ID   BRL1_YEAST              Reviewed;         471 AA.
AC   P38770; D3DKY3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Nucleus export protein BRL1;
DE   AltName: Full=BRR6-like protein 1;
GN   Name=BRL1; OrderedLocusNames=YHR036W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BRR6.
RX   PubMed=15882446; DOI=10.1111/j.1600-0854.2005.00295.x;
RA   Saitoh Y.-H., Ogawa K., Nishimoto T.;
RT   "Brl1p - a novel nuclear envelope protein required for nuclear transport.";
RL   Traffic 6:502-517(2005).
RN   [5]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Involved in mRNA and protein export from nucleus.
CC       {ECO:0000269|PubMed:15882446}.
CC   -!- SUBUNIT: Interacts with BRR6. {ECO:0000269|PubMed:15882446}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:15882446};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:15882446}.
CC   -!- MISCELLANEOUS: Present with 1280 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the BRL1/BRR6 family. {ECO:0000305}.
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DR   EMBL; U00062; AAB68908.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06727.1; -; Genomic_DNA.
DR   PIR; S46739; S46739.
DR   RefSeq; NP_011901.1; NM_001179166.1.
DR   AlphaFoldDB; P38770; -.
DR   SMR; P38770; -.
DR   BioGRID; 36467; 842.
DR   DIP; DIP-5580N; -.
DR   IntAct; P38770; 12.
DR   MINT; P38770; -.
DR   STRING; 4932.YHR036W; -.
DR   TCDB; 9.A.34.1.1; the nuclear pore complex biogenesis (npc-b) family.
DR   iPTMnet; P38770; -.
DR   MaxQB; P38770; -.
DR   PaxDb; 4932-YHR036W; -.
DR   PeptideAtlas; P38770; -.
DR   EnsemblFungi; YHR036W_mRNA; YHR036W; YHR036W.
DR   GeneID; 856431; -.
DR   KEGG; sce:YHR036W; -.
DR   AGR; SGD:S000001078; -.
DR   SGD; S000001078; BRL1.
DR   VEuPathDB; FungiDB:YHR036W; -.
DR   eggNOG; KOG4503; Eukaryota.
DR   HOGENOM; CLU_031411_1_0_1; -.
DR   InParanoid; P38770; -.
DR   OMA; ETHSSMT; -.
DR   OrthoDB; 1363441at2759; -.
DR   BioCyc; YEAST:G3O-31096-MONOMER; -.
DR   BioGRID-ORCS; 856431; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P38770; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38770; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IDA:SGD.
DR   GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055088; P:lipid homeostasis; IMP:SGD.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006998; P:nuclear envelope organization; IMP:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR040202; Brl1/Brr6.
DR   InterPro; IPR018767; Brl1/Brr6_dom.
DR   PANTHER; PTHR28136:SF1; NUCLEUS EXPORT PROTEIN BRL1; 1.
DR   PANTHER; PTHR28136; NUCLEUS EXPORT PROTEIN BRR6; 1.
DR   Pfam; PF10104; Brr6_like_C_C; 1.
DR   SMART; SM01042; Brr6_like_C_C; 1.
PE   1: Evidence at protein level;
KW   Membrane; mRNA transport; Nucleus; Protein transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..471
FT                   /note="Nucleus export protein BRL1"
FT                   /id="PRO_0000202892"
FT   TOPO_DOM        1..299
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..407
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..471
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          66..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..91
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  53385 MW;  732209EC74DE3463 CRC64;
     MESFENLSIR DSFTSGMEHV DEELGGLSDL SISKQGPTLS PQLINRFMPH FPSSPSPLRN
     TLDFSAAKAD EEEDDRMEID EVDDTSFEEE YNNEPIETHT EATENAVVEE IEATPEERQK
     QEKNESQDQS VEEVENIVSP HRSTVIKALL SPTDLGVAAA TKVEGVVPLP PSANQDDNES
     SNNNAEGEDI IRNEEVEDEI KSSLGNHKSS QYANAFDSEI IKRELRSRSK YQPIQVSFNT
     HNYFYSDKDG IKTYSLTKPN HNKIDEFYDQ NEAFKLPKPW SPNSHPASRA SYALMSYLQL
     FLNAITTVVI FSFILSFIIA LQKDLKSTWE QRKHELQYES RICQEQYLTN RCNQTPGLPA
     LGEQCAIWKQ CMDRNNDIFF RARSTLSAKL FGDIINSFID PLNWKTLFVI FCGVITWCFS
     SNFLLGFVRA KSYYGNGIKT YPLPSSPKSP TSEETHSSMT ASGEDSHLLK Q
//