; CLU_007002_0_0_1; -.
DR InParanoid; P40157; -.
DR OMA; PFIITWS; -.
DR BioCyc; YEAST:G3O-33218-MON; -.
DR PRO; PR:P40157; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40157; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR040458; Vid27.
DR InterPro; IPR013863; VID27_C.
DR InterPro; IPR040979; Vid27_N.
DR InterPro; IPR040768; Vid27_PH.
DR PANTHER; PTHR31913; PTHR31913; 1.
DR Pfam; PF08553; VID27; 1.
DR Pfam; PF17748; VID27_N; 1.
DR Pfam; PF17747; VID27_PH; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..782
FT /note="Vacuolar import and degradation protein 27"
FT /id="PRO_0000065827"
FT REGION 188..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 486
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 782 AA; 88846 MW; CCBB1F4CE32BF97C CRC64;
MNILKKFMES GNKPELITIP SGQFNLLRSK NSPKAALECI YNNATLSVRK IGKFDYELAV
YRVEDDSEGG TGDEAENFED DTISVLSTQS KKKEEEWSVE ISDKIMFHKT WDKQGNVALV
WENLRGDEQD EKVQFVVAAD VSFSDVEQFI QTVYRCQFEV RNKKSSLTAS ADDLKEIEHR
STRLFVQDDD DELDSSSDDF QDAKDTSFEH EKESEILERT PSPLKKVPEG EYCCLVMSSL
YMYDPIQEKF ILQEPVVKVA IIDTGKYEFW LAIEGKDNRL GTQVAPNINP TFELATDAFL
FNYTLQNITL SYMLKFKDLD KCIQFRFAWV KCLWMTLNKE TWTDVPEKEK DYILDSSSVP
LEKQFDDILH IDDRSNEERD KESSESENDS EDEDDENDHS KRIISSEAFE EPRRATSKGN
SSLTVAFRNN RSYVTRDNRI GVFKTDDEDD SLEFVAAIKN ISNLGGKSID PHKPMLYMED
RNLILTDGEN ENKLYKMDIE RGKVIEEWST GDKNVVQYGP TKKFDQMTPE QTIVGVSQKG
VFKIDPRING KNKIAVDESK DYVGKYNFSS IGTTESGYIA IGSEKGDIKL YDRLGIRAKT
AIPSLGQAIK FITTSADGKW LLATCESTLL LMDLKIKDGK NAGNIGFLKS FPASENVKTY
VLKIRPEHSA SILTYTKKPI RFTKAYFNTG IGQQEQTIVT STGPYAISWS LKGILNQDGS
NNYPYRIRRY NADVVADNFE FGSDKKVIVA LKDDVSLSKV KSFKQPSKGV LMPSASLQDF
YG
