FNX2_SCHPO
ID FNX2_SCHPO Reviewed; 577 AA.
AC O59726; Q9US91;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Vacuolar membrane amino acid uptake transporter fnx2;
GN Name=fnx2; ORFNames=SPBC3E7.06c;
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] {ECO:0000312|EMBL:CAA19010.1}
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 [2] {ECO:0000305, ECO:0000312|EMBL:BAA87255.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 38-238, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968 {ECO:0000269|PubMed:10759889};
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 [3] {ECO:0000305}
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).
RN [4]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18503766; DOI=10.1016/j.febslet.2008.05.017;
RA Chardwiriyapreecha S., Shimazu M., Morita T., Sekito T., Akiyama K.,
RA Takegawa K., Kakinuma Y.;
RT "Identification of the fnx1+ and fnx2+ genes for vacuolar amino acid
RT transporters in Schizosaccharomyces pombe.";
RL FEBS Lett. 582:2225-2230(2008).
CC -!- FUNCTION: MFS-type transporter involved in vacuolar amino acid uptake.
CC {ECO:0000269|PubMed:18503766}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}. Membrane {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000255}.
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DR EMBL; CU329671; CAA19010.1; -; Genomic_DNA.
DR EMBL; AB027951; BAA87255.1; -; Genomic_DNA.
DR PIR; T40380; T40380.
DR RefSeq; NP_596093.1; NM_001022009.2.
DR AlphaFoldDB; O59726; -.
DR SMR; O59726; -.
DR BioGRID; 277531; 3.
DR STRING; 4896.SPBC3E7.06c.1; -.
DR TCDB; 2.A.1.48.4; the major facilitator superfamily (mfs).
DR iPTMnet; O59726; -.
DR MaxQB; O59726; -.
DR PaxDb; O59726; -.
DR PRIDE; O59726; -.
DR EnsemblFungi; SPBC3E7.06c.1; SPBC3E7.06c.1:pep; SPBC3E7.06c.
DR GeneID; 2541016; -.
DR KEGG; spo:SPBC3E7.06c; -.
DR PomBase; SPBC3E7.06c; fnx2.
DR VEuPathDB; FungiDB:SPBC3E7.06c; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_3_1; -.
DR InParanoid; O59726; -.
DR OMA; GLMNIVW; -.
DR PhylomeDB; O59726; -.
DR PRO; PR:O59726; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
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:0090517; P:L-lysine transmembrane import into vacuole; 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 3: Inferred from homology;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..577
FT /note="Vacuolar membrane amino acid uptake transporter
FT fnx2"
FT /id="PRO_0000372714"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 38
FT /note="Y -> N (in Ref. 2; BAA87255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 62900 MW; F5999403CA97F64A CRC64;
MSNPRTKSPN TNRGQGLRSE RSALLNDSLS SLNGNSSYDS IKDSSKNNKD VAEVNEYPRR
PESSVSVVSN SPHRQDAATT NTVSTVSVSK VLPALLLGVV LAALDNTIVA STYTKIGAEF
GKFSQVSWTA TAYMISCTAF QPLFGKFCDI YGRKKTLLAA YCVFGIGCFL CGTSRSLWQL
VAARAIAGIG GGGMNSTVSI LMSDIVPLKQ RGTYQGIINV FFAIGSSLGG PVGGYFADQY
TWRIGFLIQV PLIAIAFLCV YFTLNLPHHN HVSFMTRFRK IDLKGLILLI IGVTTMTCAF
TLGGNVREWN DPVVISLLIA SSISYLSFVY VEAFVAFEPL APMDVLTERT CLSSYLCNFF
HSVANFGWIY GMPLFFQSIK NEGAEKSGIR LIPMIIGSSL GSLLGGAVIS LTGNYKKITV
GSYFFGSVAA LFMLRYGYSN FNWEYAVYPF SGGLGNGIAV TTTLVAIIHA SPSAFQASAI
ATSYLFRSNG CVLGVSISSS IVQTVLGIKL RKSLDFDVDE LLHHLRKDIS YVHRLPEEIR
QTVLDALLGS IHYSFLFVSF MFFCAFVCSM FIKNRNL
