BRO1_CANGA
ID BRO1_CANGA Reviewed; 888 AA.
AC Q6FJG8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Vacuolar protein-sorting protein BRO1;
DE AltName: Full=BRO domain-containing protein 1;
GN Name=BRO1; OrderedLocusNames=CAGL0M06413g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380959; CAG62602.1; -; Genomic_DNA.
DR RefSeq; XP_449626.1; XM_449626.1.
DR AlphaFoldDB; Q6FJG8; -.
DR SMR; Q6FJG8; -.
DR STRING; 5478.XP_449626.1; -.
DR EnsemblFungi; CAG62602; CAG62602; CAGL0M06413g.
DR GeneID; 2891674; -.
DR KEGG; cgr:CAGL0M06413g; -.
DR CGD; CAL0137439; CAGL0M06413g.
DR VEuPathDB; FungiDB:CAGL0M06413g; -.
DR eggNOG; KOG2220; Eukaryota.
DR HOGENOM; CLU_321635_0_0_1; -.
DR InParanoid; Q6FJG8; -.
DR OMA; ANHKQSA; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0010008; C:endosome membrane; IEA:GOC.
DR GO; GO:0035800; F:deubiquitinase activator activity; IEA:EnsemblFungi.
DR GO; GO:1904669; P:ATP export; IEA:EnsemblFungi.
DR GO; GO:0070676; P:intralumenal vesicle formation; IEA:EnsemblFungi.
DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0016579; P:protein deubiquitination; IEA:EnsemblFungi.
DR GO; GO:0036010; P:protein localization to endosome; IEA:EnsemblFungi.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:EnsemblFungi.
DR GO; GO:0007584; P:response to nutrient; IEA:EnsemblFungi.
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 Coiled coil; Cytoplasm; Endosome; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..888
FT /note="Vacuolar protein-sorting protein BRO1"
FT /id="PRO_0000218862"
FT DOMAIN 4..400
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REGION 706..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 543..578
FT /evidence="ECO:0000255"
FT COMPBIAS 706..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 101130 MW; 606D93E4A5DF3D98 CRC64;
MKPSVIGLKC KDTDKVDWKR GLSSYLKRIY GSRQWKEFYD EQLCVEMDHV RNNANGELGA
VTLVEQNYKY YAYLEQLYLR LGNNIGQFKL EFTWYDAEYG LVSSPTKHTQ KTLVFEKSCT
LYNLGVALTE VANEKINEDF KTAMVHMAKA MECFRYLSEN FFNSPSADLQ TENTKFLSDL
SHAEAQEMFL INAINNGTSE KQASLISKLA YSGSNLYENC WEFLRTEEGG LTPYGEARWN
SIVSGKHHFF RSLAAYYNAL ALEQNNKYGE AIAFLKLATQ CLSSSLPYKY ALNDNFDFDG
FGETIKDKTK QLIKDNDYIF HDSIPQSVSL SSIKALDAIK APKWEEQLKP FMEAIAHKCE
KLYRGIVPME VFEKESIYSE KKASMLRQCI NDSETADMEY SSFIEFTHLP NLLSDLKRRY
KSQNFSGTTD PQGDMMRDQI QSWIKSISQS KYKDPDEQLK LISSKKQEIL TLLAGLPSEQ
KENVVKLKMA LVEAAASDEK LFSLVQPYAA QLRLLKQPDE LWKIFNMFSI DESNKQSLLD
IDDSKNQEIL AKISDIEQMA EDLRLLKEER GRTLKELKSQ TNDDDITNTL LVNSKAESEE
LEVIFKKELD KFKPLTTRIE ATIFKQESVV NEVKNELDNV FSLSGLENKT SEEEEKQKKR
KEFFMQIEEA ATKFLIFNND LPKGLEFYDS LLKMSKDLAV SVKVQNNASG SDNNSNNGYV
SGNVIPPSLP PQPRNVGSSI DSQFQSMNLG SVPTPQRFPQ PPAPNSRPIV SMENYTSQFS
VPPAHGDLPP AYNQVPLVPT RNYDQPHGSG NYPGNVSSQH PVSSSPIPGA YDQVPMVPPK
QPPAEGRSQI SRQEQMEREE RELQRDPTAF YKKSSVFDES LYSRYSGK