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Protein

Glycerol uptake facilitator protein

Gene

glpF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transporter of glycerol across the cytoplasmic membrane, with limited permeability to water and small uncharged compounds such as polyols.

Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421Magnesium
Metal bindingi43 – 431Magnesium
Sitei48 – 481Substrate discriminationCurated
Sitei200 – 2001Substrate discriminationCurated
Sitei206 – 2061Substrate discriminationCurated

GO - Molecular functioni

  • glycerol channel activity Source: EcoCyc
  • glycerol transmembrane transporter activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • water channel activity Source: GO_Central

GO - Biological processi

  • cellular response to mercury ion Source: UniProtKB
  • glycerol transport Source: UniProtKB
  • ion transmembrane transport Source: GO_Central
  • water transport Source: GOC
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:GLPF-MONOMER.
ECOL316407:JW3898-MONOMER.
MetaCyc:GLPF-MONOMER.

Protein family/group databases

TCDBi1.A.8.1.1. the major intrinsic protein (mip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol uptake facilitator protein
Alternative name(s):
Aquaglyceroporin
Gene namesi
Name:glpF
Ordered Locus Names:b3927, JW3898
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10396. glpF.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55Cytoplasmic
Transmembranei6 – 3429Helical; Name=M1Add
BLAST
Topological domaini35 – 395Periplasmic
Transmembranei40 – 6021Helical; Name=M2Add
BLAST
Topological domaini61 – 633Cytoplasmic
Intramembranei64 – 674
Intramembranei68 – 7811Helical; Name=M3Add
BLAST
Topological domaini79 – 846Cytoplasmic
Transmembranei85 – 10824Helical; Name=M4Add
BLAST
Topological domaini109 – 14335PeriplasmicAdd
BLAST
Transmembranei144 – 16926Helical; Name=M5Add
BLAST
Topological domaini170 – 1778Cytoplasmic
Transmembranei178 – 19417Helical; Name=M6Add
BLAST
Topological domaini195 – 1984Periplasmic
Intramembranei199 – 2024
Intramembranei203 – 21614Helical; Name=M7Add
BLAST
Topological domaini217 – 23115PeriplasmicAdd
BLAST
Transmembranei232 – 25423Helical; Name=M8Add
BLAST
Topological domaini255 – 28127CytoplasmicAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi236 – 2372PL → FW: No detectable water or glycerol permeability.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281Glycerol uptake facilitator proteinPRO_0000064080Add
BLAST

Proteomic databases

PaxDbiP0AER0.
PRIDEiP0AER0.

Interactioni

Subunit structurei

Homotetramer.Curated

Protein-protein interaction databases

BioGridi4263410. 157 interactions.
DIPiDIP-47976N.
IntActiP0AER0. 1 interaction.
MINTiMINT-1256193.
STRINGi511145.b3927.

Structurei

Secondary structure

1
281
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 3428Combined sources
Helixi41 – 6323Combined sources
Helixi69 – 7810Combined sources
Turni83 – 853Combined sources
Helixi86 – 11833Combined sources
Helixi126 – 1283Combined sources
Helixi129 – 1324Combined sources
Turni133 – 1353Combined sources
Helixi145 – 16723Combined sources
Beta strandi171 – 1733Combined sources
Helixi176 – 1783Combined sources
Helixi179 – 19820Combined sources
Helixi204 – 21613Combined sources
Turni217 – 2215Combined sources
Helixi222 – 2254Combined sources
Beta strandi226 – 2305Combined sources
Helixi234 – 25421Combined sources
Helixi256 – 2583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FX8X-ray2.20A1-281[»]
1LDAX-ray2.80A1-281[»]
1LDFX-ray2.10A1-281[»]
1LDIX-ray2.70A1-281[»]
ProteinModelPortaliP0AER0.
SMRiP0AER0. Positions 6-259.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AER0.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi68 – 703NPA 1
Motifi203 – 2053NPA 2

Domaini

Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D8C. Bacteria.
COG0580. LUCA.
HOGENOMiHOG000288287.
InParanoidiP0AER0.
KOiK02440.
OMAiAREIPYF.
OrthoDBiEOG6TXQWK.
PhylomeDBiP0AER0.

Family and domain databases

Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AER0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQTSTLKGQ CIAEFLGTGL LIFFGVGCVA ALKVAGASFG QWEISVIWGL
60 70 80 90 100
GVAMAIYLTA GVSGAHLNPA VTIALWLFAC FDKRKVIPFI VSQVAGAFCA
110 120 130 140 150
AALVYGLYYN LFFDFEQTHH IVRGSVESVD LAGTFSTYPN PHINFVQAFA
160 170 180 190 200
VEMVITAILM GLILALTDDG NGVPRGPLAP LLIGLLIAVI GASMGPLTGF
210 220 230 240 250
AMNPARDFGP KVFAWLAGWG NVAFTGGRDI PYFLVPLFGP IVGAIVGAFA
260 270 280
YRKLIGRHLP CDICVVEEKE TTTPSEQKAS L
Length:281
Mass (Da):29,780
Last modified:December 20, 2005 - v1
Checksum:i94E8D2B79B6E6568
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 1681D → V in CAA33153 (PubMed:2544860).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti126 – 1261V → I in strain: HB101.
Natural varianti160 – 1601M → I in strain: HB101.
Natural varianti239 – 2391G → S in strain: HB101.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15054 Genomic DNA. Translation: CAA33153.1.
M55990 Genomic DNA. Translation: AAA23886.1.
L19201 Genomic DNA. Translation: AAB03059.1.
U00096 Genomic DNA. Translation: AAC76909.1.
AP009048 Genomic DNA. Translation: BAE77383.1.
U13915 Genomic DNA. Translation: AAA21363.1.
PIRiA42157. XMECGF.
RefSeqiNP_418362.1. NC_000913.3.
WP_000084268.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76909; AAC76909; b3927.
BAE77383; BAE77383; BAE77383.
GeneIDi948422.
KEGGiecj:JW3898.
eco:b3927.
PATRICi32123367. VBIEscCol129921_4044.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15054 Genomic DNA. Translation: CAA33153.1.
M55990 Genomic DNA. Translation: AAA23886.1.
L19201 Genomic DNA. Translation: AAB03059.1.
U00096 Genomic DNA. Translation: AAC76909.1.
AP009048 Genomic DNA. Translation: BAE77383.1.
U13915 Genomic DNA. Translation: AAA21363.1.
PIRiA42157. XMECGF.
RefSeqiNP_418362.1. NC_000913.3.
WP_000084268.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FX8X-ray2.20A1-281[»]
1LDAX-ray2.80A1-281[»]
1LDFX-ray2.10A1-281[»]
1LDIX-ray2.70A1-281[»]
ProteinModelPortaliP0AER0.
SMRiP0AER0. Positions 6-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263410. 157 interactions.
DIPiDIP-47976N.
IntActiP0AER0. 1 interaction.
MINTiMINT-1256193.
STRINGi511145.b3927.

Protein family/group databases

TCDBi1.A.8.1.1. the major intrinsic protein (mip) family.

Proteomic databases

PaxDbiP0AER0.
PRIDEiP0AER0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76909; AAC76909; b3927.
BAE77383; BAE77383; BAE77383.
GeneIDi948422.
KEGGiecj:JW3898.
eco:b3927.
PATRICi32123367. VBIEscCol129921_4044.

Organism-specific databases

EchoBASEiEB0391.
EcoGeneiEG10396. glpF.

Phylogenomic databases

eggNOGiENOG4105D8C. Bacteria.
COG0580. LUCA.
HOGENOMiHOG000288287.
InParanoidiP0AER0.
KOiK02440.
OMAiAREIPYF.
OrthoDBiEOG6TXQWK.
PhylomeDBiP0AER0.

Enzyme and pathway databases

BioCyciEcoCyc:GLPF-MONOMER.
ECOL316407:JW3898-MONOMER.
MetaCyc:GLPF-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AER0.
PROiP0AER0.

Family and domain databases

Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the region encompassing the glpKF operon and its upstream region containing a bent DNA sequence of Escherichia coli."
    Muramatsu S., Mizuno T.
    Nucleic Acids Res. 17:4378-4378(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12."
    Weissenborn D.L., Wittekindt N., Larson T.J.
    J. Biol. Chem. 267:6122-6131(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Escherichia coli HB101 nucleotide sequence of the glycerol diffusion facilitator protein gene."
    Chun B.W., Yang M.S.
    Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33694 / HB101.
  4. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Substrate specificity and transport properties of the glycerol facilitator of Escherichia coli."
    Heller K.B., Lin E.C., Wilson T.H.
    J. Bacteriol. 144:274-278(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY.
  8. "Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli."
    Borgnia M.J., Agre P.
    Proc. Natl. Acad. Sci. U.S.A. 98:2888-2893(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF PRO-236 AND LEU-237.
  9. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  10. "Structure of a glycerol-conducting channel and the basis for its selectivity."
    Fu D., Libson A., Miercke L.J., Weitzman C., Nollert P., Krucinski J., Stroud R.M.
    Science 290:481-486(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  11. Cited for: REVIEW ON THE MEMBRANE STRUCTURE.
  12. "Control of the selectivity of the aquaporin water channel family by global orientational tuning."
    Tajkhorshid E., Nollert P., Jensen M.O., Miercke L.J., O'Connell J.D. III, Stroud R.M., Schulten K.
    Science 296:525-530(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELECTIVITY OF THE WATER CHANNEL.

Entry informationi

Entry nameiGLPF_ECOLI
AccessioniPrimary (citable) accession number: P0AER0
Secondary accession number(s): P11244, Q2M8M3, Q46727
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: February 17, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The remarkable property of effective water conductance combined with a strict exclusion of all ions including protons is mediated by two conserved asparagines which force a central water molecule to serve strictly as a hydrogen bond donor to its neighboring water molecules. Assisted by the electrostatic potential generated by two half-membrane spanning loops, this dictates opposite orientations of water molecules in the two halves of the channel, and thus prevents the formation of a "proton wire", while permitting rapid water diffusion.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.