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| {{Short description|Class of transport proteins}} | |||
| ⚫ | The |
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| {{cs1 config|name-list-style=vanc|display-authors=6}} | |||
| {{Infobox protein family | |||
| | Symbol = AAAP | |||
| | Name = Amino Acid/Auxin Permease Family | |||
| | image = | |||
| | width = | |||
| | caption = | |||
| | Pfam = PF01490 | |||
| | Pfam_clan = CL0062 | |||
| | InterPro = IPR013057 | |||
| | SMART = | |||
| | PROSITE = | |||
| | MEROPS = | |||
| | SCOP = | |||
| | TCDB = 2.A.18 | |||
| | OPM family = | |||
| | OPM protein = | |||
| | CAZy = | |||
| | CDD = | |||
| }} | |||
| ⚫ | The '''Amino Acid/Auxin Permease (AAAP) Family''' () is a family of secondary carrier proteins, a member of the ] that includes hundreds of proteins from plants, animals, fungi and lower eukaryotes. Six AAAPs in '']'' are well characterized and transport neutral and charged amino acids with varying specificities and affinities.<ref name=Fischer2002>{{cite journal | vauthors = Fischer WN, Loo DD, Koch W, Ludewig U, Boorer KJ, Tegeder M, Rentsch D, Wright EM, Frommer WB | title = Low and high affinity amino acid H+-cotransporters for cellular import of neutral and charged amino acids | journal = The Plant Journal | volume = 29 | issue = 6 | pages = 717–731 | date = March 2002 | pmid = 12148530 | doi = 10.1046/j.1365-313x.2002.01248.x | doi-access = free }}</ref><ref name=TCDB>{{cite web| vauthors = Saier Jr MH |title=2.A.18 The Amino Acid/Auxin Permease (AAAP) Family|url=http://www.tcdb.org/search/result.php?tc=2.A.18|website=Transporter Classification Database|publisher=Saier Lab Bioinformatics Group}}</ref> | ||
| ==Function== | == Function == | ||
| Individual permeases of the AAAP family transport auxin (indole-3-acetic acid), a single amino acid or multiple amino acids. Some of these permeases exhibit very broad specificities transporting all twenty amino acids naturally found in proteins. Some also transport ]. All transport neutral amino acids and some acidic amino acids, always with just one proton. AAP3 and AAP5 are the only ones transporting basic amino acids, and only AAP6 transports aspartate <ref name=Fischer2002 />. <ref name=TCDB/> | |||
| ⚫ | Among animal AAAP family members are numerous growth regulating System A and System N isoforms, each exhibiting distinctive tissue and subcellular localizations. The different isoforms also exhibit different relative affinities for the amino acid substrates. Some catalyze H<sup>+</sup> antiport and can function bidirectionally. Since Systems A are ] which Systems N are not, the amino acid:cation ] may differ.<ref name=TCDB/><ref name=Chaudhry01>{{cite journal | vauthors = Chaudhry FA, Krizaj D, Larsson P, Reimer RJ, Wreden C, Storm-Mathisen J, Copenhagen D, Kavanaugh M, Edwards RH | title = Coupled and uncoupled proton movement by amino acid transport system N | journal = The EMBO Journal | volume = 20 | issue = 24 | pages = 7041–7051 | date = December 2001 | pmid = 11742981 | pmc = 125789 | doi = 10.1093/emboj/20.24.7041 }}</ref><ref name=Chaudhry02>{{cite journal | vauthors = Chaudhry FA, Schmitz D, Reimer RJ, Larsson P, Gray AT, Nicoll R, Kavanaugh M, Edwards RH | title = Glutamine uptake by neurons: interaction of protons with system a transporters | journal = The Journal of Neuroscience | volume = 22 | issue = 1 | pages = 62–72 | date = January 2002 | pmid = 11756489 | pmc = 6757603 | doi = 10.1523/JNEUROSCI.22-01-00062.2002 }}</ref><ref name=Varoqui>{{cite journal | vauthors = Varoqui H, Zhu H, Yao D, Ming H, Erickson JD | title = Cloning and functional identification of a neuronal glutamine transporter | journal = The Journal of Biological Chemistry | volume = 275 | issue = 6 | pages = 4049–4054 | date = February 2000 | pmid = 10660562 | doi = 10.1074/jbc.275.6.4049 | doi-access = free }}</ref> | ||
| ⚫ | == References == | ||
| ⚫ | Among animal AAAP family members are numerous growth regulating System A and System N isoforms, each exhibiting distinctive tissue and subcellular localizations. The different isoforms also exhibit different relative affinities for the amino acid substrates. Some catalyze H<sup>+</sup> antiport and can function bidirectionally. Since Systems A are electrogenic which Systems N are not, the amino acid:cation stoichiometries may differ <ref name=Chaudhry01>{{cite journal| |
||
| ⚫ | {{reflist}} | ||
| {{CCBYSASource|sourcepath=http://www.tcdb.org/search/result.php?tc=2.A.18|sourcearticle=The Amino Acid/Auxin Permease (AAAP) Family|revision=699866824}} | |||
| ] | |||
| Six auxin/amino acid permeases (AAAPs) from Arabidopsis mediate transport of a wide spectrum of amino acids <ref name=Fischer2002 />. AAAPs are distantly related to plasma membrane amino acid transport systems N and A and to vesicular transporters such as VGAT from mammals. Although capable of recognizing and transporting a wide spectrum of amino acids, individual AAAPs differ with respect to specificity. Apparent substrate affinities are influenced by structure and net charge and vary by three orders of magnitude <ref name=Fischer2002 />. AAAPs mediate cotransport of neutral amino acids with one proton, and uncharged forms of acidic and basic amino acids are cotransported with one proton. Since all AAAPs are differentially expressed, different tissues may be supplied with a different spectrum of amino acids. <ref name=TCDB/> | |||
| ] | |||
| ] | |||
| {{membrane-protein-stub}} | |||
| ==Transport Reaction== | |||
| The generalized transport reaction catalyzed by the proteins of the AAAP family is: <ref name=TCDB>{{cite web|last1=Saier|first1=MH Jr.|title=2.A.18 The Amino Acid/Auxin Permease (AAAP) Family|url=http://www.tcdb.org/search/result.php?tc=2.A.18|website=Transporter Classification Database|publisher=Saier Lab Bioinformatics Group}}</ref> | |||
| Substrate (out) + nH<sup>+</sup> (out) → Substrate (in) + nH<sup>+</sup> (in) | |||
| ==Structure== | |||
| AAAP family proteins, all from eukaryotes, vary from 376 to 713 amino acyl residues in length, but most are of 400-500 residues. Most of the size variation occurs as a result of the presence of long N-terminal hydrophilic extensions in some of the proteins. Some of the yeast proteins are particularly long. Variation in the loops and the C-termini also occurs. These proteins exhibit 11 (or 10) putative transmembrane α-helical spanners. One homologue, AAP1 of A. thaliana (), has 11 established TMSs <ref name=ChangBush>{{cite journal|last1=Chang|first1=HC|last2=Bush|first2=DR|title=Topology of NAT2, a prototypical example of a new family of amino acid transporters.|journal=Journal of Biological Chemistry|date=November 28, 2011|volume=272|issue=48|pages=30552-7|pmid=9374550}}</ref>. <ref name=TCDB/> | |||
| ⚫ | ==References== | ||
| ⚫ | {{reflist}} | ||
Latest revision as of 17:53, 8 May 2024
Class of transport proteinsProtein family
| Amino Acid/Auxin Permease Family | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | AAAP | ||||||||
| Pfam | PF01490 | ||||||||
| Pfam clan | CL0062 | ||||||||
| InterPro | IPR013057 | ||||||||
| TCDB | 2.A.18 | ||||||||
| |||||||||
The Amino Acid/Auxin Permease (AAAP) Family (TC# 2.A.18) is a family of secondary carrier proteins, a member of the APC Superfamily that includes hundreds of proteins from plants, animals, fungi and lower eukaryotes. Six AAAPs in A. thaliana are well characterized and transport neutral and charged amino acids with varying specificities and affinities.
Function
Among animal AAAP family members are numerous growth regulating System A and System N isoforms, each exhibiting distinctive tissue and subcellular localizations. The different isoforms also exhibit different relative affinities for the amino acid substrates. Some catalyze H antiport and can function bidirectionally. Since Systems A are electrogenic which Systems N are not, the amino acid:cation stoichiometries may differ.
References
- Fischer WN, Loo DD, Koch W, Ludewig U, Boorer KJ, Tegeder M, et al. (March 2002). "Low and high affinity amino acid H+-cotransporters for cellular import of neutral and charged amino acids". The Plant Journal. 29 (6): 717–731. doi:10.1046/j.1365-313x.2002.01248.x. PMID 12148530.
- ^ Saier Jr MH. "2.A.18 The Amino Acid/Auxin Permease (AAAP) Family". Transporter Classification Database. Saier Lab Bioinformatics Group.
- Chaudhry FA, Krizaj D, Larsson P, Reimer RJ, Wreden C, Storm-Mathisen J, et al. (December 2001). "Coupled and uncoupled proton movement by amino acid transport system N". The EMBO Journal. 20 (24): 7041–7051. doi:10.1093/emboj/20.24.7041. PMC 125789. PMID 11742981.
- Chaudhry FA, Schmitz D, Reimer RJ, Larsson P, Gray AT, Nicoll R, et al. (January 2002). "Glutamine uptake by neurons: interaction of protons with system a transporters". The Journal of Neuroscience. 22 (1): 62–72. doi:10.1523/JNEUROSCI.22-01-00062.2002. PMC 6757603. PMID 11756489.
- Varoqui H, Zhu H, Yao D, Ming H, Erickson JD (February 2000). "Cloning and functional identification of a neuronal glutamine transporter". The Journal of Biological Chemistry. 275 (6): 4049–4054. doi:10.1074/jbc.275.6.4049. PMID 10660562.
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