BRO1_YEAST
ID BRO1_YEAST Reviewed; 844 AA.
AC P48582; D6W3T3; Q02823;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Vacuolar-sorting protein BRO1;
DE AltName: Full=Amino acid sensor-independent protein 6;
DE AltName: Full=BCK1-like resistance to osmotic shock protein 1;
DE AltName: Full=BRO domain-containing protein 1;
DE AltName: Full=Nitrogen permease inactivating protein 3;
DE AltName: Full=Vacuolar protein-sorting-associated protein 31;
GN Name=BRO1; Synonyms=ASI6, LPF2, NPI3, VPS31; OrderedLocusNames=YPL084W;
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], AND FUNCTION.
RX PubMed=8649366; DOI=10.1128/mcb.16.6.2585;
RA Nickas M.E., Yaffe M.P.;
RT "BRO1, a novel gene that interacts with components of the Pkc1p-mitogen-
RT activated protein kinase pathway in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:2585-2593(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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=11454748; DOI=10.1093/genetics/158.3.973;
RA Forsberg H., Hammar M., Andreasson C., Moliner A., Ljungdahl P.O.;
RT "Suppressors of ssy1 and ptr3 null mutations define novel amino acid
RT sensor-independent genes in Saccharomyces cerevisiae.";
RL Genetics 158:973-988(2001).
RN [5]
RP FUNCTION.
RX PubMed=12062418; DOI=10.1016/s0014-5793(02)02586-3;
RA Springael J.-Y., Nikko E., Andre B., Marini A.-M.;
RT "Yeast Npi3/Bro1 is involved in ubiquitin-dependent control of permease
RT trafficking.";
RL FEBS Lett. 517:103-109(2002).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12668726; DOI=10.1242/jcs.00395;
RA Odorizzi G., Katzmann D.J., Babst M., Audhya A., Emr S.D.;
RT "Bro1 is an endosome-associated protein that functions in the MVB pathway
RT in Saccharomyces cerevisiae.";
RL J. Cell Sci. 116:1893-1903(2003).
RN [7]
RP FUNCTION.
RX PubMed=14523026; DOI=10.1074/jbc.m306953200;
RA Nikko E., Marini A.-M., Andre B.;
RT "Permease recycling and ubiquitination status reveal a particular role for
RT Bro1 in the multivesicular body pathway.";
RL J. Biol. Chem. 278:50732-50743(2003).
RN [8]
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 [9]
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DOA4.
RX PubMed=15326198; DOI=10.1083/jcb.200403139;
RA Luhtala N., Odorizzi G.;
RT "Bro1 coordinates deubiquitination in the multivesicular body pathway by
RT recruiting Doa4 to endosomes.";
RL J. Cell Biol. 166:717-729(2004).
RN [11]
RP INTERACTION WITH DOA4 AND SNF7.
RX PubMed=15086794; DOI=10.1111/j.1600-0854.2004.00169.x;
RA Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P.,
RA Stevens T.H.;
RT "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces
RT cerevisiae.";
RL Traffic 5:194-210(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-740, 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: Class E VPS protein involved in concentration and sorting of
CC cargo proteins of the multivesicular body (MVB) for incorporation into
CC intralumenal vesicles. Fusion between endosomes and the vacuole will
CC then target the cargo proteins to the vacuolar lumen. Acts as an
CC adapter that recruits the DOA4 deubiquitinase to the endosomes, leading
CC to deubiquitination of cargo proteins prior to the lumenal
CC sequestration. Its association to the endosomes depends on SNF7 and its
CC dissociation requires VPS4. Interacts functionally with the Pkc1p-
CC mitogen-activated protein kinase pathway. {ECO:0000269|PubMed:11454748,
CC ECO:0000269|PubMed:12062418, ECO:0000269|PubMed:12668726,
CC ECO:0000269|PubMed:14523026, ECO:0000269|PubMed:15326198,
CC ECO:0000269|PubMed:8649366}.
CC -!- SUBUNIT: Interacts with DOA4 and SNF7. {ECO:0000269|PubMed:15086794,
CC ECO:0000269|PubMed:15326198}.
CC -!- INTERACTION:
CC P48582; P32571: DOA4; NbExp=15; IntAct=EBI-3768, EBI-19840;
CC P48582; Q08003: RFU1; NbExp=2; IntAct=EBI-3768, EBI-2353109;
CC P48582; P39929: SNF7; NbExp=3; IntAct=EBI-3768, EBI-17554;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome.
CC -!- DOMAIN: The coiled-coil domain is essential for MVB sorting.
CC -!- DOMAIN: The BRO1 domain may be involved in the binding to SNF7.
CC -!- MISCELLANEOUS: Present with 10200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; U37364; AAB07790.1; -; Genomic_DNA.
DR EMBL; U41849; AAB68255.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11349.1; -; Genomic_DNA.
DR PIR; S61104; S61104.
DR RefSeq; NP_015241.1; NM_001183898.1.
DR PDB; 1ZB1; X-ray; 1.95 A; A/B=1-387.
DR PDBsum; 1ZB1; -.
DR AlphaFoldDB; P48582; -.
DR SMR; P48582; -.
DR BioGRID; 36097; 312.
DR DIP; DIP-2225N; -.
DR IntAct; P48582; 11.
DR MINT; P48582; -.
DR STRING; 4932.YPL084W; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; P48582; -.
DR MaxQB; P48582; -.
DR PaxDb; P48582; -.
DR PRIDE; P48582; -.
DR EnsemblFungi; YPL084W_mRNA; YPL084W; YPL084W.
DR GeneID; 856021; -.
DR KEGG; sce:YPL084W; -.
DR SGD; S000006005; BRO1.
DR VEuPathDB; FungiDB:YPL084W; -.
DR eggNOG; KOG2220; Eukaryota.
DR GeneTree; ENSGT00940000163083; -.
DR HOGENOM; CLU_321635_0_0_1; -.
DR InParanoid; P48582; -.
DR OMA; HLRNNAN; -.
DR BioCyc; YEAST:G3O-33990-MON; -.
DR EvolutionaryTrace; P48582; -.
DR PRO; PR:P48582; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P48582; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:GOC.
DR GO; GO:0035800; F:deubiquitinase activator activity; IDA:SGD.
DR GO; GO:1904669; P:ATP export; IMP:SGD.
DR GO; GO:0070676; P:intralumenal vesicle formation; IMP:SGD.
DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:2000158; P:positive regulation of ubiquitin-specific protease activity; IDA:SGD.
DR GO; GO:0016579; P:protein deubiquitination; IGI:SGD.
DR GO; GO:0036010; P:protein localization to endosome; IMP:SGD.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:SGD.
DR GO; GO:0007584; P:response to nutrient; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0007034; P:vacuolar transport; IMP:SGD.
DR Gene3D; 1.25.40.280; -; 1.
DR InterPro; IPR025304; ALIX_V_dom.
DR InterPro; IPR045251; BRO1-like.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR038499; BRO1_sf.
DR PANTHER; PTHR23030; PTHR23030; 1.
DR Pfam; PF13949; ALIX_LYPXL_bnd; 1.
DR Pfam; PF03097; BRO1; 1.
DR SMART; SM01041; BRO1; 1.
DR PROSITE; PS51180; BRO1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Endosome; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..844
FT /note="Vacuolar-sorting protein BRO1"
FT /id="PRO_0000218872"
FT DOMAIN 4..400
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REGION 703..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 547..583
FT /evidence="ECO:0000255"
FT COMPBIAS 802..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 359
FT /note="C -> Y (in Ref. 1; AAB07790)"
FT /evidence="ECO:0000305"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1ZB1"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 60..81
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:1ZB1"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1ZB1"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1ZB1"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 113..134
FT /evidence="ECO:0007829|PDB:1ZB1"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1ZB1"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 141..160
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 171..193
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 203..225
FT /evidence="ECO:0007829|PDB:1ZB1"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1ZB1"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 239..264
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 270..285
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1ZB1"
FT TURN 290..295
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 298..317
FT /evidence="ECO:0007829|PDB:1ZB1"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1ZB1"
FT HELIX 344..366
FT /evidence="ECO:0007829|PDB:1ZB1"
SQ SEQUENCE 844 AA; 97276 MW; 34DE0CDD2F4AE55E CRC64;
MKPYLFDLKL KDTEKLDWKK GLSSYLKKSY GSSQWRTFYD EKATSELDHL RNNANGELAP
SSLSEQNLKY YSFLEHLYFR LGSKGSRLKM DFTWYDAEYS SAQKGLKYTQ HTLAFEKSCT
LFNIAVIFTQ IARENINEDY KNSIANLTKA FSCFEYLSEN FLNSPSVDLQ SENTRFLANI
CHAEAQELFV LKLLNDQISS KQYTLISKLS RATCNLFQKC HDFMKEIDDD VAIYGEPKWK
TTVTCKLHFY KSLSAYYHGL HLEEENRVGE AIAFLDFSMQ QLISSLPFKT WLVEFIDFDG
FKETLEKKQK ELIKDNDFIY HESVPAVVQV DSIKALDAIK SPTWEKILEP YMQDVANKCD
SLYRGIIPLD VYEKESIYSE EKATLLRKQV EETETANLEY SSFIEFTNLP RLLSDLEKQF
SDGNIFSNTD TQGQLMRDQI QTWCKFIQTN EFRDIEEQMN KIVFKRKQIL EILSALPNDQ
KENVTKLKSS LVAASNSDEK LFACVKPHIV EINLLNDNGK IWKKFDEFNR NTPPQPSLLD
IDDTKNDKIL ELLKQVKGHA EDLRTLKEER SRNLSELRDE INNDDITKLL IINKGKSDVE
LKDLFEVELE KFEPLSTRIE ATIYKQSSMI DDIKAKLDEI FHLSNFKDKS SGEEKFLEDR
KNFFDKLQEA VKSFSIFASD LPKGIEFYDS LFNMSRDLAE RVRVAKQTED STANSPAPPL
PPLDSKASVV GGPPLLPQKS AAFQSLSRQG LNLGDQFQNL KISAGSDLPQ GPGIPPRTYE
ASPYAATPTM AAPPVPPKQS QEDMYDLRRR KAVENEEREL QENPTSFYNR PSVFDENMYS
KYSS
