GLPF_BUCAP
ID GLPF_BUCAP Reviewed; 262 AA.
AC Q8K9M9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glycerol uptake facilitator protein {ECO:0000250|UniProtKB:P0AER0};
GN Name=glpF; OrderedLocusNames=BUsg_296;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
CC -!- FUNCTION: Mediates glycerol diffusion across the cytoplasmic membrane
CC via a pore-type mechanism. {ECO:0000250|UniProtKB:P0AER0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol(in) = glycerol(out); Xref=Rhea:RHEA:29675,
CC ChEBI:CHEBI:17754; Evidence={ECO:0000250|UniProtKB:P0AER0};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P0AER0};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P0AER0}.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AE013218; AAM67851.1; -; Genomic_DNA.
DR RefSeq; WP_011053818.1; NC_004061.1.
DR AlphaFoldDB; Q8K9M9; -.
DR SMR; Q8K9M9; -.
DR STRING; 198804.BUsg_296; -.
DR EnsemblBacteria; AAM67851; AAM67851; BUsg_296.
DR KEGG; bas:BUsg_296; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_9_3_6; -.
DR OMA; ACFPGRK; -.
DR OrthoDB; 1744995at2; -.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR PROSITE; PS00221; MIP; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..262
FT /note="Glycerol uptake facilitator protein"
FT /id="PRO_0000064079"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 8..36
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 37..41
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 42..62
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 63..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 66..69
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 70..80
FT /note="Helical; Name=M3"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 81..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 87..110
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 111..145
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 146..171
FT /note="Helical; Name=M5"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 172..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 181..197
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 198..201
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 202..205
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 206..219
FT /note="Helical; Name=M7"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 220..234
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 235..259
FT /note="Helical; Name=M8"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 260..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT MOTIF 70..72
FT /note="NPA 1"
FT /evidence="ECO:0000305"
FT MOTIF 206..208
FT /note="NPA 2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 262 AA; 29939 MW; 813A1CCE95AFB8FB CRC64;
MNFCSKKKIL KQCFFEFLGT GLIIFLGISS LVVSKLTNFH FNHCEISCIW GLGVFISICF
CSSVSGAHLN PAITIFLFLS SQFNKKKVIP YILSQISGTF FFTFLIYLIF NNLLNSFESK
YNIVRGTKKS LELASLFCVF PKENYNFIHD FILEILIGII FIIILMKLSE KNNLFKFYKF
INPFLIGTLV IIINLFLTSY SNITLNPARD LGPRIFLSLI GWGKLAFTGD DNIIFPYFLI
PTIAPIIGIN LGGWIYILYI KK
