ABC transporter transmembrane region | |||||||||
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Identifiers | |||||||||
Symbol | ABC_membrane | ||||||||
Pfam | PF00664 | ||||||||
InterPro | IPR011527 | ||||||||
PROSITE | PDOC00364 | ||||||||
SCOP2 | 1pf4 / SCOPe / SUPFAM | ||||||||
TCDB | 3.A.1 | ||||||||
OPM superfamily | 17 | ||||||||
OPM protein | 2hyd | ||||||||
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ABC transporter transmembrane domain is the main transmembrane structural unit of ATP-binding cassette transporter proteins, consisting of six alpha helixes that traverse the plasma membrane. Many members of the ABC transporter family (Pfam PF00005) have two such regions.
This family appears to correspond to ABC1 by TCDB classification.
Subfamilies
- Sulphate ABC transporter permease protein 2 InterPro: IPR005667
- Phosphate transport system permease protein 2 InterPro: IPR005672
- Phosphonate uptake transporter InterPro: IPR005769
- Nitrate transport permease InterPro: IPR005889
- NifC-like ABC-type porter InterPro: IPR006469
- Phosphate ABC transporter, permease protein PstC InterPro: IPR011864
- Molybdate ABC transporter, permease protein InterPro: IPR011867
- Nickel ABC transporter, permease subunit NikB InterPro: IPR014156
- Nickel ABC transporter, permease subunit NikC InterPro: IPR014157
- Ectoine/hydroxyectoine ABC transporter, permease protein EhuD InterPro: IPR014341
- Ectoine/hydroxyectoine ABC transporter, permease protein EhuC InterPro: IPR014342
Human proteins containing this domain
ABCB1; ABCB10; ABCB11; ABCB4; ABCB5; ABCB6; ABCB7; ABCB8; ABCB9; ABCC1; ABCC10; ABCC11; ABCC12; ABCC13; ABCC2; ABCC3; ABCC4; ABCC5; ABCC6; ABCC8; ABCC9; CFTR; TAP1; TAP2; TAPL;
References
- ^ Kerr ID (2002). "Structure and association of ATP-binding cassette transporter nucleotide-binding domains". Biochim. Biophys. Acta. 1561 (1): 47–64. doi:10.1016/s0304-4157(01)00008-9. PMID 11988180. S2CID 7058003.
- ^ Hunt JF, Yuan YR, Martsinkevich O, Millen L, Thomas PJ, Karpowich N, Dai PL, MacVey K (2001). "Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter". Structure. 9 (7): 571–86. doi:10.1016/S0969-2126(01)00617-7. PMID 11470432.
- ^ Hunt JF, Yuan YR, Blecker S, Martsinkevich O, Millen L, Thomas PJ (2001). "The crystal structure of the MJ0796ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter". J. Biol. Chem. 276 (34): 32313–21. doi:10.1074/jbc.M100758200. PMID 11402022.
- ^ Kim SH, Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF (1998). "Crystal structure of the ATP-binding subunit of an ABC transporter". Nature. 396 (6712): 703–707. Bibcode:1998Natur.396..703H. doi:10.1038/25393. PMID 9872322. S2CID 204996524.
- ^ Welte W, Breed J, Boos W, Diederichs K, Vonrhein C, Muller C, Diez J, Greller G, Schnell C (2000). "Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis". EMBO J. 19 (22): 5951–61. doi:10.1093/emboj/19.22.5951. PMC 305842. PMID 11080142.
- ^ Wiley DC, Gaudet R (2001). "Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing". EMBO J. 20 (17): 4964–72. doi:10.1093/emboj/20.17.4964. PMC 125601. PMID 11532960.