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1.A.8.5.1
FPS1 glycerol efflux facilitator (important for maintaining osmotic balance during mating-induced yeast cell fusion and for tolerating hypoosmotic shock; also transports arsenite and antimonite). FPS1 is a homotetramer (Beese-Sims et al., 2011). Fps1 is important for osmo-adaptation by regulating intracellular glycerol levels during changes in external osmolarity. Upon high osmolarity conditions, yeast accumulate glycerol by increased production of the osmolyte and by restricting glycerol efflux through Fps1. The extended cytosolic termini of Fps1 contain short domains that are important for regulating glycerol flux through the channel. The transmembrane core of the protein plays an equally important role (Geijer et al., 2012).  The MAP kinase, Slt2, physically interacts with Fps1, and this interaction, dependent on phosphorylation of S537, regulates arsenite uptake (Ahmadpour et al. 2016).

Accession Number:P23900
Protein Name:FPS1 aka YLL043W
Length:669
Molecular Weight:73877.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate glycerol, arsenite, antimonite

Cross database links:

Genevestigator: P23900
eggNOG: fuNOG06419
HEGENOM: HBG202480
DIP: DIP-3979N
RefSeq: NP_013057.1   
Entrez Gene ID: 850683   
Pfam: PF00230   
KEGG: sce:YLL043W   

Gene Ontology

GO:0000324 C:fungal-type vacuole
GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0015168 F:glycerol transmembrane transporter activity
GO:0042802 F:identical protein binding
GO:0006846 P:acetate transport
GO:0015700 P:arsenite transport
GO:0000747 P:conjugation with cellular fusion
GO:0006071 P:glycerol metabolic process
GO:0015793 P:glycerol transport
GO:0046685 P:response to arsenic
GO:0042493 P:response to drug
GO:0055085 P:transmembrane transport

References (8)

[1] “A yeast homologue of the bovine lens fibre MIP gene family complements the growth defect of a Saccharomyces cerevisiae mutant on fermentable sugars but not its defect in glucose-induced RAS-mediated cAMP signalling.”  van Aelst L.et.al.   1648479
[2] “The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.”  Johnston M.et.al.   9169871
[3] “Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress.”  Luyten K.et.al.   7729414
[4] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
[5] “A global topology map of the Saccharomyces cerevisiae membrane proteome.”  Kim H.et.al.   16847258
[6] “Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.”  Li X.et.al.   17330950
[7] “Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.”  Smolka M.B.et.al.   17563356
[8] “A multidimensional chromatography technology for in-depth phosphoproteome analysis.”  Albuquerque C.P.et.al.   18407956

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSNPQKALND FLSSESVHTH DSSRKQSNKQ SSDEGRSSSQ PSHHHSGGTN NNNNNNNNNN 
61:	NSNNNNNGND GGNDDDYDYE MQDYRPSPQS ARPTPTYVPQ YSVESGTAFP IQEVIPSAYI 
121:	NTQDINHKDN GPPSASSNRA FRPRGQTTVS ANVLNIEDFY KNADDAHTIP ESHLSRRRSR 
181:	SRATSNAGHS ANTGATNGRT TGAQTNMESN ESPRNVPIMV KPKTLYQNPQ TPTVLPSTYH 
241:	PINKWSSVKN TYLKEFLAEF MGTMVMIIFG SAVVCQVNVA GKIQQDNFNV ALDNLNVTGS 
301:	SAETIDAMKS LTSLVSSVAG GTFDDVALGW AAAVVMGYFC AGGSAISGAH LNPSITLANL 
361:	VYRGFPLKKV PYYFAGQLIG AFTGALILFI WYKRVLQEAY SDWWMNESVA GMFCVFPKPY 
421:	LSSGRQFFSE FLCGAMLQAG TFALTDPYTC LSSDVFPLMM FILIFIINAS MAYQTGTAMN 
481:	LARDLGPRLA LYAVGFDHKM LWVHHHHFFW VPMVGPFIGA LMGGLVYDVC IYQGHESPVN 
541:	WSLPVYKEMI MRAWFRRPGW KKRNRARRTS DLSDFSYNND DDEEFGERMA LQKTKTKSSI 
601:	SDNENEAGEK KVQFKSVQRG KRTFGGIPTI LEEEDSIETA SLGATTTDSI GLSDTSSEDS 
661:	HYGNAKKVT