Summary: Major Facilitator Superfamily
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Major facilitator family Edit Wikipedia article
|Major Facilitator Superfamily|
|Structure of the glycerol-3-phosphate transporter from Escherichia coli.|
Recent genome-sequencing data and a wealth of biochemical and molecular genetics investigations have revealed the occurrence of dozens of families of primary and secondary transporters. Two such families have been found to occur ubiquitously in all classifications of living organisms. These are the ATP-binding cassette (ABC) superfamily and the major facilitator superfamily (MFS), also called the uniporter-symporter-antiporter family. While ABC family permeases are in general multicomponent primary active transporters, capable of transporting both small molecules and macromolecules in response to ATP hydrolysis the MFS transporters are single-polypeptide secondary carriers capable only of transporting small solutes in response to chemiosmotic ion gradients. Although well over 100 families of transporters have now been recognised and classified, the ABC superfamily and MFS account for nearly half of the solute transporters encoded within the genomes of microorganisms. They are also prevalent in higher organisms. The importance of these two families of transport systems to living organisms can therefore not be overestimated.
The MFS was originally believed to function primarily in the uptake of sugars but subsequent studies revealed that drug efflux systems, Krebs cycle metabolites, organophosphate:phosphate exchangers, oligosaccharide:H1 symport permeases, and bacterial aromatic acid permeases were all members of the MFS. These observations led to the probability that the MFS is far more widespread in nature and far more diverse in function than had been thought previously. 17 subgroups of the MFS have been identified.
Evidence suggests that the MFS permeases arose by a tandem intragenic duplication event in the early prokaryotes. This event generated a 2-transmembrane-spanner (TMS) protein topology from a primordial 6-TMS unit. Surprisingly, all currently recognised MFS permeases retain the two six-TMS units within a single polypeptide chain, although in 3 of the 17 MFS families, an additional two TMSs are found. Moreover, the well-conserved MFS specific motif between TMS2 and TMS3 and the related but less well conserved motif between TMS8 and TMS9  prove to be a characteristic of virtually all of the more than 300 MFS proteins identified.
 Human proteins containing this domain
- FLVCR; FLVCR1; FLVCR2;
- HIAT1; HIATL1; HMFN2567;
- MFSD1; MFSD2; MFSD3; MFSD4; MFSD7; MFSD8; MFSD9;
- OAT1-4; OAT7; OCTN2VT;
- SLC16A1; SLC16A10; SLC16A11; SLC16A12; SLC16A13; SLC16A14; SLC16A2; SLC16A3; SLC16A4; SLC16A5; SLC16A6; SLC16A7; SLC16A8; SLC16A9; SLC17A1; SLC17A2; SLC17A3; SLC17A4; SLC17A5; SLC17A6; SLC17A7; SLC17A8; SLC18A1; SLC18A2; SLC18A3; SLC22A1; SLC22A10; SLC22A11; SLC22A12; SLC22A14; SLC22A15; SLC22A16; SLC22A17; SLC22A18; SLC22A2; SLC22A20; SLC22A3; SLC22A5; SLC22A6; SLC22A7; SLC22A8; SLC22A9; SLC2A13; SLC2A5; SLC37A1; SLC37A2; SLC37A3; SLC37A4; SLC43A2; SLC43A3; SLC45A1; SLC45A3; SLC46A1; SLC46A3;
- SPIN1; SPNS1; SPNS2; SPNS3;
- SV2A; SV2B; SV2C; SVOP; SVOPL; *TETRAN; TSCOT;
- hCT2; hOAT1; hOCT1; hROAT1;
- Huang Y, Lemieux MJ, Song J, Auer M, Wang DN (August 2003). "Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli". Science 301 (5633): 616–20. doi:10.1126/science.1087619. PMID 12893936.
- Paulsen IT, Pao SS, Saier Jr MH (1998). "Major Facilitator Superfamily". Microbiol. Mol. Biol. Rev. 62 (1): 1–34. PMC 98904. PMID 9529885. //www.ncbi.nlm.nih.gov/pmc/articles/PMC98904/.
- Gould GW, Walmsley AR, Barrett MP, Bringaud F (1998). "Sugar transporters from bacteria, parasites and mammals: structure-activity relationships". Trends Biochem. Sci. 23 (12): 476–481. doi:10.1016/S0968-0004(98)01326-7. PMID 9868370.
- Pao SS, Paulsen IT, Saier MH (March 1998). "Major facilitator superfamily". Microbiol. Mol. Biol. Rev. 62 (1): 1–34. PMID 9529885.
- Paulsen IT, Brown MH, Skurray RA (December 1996). "Proton-dependent multidrug efflux systems". Microbiol. Rev. 60 (4): 575–608. PMC 239457. PMID 8987357. //www.ncbi.nlm.nih.gov/pmc/articles/PMC239457/.
- Henderson PJ, Maiden MC (January 1990). "Homologous sugar transport proteins in Escherichia coli and their relatives in both prokaryotes and eukaryotes". Philos. Trans. R. Soc. Lond., B, Biol. Sci. 326 (1236): 391–410. PMID 1970645.
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Major Facilitator Superfamily Provide feedback
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Internal database links
|Similarity to PfamA using HHSearch:||BT1 OATP Folate_carrier LacY_symp LacY_symp Nuc_H_symport Nuc_H_symport PTR2 PUCC Sugar_tr Sugar_tr DUF791 MFS_3 MFS_3 TRI12 DUF1228 FPN1 ATG22 ATG22 MFS_1_like MFS_2 MFS_2|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR011701Among the different families of transporter, only two occur ubiquitously in all classifications of organisms. These are the ATP-Binding Cassette (ABC) superfamily and the Major Facilitator Superfamily (MFS). The MFS transporters are single-polypeptide secondary carriers capable only of transporting small solutes in response to chemiosmotic ion gradients [PUBMED:9529885, PUBMED:9868370].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||integral to membrane (GO:0016021)|
|Biological process||transmembrane transport (GO:0055085)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
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- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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Curation and family details
|Seed source:||Pfam-B_5 (Release 13.0)|
|Number in seed:||195|
|Number in full:||181668|
|Average length of the domain:||295.20 aa|
|Average identity of full alignment:||13 %|
|Average coverage of the sequence by the domain:||82.52 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the MFS_1 domain has been found. There are 5 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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