BRO1_NEUCR
ID BRO1_NEUCR Reviewed; 1012 AA.
AC Q7SAN9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Vacuolar protein-sorting protein bro-1;
DE AltName: Full=BRO domain-containing protein 1;
GN Name=bro-1; ORFNames=B2N18.270, NCU08001;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; BX897674; CAE85528.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA33435.1; -; Genomic_DNA.
DR RefSeq; XP_962671.1; XM_957578.2.
DR AlphaFoldDB; Q7SAN9; -.
DR SMR; Q7SAN9; -.
DR STRING; 5141.EFNCRP00000008293; -.
DR PRIDE; Q7SAN9; -.
DR EnsemblFungi; EAA33435; EAA33435; NCU08001.
DR GeneID; 3878835; -.
DR KEGG; ncr:NCU08001; -.
DR VEuPathDB; FungiDB:NCU08001; -.
DR HOGENOM; CLU_003661_0_0_1; -.
DR InParanoid; Q7SAN9; -.
DR OMA; ANHKQSA; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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..1012
FT /note="Vacuolar protein-sorting protein bro-1"
FT /id="PRO_0000218868"
FT DOMAIN 5..407
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REGION 558..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..330
FT /evidence="ECO:0000255"
FT COILED 719..775
FT /evidence="ECO:0000255"
FT COMPBIAS 785..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..946
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 112195 MW; 4D5EEAE82B302208 CRC64;
MVQAPMISVP LKATSEIDWV APLKNYIRNT YGDDPERYAE ECATLNRLRQ DMRGAGKDST
SGRDLLYRYY GQLELLDLRF PVDEKNIKIS FTWFDAFTHK PTAQYSLAFE KASIIFNISA
VLSCHAAHQL RTEEAGLKTA YHSFQASAGM FTYINENFLH APSSDLSRET VKTLISIMLA
QAQEVFLEKQ IADQKKNGLL AKLSSQAAAL YAQAVEGVQE NVTKAIFEKV WLSVVQIKLN
FMNSLAQYYQ ALADEDANSY GVAIARLEIA QGLAKEANKM AHSFPTSVPP NSNLTSDCGH
ILADATKRHL ATVKEKLEEL NKENDMIYHQ PVPAEASVAP VPKLPAAKPI PVSELYAGQD
IQRITGPDLF AKIVPLAVTE SASLYDEEKA KLVRAETERV ETANSEMAAS LDYLRLPGAL
QVLKGGFDQD ILPDEDFRTW CVDVADHESP HRIFEYLHTE KQAISTILDK SSRQLDMEES
VCEKMRSKYD AEWTQQPSSR LTTTLRTDIR RYREALEVAA KSDGQLATKL RANETELDEM
RQAAQHGEID ELFQRAVRKS RKSNPNSPAT VEPNLLEADF DDGGPSVVEQ IQKVEDILKK
LSLVKKERLQ VLQDLKQKAH SDDISQILIL NKKSIANYEQ QLFQQELEKF RPHQNRLVQA
SHKQAALMRE LTVTFNNLLQ DKRVRADQSR YESVQRSRTS VINKYKRAYQ EFLDLEAGLQ
SAKNWYKDMR QEAESLEKNV EAFVNNRRAE GAQLLNQIEQ DRAANKSSHA ALEQERLKNL
MERMSMDPSP TSPKPSSGSG GRPTPAPLSF APAAVSNTPL SAYQKSNFST QYPASPPATQ
VPHNPGGQQQ TPYQQYNPSS LGRIPGPASP PPNQTSFNIG PGRHPASPPP TQTSFAQSRP
YSLTTYGNPS ALNPQGGQPQ QSQPGGYVPP GFVPPPPPPG PPPLGPQQTV HYGGNEYYAG
AMGNPNIGRP GSGQQGPQGQ QGGWGQPPPQ QQLYQQQGGG GGDPWAGLSA WK