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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)DescriptionActionsGraphical viewLength
Metal bindingi42Magnesium1
Metal bindingi43Magnesium1
Sitei48Substrate discriminationCurated1
Sitei200Substrate discriminationCurated1
Sitei206Substrate discriminationCurated1

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
  • cellular water homeostasis Source: GO_Central
  • glycerol transport Source: UniProtKB
  • ion transmembrane transport Source: GO_Central
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10396. glpF.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 5Cytoplasmic5
Transmembranei6 – 34Helical; Name=M1Add BLAST29
Topological domaini35 – 39Periplasmic5
Transmembranei40 – 60Helical; Name=M2Add BLAST21
Topological domaini61 – 63Cytoplasmic3
Intramembranei64 – 674
Intramembranei68 – 78Helical; Name=M3Add BLAST11
Topological domaini79 – 84Cytoplasmic6
Transmembranei85 – 108Helical; Name=M4Add BLAST24
Topological domaini109 – 143PeriplasmicAdd BLAST35
Transmembranei144 – 169Helical; Name=M5Add BLAST26
Topological domaini170 – 177Cytoplasmic8
Transmembranei178 – 194Helical; Name=M6Add BLAST17
Topological domaini195 – 198Periplasmic4
Intramembranei199 – 2024
Intramembranei203 – 216Helical; Name=M7Add BLAST14
Topological domaini217 – 231PeriplasmicAdd BLAST15
Transmembranei232 – 254Helical; Name=M8Add BLAST23
Topological domaini255 – 281CytoplasmicAdd BLAST27

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi236 – 237PL → FW: No detectable water or glycerol permeability. 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000640801 – 281Glycerol uptake facilitator proteinAdd BLAST281

Proteomic databases

PaxDbiP0AER0.
PRIDEiP0AER0.

Interactioni

Subunit structurei

Homotetramer.Curated

Protein-protein interaction databases

BioGridi4263410. 157 interactors.
DIPiDIP-47976N.
IntActiP0AER0. 1 interactor.
MINTiMINT-1256193.
STRINGi511145.b3927.

Structurei

Secondary structure

1281
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 34Combined sources28
Helixi41 – 63Combined sources23
Helixi69 – 78Combined sources10
Turni83 – 85Combined sources3
Helixi86 – 118Combined sources33
Helixi126 – 128Combined sources3
Helixi129 – 132Combined sources4
Turni133 – 135Combined sources3
Helixi145 – 167Combined sources23
Beta strandi171 – 173Combined sources3
Helixi176 – 178Combined sources3
Helixi179 – 198Combined sources20
Helixi204 – 216Combined sources13
Turni217 – 221Combined sources5
Helixi222 – 225Combined sources4
Beta strandi226 – 230Combined sources5
Helixi234 – 254Combined sources21
Helixi256 – 258Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0AER0.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi68 – 70NPA 13
Motifi203 – 205NPA 23

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.
PhylomeDBiP0AER0.

Family and domain databases

CDDicd00333. MIP. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti168D → V in CAA33153 (PubMed:2544860).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti126V → I in strain: HB101. 1
Natural varianti160M → I in strain: HB101. 1
Natural varianti239G → S in strain: HB101. 1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FX8X-ray2.20A1-281[»]
1LDAX-ray2.80A1-281[»]
1LDFX-ray2.10A1-281[»]
1LDIX-ray2.70A1-281[»]
ProteinModelPortaliP0AER0.
SMRiP0AER0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263410. 157 interactors.
DIPiDIP-47976N.
IntActiP0AER0. 1 interactor.
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.
PhylomeDBiP0AER0.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AER0.
PROiP0AER0.

Family and domain databases

CDDicd00333. MIP. 1 hit.
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...

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: November 2, 2016
This is version 100 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.