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21  structures 8465  species 0  interactions 34767  sequences 272  architectures

Family: Cation_efflux (PF01545)

Summary: Cation efflux family

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Cation diffusion facilitator". More...

Cation diffusion facilitator Edit Wikipedia article

Cation_efflux
Identifiers
SymbolCation_efflux
PfamPF01545
Pfam clanCL0184
InterProIPR002524
TCDB2.A.4
OPM superfamily204
OPM protein3h90

Cation diffusion facilitators are integral membrane proteins that increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are considered to be efflux pumps that remove these ions from cells,,[1][2] however others are implicated in ion uptake.[3] These proteins have six predicted transmembrane domains.

References

  1. ^ Xiong A, Jayaswal RK (1998). "Molecular characterization of a chromosomal determinant conferring resistance to zinc and cobalt ions in Staphylococcus aureus". J. Bacteriol. 180 (16): 4024–9. PMC 107394. PMID 9696746. {{cite journal}}: Unknown parameter |month= ignored (help)
  2. ^ Kunito T, Kusano T, Oyaizu H, Senoo K, Kanazawa S, Matsumoto S (1996). "Cloning and sequence analysis of czc genes in Alcaligenes sp. strain CT14". Biosci. Biotechnol. Biochem. 60 (4): 699–704. PMID 8829543. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  3. ^ Conklin DS, McMaster JA, Culbertson MR, Kung C (1992). "COT1, a gene involved in cobalt accumulation in Saccharomyces cerevisiae". Mol. Cell. Biol. 12 (9): 3678–88. PMC 360222. PMID 1508175. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
This article incorporates text from the public domain Pfam and InterPro: IPR002524

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This is the Wikipedia entry entitled "Zinc transporter protein". More...

Zinc transporter protein Edit Wikipedia article

Zinc transporter proteins, or simply zinc transporters, are membrane transport proteins of the solute carrier family which control the membrane transport of zinc and regulate its intracellular and cytoplasmic concentrations.[1] They include two major groups: (1) the zinc transporter (ZnT) or solute carrier 30 (SLC30) family, which controls the efflux of zinc from the cytoplasm out of the cell and from the cytoplasm into vesicles; and (2) the zinc importer, Zrt- and Irt-like protein (ZIP), or solute carrier 39A (SLC39A) family, which controls the influx of zinc into the cytoplasm from outside of the cell and from vesicles.[1]

One zinc transporter, ZIP9, is also a membrane androgen receptor.[2]

Families

ZnT (SLC30)

ZnT1, ZnT2, ZnT3, ZnT4, ZnT5, ZnT6, ZnT7, ZnT8, ZnT9, ZnT10

ZIP (SLC39A)

ZIP1, ZIP2, ZIP3, ZIP4, ZIP5, ZIP6, ZIP7, ZIP8, ZIP9, ZIP10, ZIP11, ZIP12, ZIP13, ZIP14

References

  1. ^ a b Hara T, Takeda TA, Takagishi T, Fukue K, Kambe T, Fukada T (2017). "Physiological roles of zinc transporters: molecular and genetic importance in zinc homeostasis". J Physiol Sci. 67 (2): 283–301. doi:10.1007/s12576-017-0521-4. PMID 28130681.
  2. ^ Thomas P, Converse A, Berg HA (2017). "ZIP9, a novel membrane androgen receptor and zinc transporter protein". Gen. Comp. Endocrinol. doi:10.1016/j.ygcen.2017.04.016. PMID 28479083.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Cation efflux family Provide feedback

Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells.

Literature references

  1. Xiong A, Jayaswal RK; , J Bacteriol 1998;180:4024-4029.: Molecular characterization of a chromosomal determinant conferring resistance to zinc and cobalt ions in Staphylococcus aureus. PUBMED:9696746 EPMC:9696746

  2. Kunito T, Kusano T, Oyaizu H, Senoo K, Kanazawa S, Matsumoto S; , Biosci Biotechnol Biochem 1996;60:699-704.: Cloning and sequence analysis of czc genes in Alcaligenes sp. strain CT14. PUBMED:8829543 EPMC:8829543


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002524

Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are considered to be efflux pumps that remove these ions from cells [ PUBMED:9696746 , PUBMED:8829543 ], however others are implicated in ion uptake [ PUBMED:1508175 ]. The family has six predicted transmembrane domains. Members of the family are variable in length because of variably sized inserts, often containing low-complexity sequence.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(59)
Full
(34767)
Representative proteomes UniProt
(122283)
RP15
(5042)
RP35
(16006)
RP55
(32630)
RP75
(52831)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(59)
Full
(34767)
Representative proteomes UniProt
(122283)
RP15
(5042)
RP35
(16006)
RP55
(32630)
RP75
(52831)
Alignment:
Format:
Order:
Sequence:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(59)
Full
(34767)
Representative proteomes UniProt
(122283)
RP15
(5042)
RP35
(16006)
RP55
(32630)
RP75
(52831)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_232 (release 4.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A
Number in seed: 59
Number in full: 34767
Average length of the domain: 203.5 aa
Average identity of full alignment: 20 %
Average coverage of the sequence by the domain: 55.16 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 26.6 26.6
Trusted cut-off 26.6 26.6
Noise cut-off 26.5 26.5
Model length: 199
Family (HMM) version: 24
Download: download the raw HMM for this family

Species distribution

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Selections

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Structures

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 Cation_efflux domain has been found. There are 21 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 sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044S0Z7 View 3D Structure Click here
A0A044S5B2 View 3D Structure Click here
A0A044S9B4 View 3D Structure Click here
A0A044TFJ2 View 3D Structure Click here
A0A044UJS5 View 3D Structure Click here
A0A044UTP2 View 3D Structure Click here
A0A044VAB4 View 3D Structure Click here
A0A044VBR4 View 3D Structure Click here
A0A077YVX4 View 3D Structure Click here
A0A077YW75 View 3D Structure Click here
A0A077Z9N6 View 3D Structure Click here
A0A077ZC71 View 3D Structure Click here
A0A077ZCQ1 View 3D Structure Click here
A0A077ZE56 View 3D Structure Click here
A0A077ZG62 View 3D Structure Click here
A0A077ZIP7 View 3D Structure Click here
A0A077ZJJ7 View 3D Structure Click here
A0A077ZMY3 View 3D Structure Click here
A0A0A2V2F7 View 3D Structure Click here
A0A0D2DUA4 View 3D Structure Click here
A0A0D2E3B3 View 3D Structure Click here
A0A0D2FIP0 View 3D Structure Click here
A0A0D2GSM2 View 3D Structure Click here
A0A0D2GY55 View 3D Structure Click here
A0A0D2H7K6 View 3D Structure Click here
A0A0D2HH92 View 3D Structure Click here
A0A0D2HJH3 View 3D Structure Click here
A0A0H3GLF2 View 3D Structure Click here
A0A0H3GQC6 View 3D Structure Click here
A0A0H3GY43 View 3D Structure Click here
A0A0H5S5Q5 View 3D Structure Click here
A0A0K0DS87 View 3D Structure Click here
A0A0K0DUG7 View 3D Structure Click here
A0A0K0DXY9 View 3D Structure Click here
A0A0K0E0P9 View 3D Structure Click here
A0A0K0E1C9 View 3D Structure Click here
A0A0K0E3F8 View 3D Structure Click here
A0A0K0E7V8 View 3D Structure Click here
A0A0K0EFJ0 View 3D Structure Click here
A0A0K0ELC7 View 3D Structure Click here