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6  structures 2482  species 0  interactions 7523  sequences 89  architectures

Family: ABC_membrane_2 (PF06472)

Summary: ABC transporter transmembrane region 2

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 "Transmembrane domain of ABC transporters". More...

Transmembrane domain of ABC transporters Edit Wikipedia article

ABC transporter transmembrane region
OPM superfamily18
OPM protein1pf4

ABC transporter transmembrane domain is main transmembrane structural unit of ABC transporters which consist of six transmembrane helixes. Many members of the ABC transporter family (Pfam PF00005) have two such regions.

Human proteins containing this domain



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.

ABC transporter transmembrane region 2 Provide feedback

This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with PF00664. Mutations in this domain in P28288 are believed responsible for Zellweger Syndrome-2 [1]; mutations in P33897 are responsible for recessive X-linked adrenoleukodystrophy [2]. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids [3].

Literature references

  1. Gartner J, Moser H, Valle D; , Nat Genet 1992;1:16-23.: Mutations in the 70K peroxisomal membrane protein gene in Zellweger syndrome. PUBMED:1301993 EPMC:1301993

  2. Mosser J, Douar AM, Sarde CO, Kioschis P, Feil R, Moser H, Poustka AM, Mandel JL, Aubourg P; , Nature 1993;361:726-730.: Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters. PUBMED:8441467 EPMC:8441467

  3. Hettema EH, van Roermund CW, Distel B, van den Berg M, Vilela C, Rodrigues-Pousada C, Wanders RJ, Tabak HF; , EMBO J 1996;15:3813-3822.: The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae. PUBMED:8670886 EPMC:8670886

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR011527

This entry represents the transmembrane domain in cases where the TMD and ABC region are found in the same protein, and corresponds to ABC type 1 from Transporter Classification Database (http://www.tcdb.org/tcdb/index.php?tc=3.A.1).

ABC transporters minimally contain two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). In certain bacterial transporters, these regions are found on different polypeptides. The function of the integral inner-membrane protein is to translocate the substrate across the membrane, as well as in substrate recognition [ PUBMED:9873074 , PUBMED:10529352 ].

ABC transporters belong to the ATP-Binding Cassette (ABC) superfamily, which uses the hydrolysis of ATP to energise diverse biological systems. ABC transporters minimally consist of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). These can be found on the same protein or on two different ones. Most ABC transporters function as a dimer and therefore are constituted of four domains, two ABC modules and two TMDs.

ABC transporters are involved in the export or import of a wide variety of substrates ranging from small ions to macromolecules. The major function of ABC import systems is to provide essential nutrients to bacteria. They are found only in prokaryotes and their four constitutive domains are usually encoded by independent polypeptides (two ABC proteins and two TMD proteins). Prokaryotic importers require additional extracytoplasmic binding proteins (one or more per systems) for function. In contrast, export systems are involved in the extrusion of noxious substances, the export of extracellular toxins and the targeting of membrane components. They are found in all living organisms and in general the TMD is fused to the ABC module in a variety of combinations. Some eukaryotic exporters encode the four domains on the same polypeptide chain [ PUBMED:9873074 ].

The ATP-Binding Cassette (ABC) superfamily forms one of the largest of all protein families with a diversity of physiological functions [ PUBMED:9873074 ]. Several studies have shown that there is a correlation between the functional characterisation and the phylogenetic classification of the ABC cassette [ PUBMED:9873074 , PUBMED:11421270 ]. More than 50 subfamilies have been described based on a phylogenetic and functional classification [ PUBMED:9873074 , PUBMED:11421269 , PUBMED:11421270 ]; (for further information see http://www.tcdb.org/tcdb/index.php?tc=3.A.1).

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 ABC_membrane (CL0241), which has the following description:

This clan includes families that are the membrane components of ABC transporter complexes. In general these regions are composed of six transmembrane helices [1].

The clan contains the following 4 members:

ABC_membrane ABC_membrane_2 ABC_membrane_3 SbmA_BacA


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.

Representative proteomes UniProt
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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.

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Representative proteomes UniProt

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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.

Representative proteomes UniProt
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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...


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: ADDA_6479
Previous IDs: Ald_N;
Type: Family
Sequence Ontology: SO:0100021
Author: Yeats C
Number in seed: 25
Number in full: 7523
Average length of the domain: 250 aa
Average identity of full alignment: 26 %
Average coverage of the sequence by the domain: 39.81 %

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 24.4 24.4
Trusted cut-off 24.4 24.4
Noise cut-off 24.3 24.2
Model length: 269
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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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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The tree shows the occurrence of this domain across different species. More...


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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 ABC_membrane_2 domain has been found. There are 6 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
A0A044STV0 View 3D Structure Click here
A0A044TS98 View 3D Structure Click here
A0A044U356 View 3D Structure Click here
A0A077ZB97 View 3D Structure Click here
A0A0D2DUY1 View 3D Structure Click here
A0A0D2GF48 View 3D Structure Click here
A0A0K0DSK3 View 3D Structure Click here
A0A0K0E0Q3 View 3D Structure Click here
A0A0K0E1Y7 View 3D Structure Click here
A0A0K0E2F0 View 3D Structure Click here
A0A0K0E2F1 View 3D Structure Click here
A0A0K0EFB9 View 3D Structure Click here
A0A0K0EM28 View 3D Structure Click here
A0A0K0ETP1 View 3D Structure Click here
A0A0N4U174 View 3D Structure Click here
A0A0N4UDG0 View 3D Structure Click here
A0A0R0HLA9 View 3D Structure Click here
A0A0R0IR91 View 3D Structure Click here
A0A0R4IRL4 View 3D Structure Click here
A0A175WGW3 View 3D Structure Click here
A0A175WH80 View 3D Structure Click here
A0A1C1CJG8 View 3D Structure Click here
A0A1C1CP94 View 3D Structure Click here
A0A1D6FW36 View 3D Structure Click here
A0A1D6N0G6 View 3D Structure Click here
A0A1D8PFB0 View 3D Structure Click here
A0A1D8PRN3 View 3D Structure Click here
A0A3P7DYE3 View 3D Structure Click here
A0A3P7DZP9 View 3D Structure Click here
A0A3P7E0I2 View 3D Structure Click here
A0A3P7E0U5 View 3D Structure Click here
A0A3P7E2G1 View 3D Structure Click here
A0A3P7EM13 View 3D Structure Click here
A0A5S6PF30 View 3D Structure Click here
A4I2N3 View 3D Structure Click here
A4I6L1 View 3D Structure Click here
A4I948 View 3D Structure Click here
B0UY91 View 3D Structure Click here
C0NCD1 View 3D Structure Click here
C0NRD4 View 3D Structure Click here