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   27-MAR-2024, entry version 185.
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;
GN   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; 319.
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   GlyGen; P48582; 7 sites, 1 O-linked glycan (7 sites).
DR   iPTMnet; P48582; -.
DR   MaxQB; P48582; -.
DR   PaxDb; 4932-YPL084W; -.
DR   PeptideAtlas; P48582; -.
DR   EnsemblFungi; YPL084W_mRNA; YPL084W; YPL084W.
DR   GeneID; 856021; -.
DR   KEGG; sce:YPL084W; -.
DR   AGR; SGD:S000006005; -.
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; YLKRSYG; -.
DR   OrthoDB; 24567at2759; -.
DR   BioCyc; YEAST:G3O-33990-MONOMER; -.
DR   BioGRID-ORCS; 856021; 2 hits in 10 CRISPR screens.
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:1903003; P:positive regulation of protein deubiquitination; 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:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   GO; GO:0007034; P:vacuolar transport; IMP:SGD.
DR   CDD; cd09242; BRO1_ScBro1_like; 1.
DR   CDD; cd09237; V_ScBro1_like; 1.
DR   Gene3D; 1.20.120.560; alix/aip1 in complex with the ypdl late domain; 1.
DR   Gene3D; 1.20.140.50; alix/aip1 like domains; 1.
DR   Gene3D; 1.25.40.280; alix/aip1 like domains; 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; PCD6 INTERACTING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR23030:SF45; VACUOLAR-SORTING PROTEIN BRO1; 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
//