BRO1_ARATH
ID BRO1_ARATH Reviewed; 846 AA.
AC F4HXZ1; Q8H1H8; Q9XI56;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Vacuolar-sorting protein BRO1 {ECO:0000305};
DE AltName: Full=BRO domain-containing protein 1 {ECO:0000305};
DE Short=AtBRO1 {ECO:0000303|PubMed:26902184};
GN Name=BRO1 {ECO:0000303|PubMed:26902184};
GN Synonyms=ALIX {ECO:0000303|PubMed:26324913, ECO:0000303|PubMed:26342016},
GN SPHR1 {ECO:0000303|PubMed:26342016};
GN OrderedLocusNames=At1g15130 {ECO:0000312|Araport:AT1G15130};
GN ORFNames=F9L1.7 {ECO:0000312|EMBL:AAD39642.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [5]
RP NOMENCLATURE, AND INTERACTION WITH VPS32.1 AND VPS32.2.
RX PubMed=22639582; DOI=10.3389/fpls.2011.00020;
RA Richardson L.G., Howard A.S., Khuu N., Gidda S.K., McCartney A.,
RA Morphy B.J., Mullen R.T.;
RT "Protein-protein interaction network and subcellular localization of the
RT Arabidopsis thaliana ESCRT machinery.";
RL Front. Plant Sci. 2:20-20(2011).
RN [6]
RP SUBUNIT, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP VPS32.1 AND VPS32.2, AND FUNCTION.
RX PubMed=26342016; DOI=10.1105/tpc.15.00393;
RA Cardona-Lopez X., Cuyas L., Marin E., Rajulu C., Irigoyen M.L., Gil E.,
RA Puga M.I., Bligny R., Nussaume L., Geldner N., Paz-Ares J., Rubio V.;
RT "ESCRT-III-associated protein ALIX mediates high-affinity phosphate
RT transporter trafficking to maintain phosphate homeostasis in Arabidopsis.";
RL Plant Cell 27:2560-2581(2015).
RN [7]
RP INTERACTION WITH AMSH3, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP FUNCTION, AND MUTAGENESIS OF GLY-260.
RX PubMed=26324913; DOI=10.1073/pnas.1510516112;
RA Kalinowska K., Nagel M.K., Goodman K., Cuyas L., Anzenberger F.,
RA Alkofer A., Paz-Ares J., Braun P., Rubio V., Otegui M.S., Isono E.;
RT "Arabidopsis ALIX is required for the endosomal localization of the
RT deubiquitinating enzyme AMSH3.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E5543-E5551(2015).
RN [8]
RP SUBCELLULAR LOCATION, INTERACTION WITH ELC, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
RX PubMed=26902184; DOI=10.1016/j.molp.2016.02.005;
RA Shen J., Gao C., Zhao Q., Lin Y., Wang X., Zhuang X., Jiang L.;
RT "AtBRO1 functions in ESCRT-I complex to regulate multivesicular body
RT protein sorting.";
RL Mol. Plant 9:760-763(2016).
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 (Probable).
CC Associates with FREE1 and ELC to perform function in the ESCRT-I
CC complex. Binds ubiquitin in vitro (PubMed:26902184). Plays a role in
CC the biogenesis of vacuole and multivesicular bodies (MVBs)
CC (PubMed:26342016, PubMed:26324913). Required for the endosomal location
CC of AMSH3 (PubMed:26324913). Mediates high-affinity phosphate
CC transporter trafficking to maintain phosphate homeostasis. Regulates
CC vacuolar degradation of PHT1-1 (PubMed:26342016).
CC {ECO:0000269|PubMed:26324913, ECO:0000269|PubMed:26342016,
CC ECO:0000269|PubMed:26902184, ECO:0000305|PubMed:26342016}.
CC -!- SUBUNIT: Homodimer (PubMed:26342016). Interacts with AMSH3
CC (PubMed:26324913). Interacts with VPS32.1/SNF7B and VPS32.2/SNF7A
CC (PubMed:22639582, PubMed:26342016). Interacts with ELC/VPS23A
CC (PubMed:26902184). {ECO:0000269|PubMed:22639582,
CC ECO:0000269|PubMed:26324913, ECO:0000269|PubMed:26342016,
CC ECO:0000269|PubMed:26902184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26324913,
CC ECO:0000269|PubMed:26342016}. Late endosome
CC {ECO:0000269|PubMed:26324913}. Endosome, multivesicular body
CC {ECO:0000269|PubMed:26342016, ECO:0000269|PubMed:26902184}.
CC -!- DISRUPTION PHENOTYPE: Seedlings lethality. Severe vacuole biogenesis
CC defects. {ECO:0000269|PubMed:26324913, ECO:0000269|PubMed:26342016,
CC ECO:0000269|PubMed:26902184}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39642.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007591; AAD39642.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29270.1; -; Genomic_DNA.
DR EMBL; AY149441; AAN12917.1; -; mRNA.
DR EMBL; BT005821; AAO64756.1; -; mRNA.
DR PIR; B86285; B86285.
DR RefSeq; NP_172965.1; NM_101381.3.
DR AlphaFoldDB; F4HXZ1; -.
DR SMR; F4HXZ1; -.
DR IntAct; F4HXZ1; 3.
DR STRING; 3702.AT1G15130.1; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; F4HXZ1; -.
DR PaxDb; F4HXZ1; -.
DR PRIDE; F4HXZ1; -.
DR ProMEX; F4HXZ1; -.
DR ProteomicsDB; 240633; -.
DR EnsemblPlants; AT1G15130.1; AT1G15130.1; AT1G15130.
DR GeneID; 838077; -.
DR Gramene; AT1G15130.1; AT1G15130.1; AT1G15130.
DR KEGG; ath:AT1G15130; -.
DR Araport; AT1G15130; -.
DR TAIR; locus:2037693; AT1G15130.
DR eggNOG; KOG2220; Eukaryota.
DR HOGENOM; CLU_007181_1_0_1; -.
DR InParanoid; F4HXZ1; -.
DR OMA; SEWIHHM; -.
DR OrthoDB; 550620at2759; -.
DR PRO; PR:F4HXZ1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HXZ1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005771; C:multivesicular body; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IMP:UniProtKB.
DR GO; GO:0099638; P:endosome to plasma membrane protein transport; IMP:TAIR.
DR GO; GO:0036257; P:multivesicular body organization; IMP:UniProtKB.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:TAIR.
DR GO; GO:0007033; P:vacuole organization; IMP:UniProtKB.
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 Coiled coil; Cytoplasm; Endosome; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..846
FT /note="Vacuolar-sorting protein BRO1"
FT /id="PRO_0000440687"
FT DOMAIN 5..403
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REGION 726..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 565..592
FT /evidence="ECO:0000255"
FT COMPBIAS 726..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..805
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 260
FT /note="G->D: Reduces binding to VPS32."
FT /evidence="ECO:0000269|PubMed:26324913"
FT CONFLICT 70
FT /note="D -> E (in Ref. 3; AAN12917/AAO64756)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="N -> D (in Ref. 3; AAN12917/AAO64756)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="K -> Q (in Ref. 3; AAN12917/AAO64756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 846 AA; 95209 MW; 5033F5A235D4E51E CRC64;
MASSSLSNLM LAIHEKKTSS VDLYRPLRNY VTFTYSEREA QLIDDDLETL KQLRSDIERV
SDPSPAARRD LLISYYKVLC LVETRFPISP DKDHVNAVSF VWYDAFKQKH KATQQNIHLE
KAAVLFNLGA SYSQIGLGHD RTTVDGRRQA SHAFMAAAGA FAHLRDNESI KATIGPSTTV
DVSVECVGML ERLMVAQAQE CVFENTIAKG STPGVSAKIA RQVGIFYEEA LSALIISPLK
DHFDKGWISH VQLKAALFYG EACFRYGKEL HEKEEIAEEI ARLRSGASRL AEAKKSSRGA
PAQLIEAMNT LESSINGNLD RAVKENDRVY LMRVPSPSSL SPLPAFSMVK PMNMTDILDA
SKEKMFSILV PDSSAKALSR YTEMVDDVIR TQAERLQQAS ELTRVRLKEM DLPDSILAVD
GNSALPVDLK EDVEAVQISG GPAGLEAELQ QLRDLKRVNQ ELLVHTEELL QKEATEDSQF
RSQFGTRWTR PQSSTLTKNL QDRLNRFAAN LKQAGESDVK IERSVRDNSA LMSILDRRPI
ESAVPTLARP IMSLDATEDA IVGTLKQSLR QLENLGAQRA GLEDMLKEMK RKDDILPKLM
TITGSYEDMF RKEISKYDHI CEDISQNIEV QEQLLMQIQA QNEEFSTIFN LEDYKASKEK
CYKQIQAAIM KYREIKENIN EGLKFYVTLQ DAITNVKQQC SDFVMTRSIQ CRDMIEDVQR
QMSGLSFQDH RSSGPYPSVH QPTASSPPPP PETQNPSHPH PHAPYYRPPE QMSRPGYSIP
PYGPPPPYHT PHGQAPQPYP PQAQQQPHPS WQQGSYYDPQ GQQPRPPYPG QSPYQPPHQG
GGYYRQ
