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0  structures 1383  species 0  interactions 3668  sequences 61  architectures

Family: MPC (PF03650)

Summary: Mitochondrial pyruvate carriers

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

The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

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.

Mitochondrial pyruvate carriers Provide feedback

This family includes mitochondrial pyruvate carrier proteins, such as Mpc 1/2 and their homologues. They mediate the uptake of pyruvate into mitochondria [1]. In humans, Mpc1 and Mpc2 associate to form an ~150-kilodalton complex in the inner mitochondrial membrane [2]. MPC1 contains two predicted transmembrane regions. MPC2 contains three predicted transmembrane regions. Several studies have demonstrated MPC involvement in the control of cell fate in cancer and gluconeogenesis in models of type 2 diabetes [3].

Literature references

  1. Bricker DK, Taylor EB, Schell JC, Orsak T, Boutron A, Chen YC, Cox JE, Cardon CM, Van Vranken JG, Dephoure N, Redin C, Boudina S, Gygi SP, Brivet M, Thummel CS, Rutter J;, Science. 2012;337:96-100.: A mitochondrial pyruvate carrier required for pyruvate uptake in yeast, Drosophila, and humans. PUBMED:22628558 EPMC:22628558

  2. Bricker DK, Taylor EB, Schell JC, Orsak T, Boutron A, Chen YC, Cox JE, Cardon CM, Van Vranken JG, Dephoure N, Redin C, Boudina S, Gygi SP, Brivet M, Thummel CS, Rutter J;, Science. 2012;337:96-100.: A mitochondrial pyruvate carrier required for pyruvate uptake in yeast, Drosophila, and humans. PUBMED:22628558 EPMC:22628558

  3. Gray LR, Rauckhorst AJ, Taylor EB;, J Biol Chem. 2016;291:7409-7417.: A Method for Multiplexed Measurement of Mitochondrial Pyruvate Carrier Activity. PUBMED:26823462 EPMC:26823462


This tab holds annotation information from the InterPro database.

InterPro entry IPR005336

This entry represents the mitochondrial pyruvate carrier proteins, including Mpc 1/2 and their homologues. They mediate the uptake of pyruvate into mitochondria [ PUBMED:22628558 ]. In humans, Mpc1 and Mpc2 associate to form an ~150-kilodalton complex in the inner mitochondrial membrane [ PUBMED:22628558 ].

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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Pfam Clan

This family is a member of clan MtN3-like (CL0141), which has the following description:

The clan forms a large and diverse family of proteins with seven transmembrane helices, common topology and, most likely, similar function. Their coding genes exist in all eukaryota and in several prokaryota. Some are responsible for metabolic diseases (cystinosis, congenital disorder of glycosylation), others are candidate genes for genetic disorders (cleft lip and palate, certain forms of cancer) or solute uptake and efflux (SWEETs) and many have not yet been assigned a function. Comparison with the properties of well-annotated clan members suggests that the proteins could be involved in protein trafficking and serve as cargo receptors in vesicle trafficking [3].

The clan contains the following 5 members:

ER_lumen_recept LAB_N MPC MtN3_slv PQ-loop

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...

View options

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
(41)
Full
(3668)
Representative proteomes UniProt
(6290)
RP15
(689)
RP35
(1719)
RP55
(2886)
RP75
(3907)
Jalview View  View  View  View  View  View  View 
HTML View  View           
PP/heatmap 1 View           

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

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

Format an alignment

  Seed
(41)
Full
(3668)
Representative proteomes UniProt
(6290)
RP15
(689)
RP35
(1719)
RP55
(2886)
RP75
(3907)
Alignment:
Format:
Order:
Sequence:
Gaps:
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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
(41)
Full
(3668)
Representative proteomes UniProt
(6290)
RP15
(689)
RP35
(1719)
RP55
(2886)
RP75
(3907)
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: SWISS-PROT
Previous IDs: UPF0041;
Type: Repeat
Sequence Ontology: SO:0001068
Author: Bateman A , El-Gebali S
Number in seed: 41
Number in full: 3668
Average length of the domain: 100.20 aa
Average identity of full alignment: 36 %
Average coverage of the sequence by the domain: 72.47 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.5 20.5
Trusted cut-off 20.6 20.6
Noise cut-off 20.4 20.4
Model length: 110
Family (HMM) version: 15
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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
A0A0R0EVG8 View 3D Structure Click here
A0A0R0FM05 View 3D Structure Click here
A0A1D6G4J7 View 3D Structure Click here
A0A1D6IYU1 View 3D Structure Click here
A0A1D6IYU1 View 3D Structure Click here
A0A1D6L8C5 View 3D Structure Click here
A0A1D8PJH2 View 3D Structure Click here
A4HRF6 View 3D Structure Click here
A4HW93 View 3D Structure Click here
B6SX80 View 3D Structure Click here
B6UEL2 View 3D Structure Click here
C6TIH5 View 3D Structure Click here
F1Q6Z3 View 3D Structure Click here
F1RD76 View 3D Structure Click here
I1KZY3 View 3D Structure Click here
I1LF33 View 3D Structure Click here
I1MFM5 View 3D Structure Click here
I1MJ03 View 3D Structure Click here
I1N324 View 3D Structure Click here
I1N7N2 View 3D Structure Click here
I1NFA7 View 3D Structure Click here
K7L1Z1 View 3D Structure Click here
O01578 View 3D Structure Click here
O49636 View 3D Structure Click here
O74847 View 3D Structure Click here
O95563 View 3D Structure Click here
P0DKB6 View 3D Structure Click here
P38718 View 3D Structure Click here
P38857 View 3D Structure Click here
P53157 View 3D Structure Click here
P53311 View 3D Structure Click here
P63030 View 3D Structure Click here
P63031 View 3D Structure Click here
Q09896 View 3D Structure Click here
Q0D5K8 View 3D Structure Click here
Q21828 View 3D Structure Click here
Q4CPM4 View 3D Structure Click here
Q4D773 View 3D Structure Click here
Q4DM20 View 3D Structure Click here
Q4DMF5 View 3D Structure Click here
Q55GU3 View 3D Structure Click here
Q55GU4 View 3D Structure Click here
Q5A328 View 3D Structure Click here
Q6H4I2 View 3D Structure Click here
Q6IQT9 View 3D Structure Click here
Q6Z565 View 3D Structure Click here
Q6ZB58 View 3D Structure Click here
Q7KSC4 View 3D Structure Click here
Q7XIT4 View 3D Structure Click here
Q8IDS8 View 3D Structure Click here
Q8IKD4 View 3D Structure Click here
Q8INZ7 View 3D Structure Click here
Q8L7H8 View 3D Structure Click here
Q8LD38 View 3D Structure Click here
Q949R9 View 3D Structure Click here
Q9D023 View 3D Structure Click here
Q9VHB1 View 3D Structure Click here
Q9VHB2 View 3D Structure Click here
Q9Y5U8 View 3D Structure Click here

trRosetta Structure

The structural model below was generated by the Baker group with the trRosetta software using the Pfam UniProt multiple sequence alignment.

The InterPro website shows the contact map for the Pfam SEED alignment. Hovering or clicking on a contact position will highlight its connection to other residues in the alignment, as well as on the 3D structure.

Improved protein structure prediction using predicted inter-residue orientations. Jianyi Yang, Ivan Anishchenko, Hahnbeom Park, Zhenling Peng, Sergey Ovchinnikov, David Baker Proceedings of the National Academy of Sciences Jan 2020, 117 (3) 1496-1503; DOI: 10.1073/pnas.1914677117;