ID   BRO1_DEBHA              Reviewed;         970 AA.
AC   Q6BRL3;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Vacuolar protein-sorting protein BRO1;
DE   AltName: Full=BRO domain-containing protein 1;
GN   Name=BRO1; OrderedLocusNames=DEHA2D15510g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Involved in concentration and sorting of cargo proteins of
CC       the multivesicular body (MVB) for incorporation into intralumenal
CC       vesicles. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BRO1 family. {ECO:0000305}.
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DR   EMBL; CR382136; CAG87328.2; -; Genomic_DNA.
DR   RefSeq; XP_459157.2; XM_459157.1.
DR   AlphaFoldDB; Q6BRL3; -.
DR   SMR; Q6BRL3; -.
DR   STRING; 4959.XP_459157.2; -.
DR   EnsemblFungi; CAG87328; CAG87328; DEHA2D15510g.
DR   GeneID; 2901037; -.
DR   KEGG; dha:DEHA2D15510g; -.
DR   VEuPathDB; FungiDB:DEHA2D15510g; -.
DR   eggNOG; KOG2220; Eukaryota.
DR   HOGENOM; CLU_003661_0_0_1; -.
DR   InParanoid; Q6BRL3; -.
DR   OMA; ANHKQSA; -.
DR   OrthoDB; 550620at2759; -.
DR   Proteomes; UP000000599; Chromosome D.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0071985; P:multivesicular body sorting pathway; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cytoplasm; Endosome; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..970
FT                   /note="Vacuolar protein-sorting protein BRO1"
FT                   /id="PRO_0000218864"
FT   DOMAIN          4..458
FT                   /note="BRO1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT   REGION          254..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..270
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        830..889
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..916
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..957
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   970 AA;  109265 MW;  9012F42A1D3AEE35 CRC64;
     MKTYLFSIPT KKTDETSWVK PLNNYLLSIY GNTTEYQSDL EKFDKLRQDI RGVNPDNTGI
     KLYYNYYSQL ELLDLRFPFS TVNRHKKVNF SWYDAFQPSV VHKQTALAFE KACVLFNLGA
     LLSTYAGAKY EEAQRNSSIA AADETIKESL QIFQQTAGIY QFLNENFLHA PSNDLHQASV
     KFLVKLMLAQ AQEVFVLKVI SGDLEQNKNS LIAKLCQGTT NHYTECFNMV CNINKSGGGS
     SHDDFAVTDT NESVDDILGD DDDDDDLGDY NPEKSGEPQV TASIDSAWVA TIHFKVQFYE
     SLSHYFHGLQ LEKNNKYGDS IAYLTKSQNI LNEISSATLK AISKSGSNDS YELLDNYKYQ
     KDAVGIKLTE MNKDNDFIYH DIIPSLITLP EIKPMDGVKT IPINNSKLFN DLNEYNYSNF
     FNNVVPINIH ELLSFYSEEK SQFLRNELDL VDVSNEESAS ILEYLKMPKS LVNLKEIMNS
     SKHVDTMSTS SETNIDPGVR SIVNEVSSKY QTDMSNKDHI STIRKEIYNT ITESESNLSG
     KFSESLIKYK DDLVRLKKSL IDASNSDNNL FGLINNDNSH LYAILGKGAD SPEFKMLFNV
     DSQTSKKQSN NVENEISLLD IDDSQLSSSV NATDSIDSKI KSIEDILHDL NSIKNNKAKL
     VDTLKKEIHN DDISDILILN SKIKSTNEIK TVIFPEELKK FDPYGKELDN LIEQEKTFIN
     ELKNQWANLS DDPKVKEIQS SKQFQSNLIK HQTDKIIKFY NQNWKKYSLG LSAGVDFYNK
     LLAYARSLKQ NIATAVNAPP QSSFNENFSN LNLGPQHSGP RAPPRPNQSY RPSYGDQSGT
     PQYNASHFSS NSPSLNHNLP PQYSQSSLHR SSTGGSFASH HSNESPGSYS RPPPALPPKR
     PSYSAQPTPH APPQAPYTQF QPQASNYTDN SSSSANPTNL PQHPDSGTND LIYNQPSTYQ
     PNMYNFFSSN