BRE4_ASHGO
ID BRE4_ASHGO Reviewed; 1053 AA.
AC Q75E41;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Protein BRE4;
GN Name=BRE4; OrderedLocusNames=ABL171W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 204 AND 257-258.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: May be involved in intracellular vesicle transport.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BRE4 family. {ECO:0000305}.
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DR EMBL; AE016815; AAS50600.2; -; Genomic_DNA.
DR RefSeq; NP_982776.2; NM_208129.2.
DR AlphaFoldDB; Q75E41; -.
DR SMR; Q75E41; -.
DR STRING; 284811.Q75E41; -.
DR EnsemblFungi; AAS50600; AAS50600; AGOS_ABL171W.
DR GeneID; 4618856; -.
DR KEGG; ago:AGOS_ABL171W; -.
DR eggNOG; KOG4711; Eukaryota.
DR HOGENOM; CLU_004486_0_0_1; -.
DR InParanoid; Q75E41; -.
DR OMA; FWGWAAN; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR023244; Brefeldin_A-sensitivity_4.
DR PRINTS; PR02047; BREFELDNASP4.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1053
FT /note="Protein BRE4"
FT /id="PRO_0000239633"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 794..814
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1003
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1053 AA; 119045 MW; DB0E289904773BD6 CRC64;
MEVLKGSYKQ KSFQSLKDLG QQGSSAAPGV RPTKSLQTSP IGSWTSLSHL RLEKLAEGSG
WEELQDYGLE ELRDGFFDAS YSRPQRVAAT EPPVSTSPKA QSPLAVRCKA FRDRLRVHWK
AVVKFTVAYL AAMFLCLVRP ASDWIGDVYS CFLPVAVLIH HPVRTVGVQL EITVQSIVGL
ALGQGWSALW WYVCSVARVG RHEGALLFLS LVLSGLWSSW LAAAYGRLVY MSVSFGITAT
FFATSMPPSE GSLPIWRHFW DQGMSYLFGL LLSLLVCIFL FPRFGHATIG RGFSSAANDL
KHLLDYLVDA RYCNDIPMLV EAQENAVSAI DVRLSEGYRE FANQFSITRF DGKLLEQLRN
SLTIAASPLR SLPLGHGLLT NVELERFHQA RPQSAPENTI CVRDADDHYE DQAIKTEESA
NLGLACGSTD LCSAIIRDKF SETIFDLIME LIHALNSLQV GLNNISESNV SASERADIKA
NILACLSNLH DRIRRLDIKY KEFGRAGLFT SELLLNPKSS DALVFLRYIR QCAKHMTKVL
EVFLQLNASV HWRVIPPKYQ WHRAIHRLSH QCALDQGASF LWNYFQTKRD VDDAFEMIYN
SYTSKHHEVS DLFSRQGMRP RIRAFDHKDF AVHSTSNPIR YKLWQLNNSL LGPESRWARK
FTVVLVALCL PGWLPGSKVW YREYHCLWAP IIYVILSNRR NSSNWRALYK RLAGCVLGVF
WAWCANQAKH YSNPFIIATF SVLLCIPLAF NYFAYNRRKS TLAALICFTV PALVTFFLEE
HTTASLWKQA WTTGVALLIG TFCSIPINWF IWTFTARSEL SLAVSGLLMH LSQSYQIVAG
RYLYRDTDDH PNDLTRSLAS IREVRLSQSL LATRALVRSA VSEPNIVSEF RAYLFDELLD
HFSVLLERLI EARRLGQHFQ VWDRDPNTET TRALLSLRRD NVASVIFIFY MLSNCFSSGS
KVPKYLPNPI FVRKKLFDTF MKLAEDASAR GTSAHSSTPA APNNTDPSSP SSAGQDHWDE
VYAICFSRAF TDISVELQRI IDLAKEILGQ EGD