BFR1_SCHPO
ID BFR1_SCHPO Reviewed; 1530 AA.
AC P41820; O00035; P87254; Q09194; Q9C0U4; Q9USL8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Brefeldin A resistance protein;
GN Name=bfr1; Synonyms=hba2; ORFNames=SPCC18B5.01c, SPCPJ732.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7883711; DOI=10.1128/jb.177.6.1536-1543.1995;
RA Nagao K., Taguchi Y., Arioka M., Kadokura H., Takatsuki A., Yoda K.,
RA Yamasaki M.;
RT "bfr1+, a novel gene of Schizosaccharomyces pombe which confers brefeldin A
RT resistance, is structurally related to the ATP-binding cassette
RT superfamily.";
RL J. Bacteriol. 177:1536-1543(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BAP1;
RX PubMed=7646493; DOI=10.1006/bbrc.1995.2147;
RA Turi T.G., Rose J.K.;
RT "Characterization of a novel Schizosaccharomyces pombe multidrug resistance
RT transporter conferring brefeldin A resistance.";
RL Biochem. Biophys. Res. Commun. 213:410-418(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486; SER-489; THR-491 AND
RP THR-1186, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Confers hyper-resistance to brefeldin A (BFA), an inhibitor
CC of intracellular protein transport. Could serve as an efflux pump of
CC various antibiotics.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB003671; BAA19929.1; -; Genomic_DNA.
DR EMBL; X82891; CAA58062.1; -; Genomic_DNA.
DR EMBL; S76267; AAB33744.1; -; Genomic_DNA.
DR EMBL; CU329672; CAC34990.1; -; Genomic_DNA.
DR PIR; S52239; S52239.
DR PIR; T52010; T52010.
DR RefSeq; NP_587932.3; NM_001022923.3.
DR AlphaFoldDB; P41820; -.
DR SMR; P41820; -.
DR BioGRID; 275766; 8.
DR STRING; 4896.SPCC18B5.01c.1; -.
DR TCDB; 3.A.1.205.11; the atp-binding cassette (abc) superfamily.
DR iPTMnet; P41820; -.
DR MaxQB; P41820; -.
DR PaxDb; P41820; -.
DR PRIDE; P41820; -.
DR EnsemblFungi; SPCC18B5.01c.1; SPCC18B5.01c.1:pep; SPCC18B5.01c.
DR GeneID; 2539195; -.
DR KEGG; spo:SPCC18B5.01c; -.
DR PomBase; SPCC18B5.01c; bfr1.
DR VEuPathDB; FungiDB:SPCC18B5.01c; -.
DR eggNOG; KOG0061; Eukaryota.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; P41820; -.
DR OMA; NGARRCE; -.
DR PhylomeDB; P41820; -.
DR PRO; PR:P41820; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; TAS:PomBase.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR005285; Drug-R_PDR/CDR.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 2.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00956; 3a01205; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Antibiotic resistance; ATP-binding; Glycoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1530
FT /note="Brefeldin A resistance protein"
FT /id="PRO_0000093451"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1220..1240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1255..1275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1300..1320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1338..1358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1367..1387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1392..1412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1492..1512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 153..410
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 882..1125
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 918..925
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 491
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1186
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 245
FT /note="N -> H (in Ref. 1; BAA19929/AAB33744)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="A -> D (in Ref. 1; AAB33744)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="P -> A (in Ref. 1; AAB33744)"
FT /evidence="ECO:0000305"
FT CONFLICT 997
FT /note="E -> G (in Ref. 1; BAA19929/AAB33744)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="W -> C (in Ref. 1; AAB33744)"
FT /evidence="ECO:0000305"
FT CONFLICT 1075
FT /note="A -> E (in Ref. 1; AAB33744)"
FT /evidence="ECO:0000305"
FT CONFLICT 1079
FT /note="T -> P (in Ref. 1; AAB33744)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1530 AA; 171751 MW; AD38B029AD14F8AB CRC64;
MNQNSDTTHG QALGSTLNHT TEVTRISNSS DHFEDSSSNV DESLDSSNPS SNEKASHTNE
EYRSKGNQSY VPSSSNEPSP ESSSNSDSSS SDDSSVDRLA GDPFELGENF NLKHYLRAYK
DSLQRDDIIT RSSGVCMRDH SVYGVGSGYE FLKTFPDIFL QPYRAITEKQ VVEKAILSHC
HALANAGELV MVLGQPGSGC STFLRSVTSD TVHYKRVEGT THYDGIDKAD MKKFFPGDLL
YSGENDVHFP SLTTAETLDF AAKCRTPNNR PCNLTRQEYV SRERHLIATA FGLTHTFNTK
VGNDFVRGVS GGERKRVTIS EGFATRPTIA CWDNSTRGLD SSTAFEFVNV LRTCANELKM
TSFVTAYQAS EKIYKLFDRI CVLYAGRQIY YGPADKAKQY FLDMGFDCHP RETTPDFLTA
ISDPKARFPR KGFENRVPRT PDEFEQMWRN SSVYADLMAE MESYDKRWTE TTPASSEAPE
KDNFGSDISA TTKHELYRQS AVAEKSKRVK DTSPYTVTFS QQLWYCLARS WERYINDPAY
IGSMAFAFLF QSLIIGSIFY DMKLNTVDVF SRGGVLFFSI LFCALQSLSE IANMFSQRPI
IAKHRASALY HPAADVISSL IVDLPFRFIN ISVFSIVLYF LTNLKRTAGG FWTYFLFLFI
GATCMSAFFR SLAGIMPNVE SASALGGIGV LAIAIYTGYA IPNIDVGWWF RWIAYLDPLQ
FGFESLMINE FKARQFECSQ LIPYGSGYDN YPVANKICPV TSAEPGTDYV DGSTYLYISF
NYKTRQLWRN LAIIIGYYAF LVFVNIVASE TLNFNDLKGE YLVFRRGHAP DAVKAAVNEG
GKPLDLETGQ DTQGGDVVKE SPDNEEELNK EYEGIEKGHD IFSWRNLNYD IQIKGEHRRL
LNGVQGFVVP GKLTALMGES GAGKTTLLNV LAQRVDTGVV TGDMLVNGRG LDSTFQRRTG
YVQQQDVHIG ESTVREALRF SAALRQPASV PLSEKYEYVE SVIKLLEMES YAEAIIGTPG
SGLNVEQRKR ATIGVELAAK PALLLFLDEP TSGLDSQSAW SIVCFLRKLA DAGQAILCTI
HQPSAVLFDQ FDRLLLLQKG GKTVYFGDIG EHSKTLLNYF ESHGAVHCPD DGNPAEYILD
VIGAGATATT NRDWHEVWNN SEERKAISAE LDKINASFSN SEDKKTLSKE DRSTYAMPLW
FQVKMVMTRN FQSYWREPSI LMSKLALDIF AGLFIGFTFY NQGLGVQNIQ NKLFAVFMAT
VLAVPLINGL QPKFIELRNV FEVREKPSNI YSWVAFVFSA IIVEIPFNLV FGTLFFLCWF
YPIKFYKHIH HPGDKTGYAW LLYMFFQMYF STFGQAVASA CPNAQTASVV NSLLFTFVIT
FNGVLQPNSN LVGFWHWMHS LTPFTYLIEG LLSDLVHGLP VECKSHEMLT INPPSGQTCG
EYMSAFLTNN TAAGNLLNPN ATTSCSYCPY QTADQFLERF SMRYTHRWRN LGIFVGYVFF
NIFAVLLLFY VFRVMKLRST WLGKKITGTG
