MVB12_YEAST
ID MVB12_YEAST Reviewed; 101 AA.
AC P42939; D6VUY9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Multivesicular body sorting factor 12;
DE AltName: Full=12 kDa multivesicular body sorting factor;
DE AltName: Full=ESCRT-I complex subunit MVB12;
GN Name=MVB12; OrderedLocusNames=YGR206W; ORFNames=G7740;
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 204508 / S288c;
RX PubMed=8904340;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<273::aid-yea898>3.0.co;2-1;
RA Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A.,
RA Rodrigues-Pousada C.;
RT "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII
RT reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the
RT yeast PMT and EF1G genes, of the human and bacterial electron-transferring
RT flavoproteins (beta-chain) and of the Escherichia coli phosphoserine
RT phosphohydrolase, and five new ORFs.";
RL Yeast 12:273-280(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 IDENTIFICATION IN THE ESCRT-I COMPLEX, AND COMPOSITION OF THE ESCRT-I
RP COMPLEX.
RX PubMed=17215868; DOI=10.1038/sj.emboj.7601501;
RA Gill D.J., Teo H., Sun J., Perisic O., Veprintsev D.B., Emr S.D.,
RA Williams R.L.;
RT "Structural insight into the ESCRT-I/-II link and its role in MVB
RT trafficking.";
RL EMBO J. 26:600-612(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE ESCRT-I COMPLEX.
RX PubMed=17135292; DOI=10.1091/mbc.e06-07-0588;
RA Curtiss M., Jones C., Babst M.;
RT "Efficient cargo sorting by ESCRT-I and the subsequent release of ESCRT-I
RT from multivesicular bodies requires the subunit Mvb12.";
RL Mol. Biol. Cell 18:636-645(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE 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).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 4-81, COMPOSITION OF THE ESCRT-I
RP COMPLEX, INTERACTION WITH STP22 AND SRN2, AND MUTAGENESIS OF CYS-54; ILE-57
RP AND HIS-64.
RX PubMed=17442384; DOI=10.1016/j.cell.2007.03.016;
RA Kostelansky M.S., Schluter C., Tam Y.Y., Lee S., Ghirlando R., Beach B.,
RA Conibear E., Hurley J.H.;
RT "Molecular architecture and functional model of the complete yeast ESCRT-I
RT heterotetramer.";
RL Cell 129:485-498(2007).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular
CC trafficking process. Binds to ubiquitinated cargo proteins and is
CC required for the sorting of endocytic ubiquitinated cargos into
CC multivesicular bodies (MVBs). Appears to be involved in cargo sorting
CC and release of the ESCRT-I complex from the MVBs.
CC {ECO:0000269|PubMed:17135292}.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of STP22, VPS28, SRN2 and
CC MVB12 in a 1:1:1:1 stoichiometry. Interacts with STP22 and SRN2.
CC {ECO:0000269|PubMed:17135292, ECO:0000269|PubMed:17215868,
CC ECO:0000269|PubMed:17442384}.
CC -!- INTERACTION:
CC P42939; Q99176: SRN2; NbExp=10; IntAct=EBI-23478, EBI-18076;
CC P42939; P25604: STP22; NbExp=12; IntAct=EBI-23478, EBI-411625;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17135292}. Endosome
CC {ECO:0000269|PubMed:17135292}. Late endosome membrane
CC {ECO:0000305|PubMed:17135292}; Peripheral membrane protein
CC {ECO:0000305|PubMed:17135292}.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49133; CAA88999.1; -; Genomic_DNA.
DR EMBL; Z72991; CAA97233.1; -; Genomic_DNA.
DR EMBL; AY692570; AAT92589.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08300.1; -; Genomic_DNA.
DR PIR; S53929; S53929.
DR RefSeq; NP_011722.3; NM_001181335.3.
DR PDB; 2P22; X-ray; 2.70 A; D=4-81.
DR PDBsum; 2P22; -.
DR AlphaFoldDB; P42939; -.
DR SMR; P42939; -.
DR BioGRID; 33459; 160.
DR ComplexPortal; CPX-940; ESCRT-I complex.
DR DIP; DIP-5332N; -.
DR IntAct; P42939; 6.
DR MINT; P42939; -.
DR STRING; 4932.YGR206W; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; P42939; -.
DR MaxQB; P42939; -.
DR PaxDb; P42939; -.
DR PRIDE; P42939; -.
DR EnsemblFungi; YGR206W_mRNA; YGR206W; YGR206W.
DR GeneID; 853120; -.
DR KEGG; sce:YGR206W; -.
DR SGD; S000003438; MVB12.
DR VEuPathDB; FungiDB:YGR206W; -.
DR eggNOG; ENOG502S5VY; Eukaryota.
DR HOGENOM; CLU_154027_0_0_1; -.
DR InParanoid; P42939; -.
DR OMA; PWYEECD; -.
DR BioCyc; YEAST:G3O-30889-MON; -.
DR EvolutionaryTrace; P42939; -.
DR PRO; PR:P42939; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P42939; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0000813; C:ESCRT I complex; IDA:SGD.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:1904669; P:ATP export; IMP:SGD.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IC:SGD.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR InterPro; IPR019014; Mvb12.
DR Pfam; PF09452; Mvb12; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..101
FT /note="Multivesicular body sorting factor 12"
FT /id="PRO_0000202845"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MUTAGEN 47
FT /note="L->D: Defective in MVB12 incorporation in ESCRT-I
FT complex; reduces localization to MVBs; abolishes
FT interaction with STP22 and SRN2; when associated with D-
FT 57."
FT MUTAGEN 54
FT /note="C->D: Defective in MVB12 incorporation in ESCRT-I
FT complex; when associated with D-57."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 57
FT /note="I->D: Defective in MVB12 incorporation in ESCRT-I
FT complex; reduces localization to MVBs; abolishes
FT interaction with STP22 and SRN2; when associated with D-
FT 47."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 64
FT /note="H->D: Defective in MVB12 incorporation in ESCRT-I
FT complex; when associated with D-47."
FT /evidence="ECO:0000269|PubMed:17442384"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:2P22"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 41..65
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:2P22"
SQ SEQUENCE 101 AA; 11968 MW; E48B085E0FACBAC8 CRC64;
MNNNVEELLR RIPLYNKYGK DFPQETVTRF QMPEFKLPAL QPTRDLLCPW YEECDNITKV
CQLHDSSNKK FDQWYKEQYL SKKPPGIVGN TLLSPSRKDN S
