BRO1_USTMA
ID BRO1_USTMA Reviewed; 1076 AA.
AC Q4PHA8; A0A0D1D137;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
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; ORFNames=UMAG_00505;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003140; KIS72083.1; -; Genomic_DNA.
DR RefSeq; XP_011386352.1; XM_011388050.1.
DR AlphaFoldDB; Q4PHA8; -.
DR SMR; Q4PHA8; -.
DR STRING; 5270.UM00505P0; -.
DR EnsemblFungi; KIS72083; KIS72083; UMAG_00505.
DR GeneID; 23561785; -.
DR KEGG; uma:UMAG_00505; -.
DR VEuPathDB; FungiDB:UMAG_00505; -.
DR eggNOG; KOG2220; Eukaryota.
DR HOGENOM; CLU_003661_0_0_1; -.
DR InParanoid; Q4PHA8; -.
DR OMA; ANHKQSA; -.
DR OrthoDB; 550620at2759; -.
DR Proteomes; UP000000561; Chromosome 1.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
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..1076
FT /note="Vacuolar protein-sorting protein BRO1"
FT /id="PRO_0000218870"
FT DOMAIN 8..413
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REGION 775..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 489..550
FT /evidence="ECO:0000255"
FT COMPBIAS 775..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..870
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 115259 MW; 6AB425B1A4B4E1CA CRC64;
MADAHQSPLL LLPLKTTEEV DLGSAVKSLI TNSYGEDSKK YSEQTSQLNR ARQDAVKGAA
SDATGRDLLF KWFHMLEMLE LRFPELRVPF PWKDAFTQKT ISQSSLAYEK ASIIFNIAAT
LSSLASSQPR MPGNADGLKR AYAALRQAAG MLSYINENFL HAPSTDMSKD VVKCLVGITL
AQASEVFLEK TIEEKKGAGL ISKLASQTAA AYTGLVDDSR ENVTKGIFER SWAYLIQVKA
RHFTSVMQYY KALADDAAGS HGACLVRLTV AETAAKEARN LLTTFSASAT ASVTADRPSL
PSDAASALVA IVNAQVARCT ERKESAVKDN DLIYHDILPS ESSLPAVDKL VAANPIPIQE
IFAAPEVQRV IGPDLFQNLV PLGVHEKASL YSEEKAKIAR AESERHDLAT GEMQASLDYL
GLPSSLQKYR ALAQGSGSNA MLDSLADPGP EVMRWSTEEA EGGGGRGADG LGVGATGVDS
ALQRIESIKS QAANDIDAAL AALDDENREC EKQRVRFGHK WSQDPAGLHT KDMRVNLKEN
KEAMQQASQN DAQIGGLWKS IRQDVQLLVS GREALEAAFA AALTGQTGLY GEGSAPTSLI
DTSAEEESAS EGEIASVRAK LAQIDEALIK LNKIKKERGE VLADLKEKIQ TDDISQVLVL
NRRAQNVDSS IFAAELEKFK PHQNRIAVSL HHQQALLAEV ETAFKELIEL PASKAAGAKW
DEKEQARNKL VARLKRARDS NAQVRAGVAK GLQFYADLQE IVKATRQNVN RYVGERKSER
SKLVSELEWE EKGSDGLSSS MAGLSGLGGA GGHPAPPTPH RHTSYASAYG GAGAPGPLSP
GPPPAALPGV RQTSNSGPPP PPPLPHQQAS YQQQPPPAAA APAHDPYSSM FSSGPFSAAL
QQPASPQHQR PPTHYGSQLG YACDAPQRAP ALPPPPQQFQ PSFAPSVASP TQSRYTSPPP
VPQGQQTFSG SSGYGMPPAP LQHGGGYGGS QPYAAHDYSS PPPQSPYGVP IGQQQYGGGH
AQNQPQYQAY GAPPQQHASQ QVYGSRAQPP PPQQQQYQQP SYAQHGGYQG GYQPPY