FNX1_SCHPO
ID FNX1_SCHPO Reviewed; 531 AA.
AC Q09752; Q9URP7; Q9USV8; Q9UTY2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Multidrug resistance protein fnx1;
GN Name=fnx1; ORFNames=SPBC12C2.13c, SPBC21D10.04c;
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], FUNCTION, AND INDUCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9710608; DOI=10.1128/mcb.18.9.5239;
RA Dimitrov K., Sazer S.;
RT "The role of fnx1, a fission yeast multidrug resistance protein, in the
RT transition of cells to a quiescent G0 state.";
RL Mol. Cell. Biol. 18:5239-5246(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 292-462, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Efflux transporter. Confers resistance to a variety of toxic
CC compounds. {ECO:0000269|PubMed:9710608}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: By nitrogen starvation. {ECO:0000269|PubMed:9710608}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AF029304; AAC32768.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA20760.1; -; Genomic_DNA.
DR EMBL; AB027935; BAA87239.1; -; Genomic_DNA.
DR PIR; T43551; T43551.
DR RefSeq; NP_596009.1; NM_001021917.2.
DR AlphaFoldDB; Q09752; -.
DR SMR; Q09752; -.
DR BioGRID; 276336; 3.
DR STRING; 4896.SPBC12C2.13c.1; -.
DR TCDB; 2.A.1.48.3; the major facilitator superfamily (mfs).
DR iPTMnet; Q09752; -.
DR MaxQB; Q09752; -.
DR PaxDb; Q09752; -.
DR PRIDE; Q09752; -.
DR EnsemblFungi; SPBC12C2.13c.1; SPBC12C2.13c.1:pep; SPBC12C2.13c.
DR GeneID; 2539786; -.
DR KEGG; spo:SPBC12C2.13c; -.
DR PomBase; SPBC12C2.13c; fnx1.
DR VEuPathDB; FungiDB:SPBC12C2.13c; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_3_1; -.
DR InParanoid; Q09752; -.
DR OMA; ITNIVWG; -.
DR PhylomeDB; Q09752; -.
DR PRO; PR:Q09752; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0071627; C:integral component of fungal-type vacuolar membrane; IC:PomBase.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015182; F:L-asparagine transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0015188; F:L-isoleucine transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1990591; P:asparagine transmembrane import into vacuole; IMP:PomBase.
DR GO; GO:0015802; P:basic amino acid transport; IBA:GO_Central.
DR GO; GO:1903714; P:isoleucine transmembrane transport; IMP:PomBase.
DR GO; GO:1901482; P:L-lysine import into vacuole involved in cellular response to nitrogen starvation; IMP:PomBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..531
FT /note="Multidrug resistance protein fnx1"
FT /id="PRO_0000173421"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..225
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..297
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..385
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..531
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CONFLICT 72
FT /note="V -> A (in Ref. 1; AAC32768)"
FT /evidence="ECO:0000305"
FT CONFLICT 295..300
FT /note="NVCLGN -> ECLFGY (in Ref. 1; AAC32768)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..333
FT /note="MPSSEAGVRI -> CHRLRPVFVS (in Ref. 1; AAC32768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 58058 MW; 7052F7F8A82C63F9 CRC64;
MVDQVNLATE QTSLLYPEVS RKKEELSVNK WTILPALWVG GFLSALDMTI VASLYPVIGS
EFKLMNNASY IVTAYLITNT AFQPLYGRLS DIFGRRPTVV FANAAFTLGT FWCGISRSLP
ELCMARALAG IGGGGLGTMS SIISSDIVSL RERGTWQGIT NIVWGIGGSL GGPLGGLIAQ
RWGWRTAFHF QVPMGILSTI LVAWRVRVKP TVRNSNASLL SRIDYLGSFL LVTGITALVV
TFNMGGDAFP WVSPVIITLL VSSVLILFAF YWVEKNIAVE PIAPVEILSQ PTPLNVCLGN
FFNAFCSFVI VYELPLFFET TLLMPSSEAG VRIFPYVIST SVGSLCSGLY MKKTGRYRNL
VIAGFFFMLM GIVSFAVLTS FGHRTPLILI SLCLAMTGCS YGMNLTSTLI AIISSLAPEE
QAVATGLSYL FRATGSVIGI SLSQTTTLSI LMKQLASNLK DDPDKDDLIR RLRESISIIP
NLPKDIQKLV IKSYATAFTW TFALVAIIAF AGFWCSLRIK QFYLHTSVDR S
