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Protein

Multidrug resistance protein fnx1

Gene

fnx1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Efflux transporter. Confers resistance to a variety of toxic compounds.1 Publication

GO - Molecular functioni

  • L-asparagine transmembrane transporter activity Source: PomBase
  • L-isoleucine transmembrane transporter activity Source: PomBase
  • L-lysine transmembrane transporter activity Source: PomBase

GO - Biological processi

  • asparagine transmembrane import into vacuole Source: PomBase
  • G1 to G0 transition Source: PomBase
  • isoleucine transmembrane transport Source: PomBase
  • L-alpha-amino acid transmembrane transport Source: GOC
  • L-lysine import involved in cellular response to nitrogen starvation Source: PomBase
  • L-lysine transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Biological processi

Stress response, Transport

Protein family/group databases

TCDBi2.A.1.48.3. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Multidrug resistance protein fnx1
Gene namesi
Name:fnx1
ORF Names:SPBC12C2.13c, SPBC21D10.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC12C2.13c.
PomBaseiSPBC12C2.13c. fnx1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3030CytoplasmicSequence analysisAdd
BLAST
Transmembranei31 – 5121HelicalSequence analysisAdd
BLAST
Topological domaini52 – 225174LumenalSequence analysisAdd
BLAST
Transmembranei226 – 24621HelicalSequence analysisAdd
BLAST
Topological domaini247 – 2526CytoplasmicSequence analysis
Transmembranei253 – 27321HelicalSequence analysisAdd
BLAST
Topological domaini274 – 29724LumenalSequence analysisAdd
BLAST
Transmembranei298 – 31821HelicalSequence analysisAdd
BLAST
Topological domaini319 – 36042CytoplasmicSequence analysisAdd
BLAST
Transmembranei361 – 38121HelicalSequence analysisAdd
BLAST
Topological domaini382 – 3854LumenalSequence analysis
Transmembranei386 – 40621HelicalSequence analysisAdd
BLAST
Topological domaini407 – 49690CytoplasmicSequence analysisAdd
BLAST
Transmembranei497 – 51721HelicalSequence analysisAdd
BLAST
Topological domaini518 – 53114LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • fungal-type vacuole Source: PomBase
  • fungal-type vacuole membrane Source: PomBase
  • integral component of vacuolar membrane Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 531531Multidrug resistance protein fnx1PRO_0000173421Add
BLAST

Proteomic databases

MaxQBiQ09752.

Expressioni

Inductioni

By nitrogen starvation.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi276336. 1 interaction.
MINTiMINT-4694705.

Structurei

3D structure databases

ProteinModelPortaliQ09752.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the major facilitator superfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000214685.
InParanoidiQ09752.
OMAiQFAMGSI.
OrthoDBiEOG74FF92.
PhylomeDBiQ09752.

Family and domain databases

InterProiIPR011701. MFS.
IPR020846. MFS_dom.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 3 hits.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09752-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDQVNLATE QTSLLYPEVS RKKEELSVNK WTILPALWVG GFLSALDMTI
60 70 80 90 100
VASLYPVIGS EFKLMNNASY IVTAYLITNT AFQPLYGRLS DIFGRRPTVV
110 120 130 140 150
FANAAFTLGT FWCGISRSLP ELCMARALAG IGGGGLGTMS SIISSDIVSL
160 170 180 190 200
RERGTWQGIT NIVWGIGGSL GGPLGGLIAQ RWGWRTAFHF QVPMGILSTI
210 220 230 240 250
LVAWRVRVKP TVRNSNASLL SRIDYLGSFL LVTGITALVV TFNMGGDAFP
260 270 280 290 300
WVSPVIITLL VSSVLILFAF YWVEKNIAVE PIAPVEILSQ PTPLNVCLGN
310 320 330 340 350
FFNAFCSFVI VYELPLFFET TLLMPSSEAG VRIFPYVIST SVGSLCSGLY
360 370 380 390 400
MKKTGRYRNL VIAGFFFMLM GIVSFAVLTS FGHRTPLILI SLCLAMTGCS
410 420 430 440 450
YGMNLTSTLI AIISSLAPEE QAVATGLSYL FRATGSVIGI SLSQTTTLSI
460 470 480 490 500
LMKQLASNLK DDPDKDDLIR RLRESISIIP NLPKDIQKLV IKSYATAFTW
510 520 530
TFALVAIIAF AGFWCSLRIK QFYLHTSVDR S
Length:531
Mass (Da):58,058
Last modified:August 14, 2001 - v2
Checksum:i7052F7F8A82C63F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721V → A in AAC32768 (PubMed:9710608).Curated
Sequence conflicti295 – 3006NVCLGN → ECLFGY in AAC32768 (PubMed:9710608).Curated
Sequence conflicti324 – 33310MPSSEAGVRI → CHRLRPVFVS in AAC32768 (PubMed:9710608).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029304 Genomic DNA. Translation: AAC32768.1.
CU329671 Genomic DNA. Translation: CAA20760.1.
AB027935 Genomic DNA. Translation: BAA87239.1.
PIRiT43551.
RefSeqiNP_596009.1. NM_001021917.2.

Genome annotation databases

EnsemblFungiiSPBC12C2.13c.1; SPBC12C2.13c.1:pep; SPBC12C2.13c.
GeneIDi2539786.
KEGGispo:SPBC12C2.13c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029304 Genomic DNA. Translation: AAC32768.1.
CU329671 Genomic DNA. Translation: CAA20760.1.
AB027935 Genomic DNA. Translation: BAA87239.1.
PIRiT43551.
RefSeqiNP_596009.1. NM_001021917.2.

3D structure databases

ProteinModelPortaliQ09752.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276336. 1 interaction.
MINTiMINT-4694705.

Protein family/group databases

TCDBi2.A.1.48.3. the major facilitator superfamily (mfs).

Proteomic databases

MaxQBiQ09752.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC12C2.13c.1; SPBC12C2.13c.1:pep; SPBC12C2.13c.
GeneIDi2539786.
KEGGispo:SPBC12C2.13c.

Organism-specific databases

EuPathDBiFungiDB:SPBC12C2.13c.
PomBaseiSPBC12C2.13c. fnx1.

Phylogenomic databases

HOGENOMiHOG000214685.
InParanoidiQ09752.
OMAiQFAMGSI.
OrthoDBiEOG74FF92.
PhylomeDBiQ09752.

Miscellaneous databases

PROiQ09752.

Family and domain databases

InterProiIPR011701. MFS.
IPR020846. MFS_dom.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 3 hits.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The role of fnx1, a fission yeast multidrug resistance protein, in the transition of cells to a quiescent G0 state."
    Dimitrov K., Sazer S.
    Mol. Cell. Biol. 18:5239-5246(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 292-462, SUBCELLULAR LOCATION.
    Strain: ATCC 38364 / 968.
  4. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFNX1_SCHPO
AccessioniPrimary (citable) accession number: Q09752
Secondary accession number(s): Q9URP7, Q9USV8, Q9UTY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 14, 2001
Last modified: June 8, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.