Auxin binding protein
| Auxin binding protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of auxin-binding protein 1 in complex with 1-naphthalene acetic acid | |||||||||
| Identifiers | |||||||||
| Symbol | Auxin_BP | ||||||||
| Pfam | PF02041 | ||||||||
| Pfam clan | CL0029 | ||||||||
| InterPro | IPR000526 | ||||||||
| SCOP | 1lr5 | ||||||||
| SUPERFAMILY | 1lr5 | ||||||||
| |||||||||
In molecular biology, the auxin binding protein family is a family of proteins which bind auxin.[1] They are located in the lumen of the endoplasmic reticulum (ER). The primary structure of these proteins contains an N-terminal hydrophobic leader sequence of 30-40 amino acids, which could represent a signal for translocation of the protein to the ER.[2][3] The mature protein comprises around 165 residues, and contains a number of potential N-glycosylation sites. In vitro transport studies have demonstrated co-translational glycosylation.[3] Retention within the lumen of the ER correlates with an additional signal located at the C terminus, represented by the sequence Lys-Asp-Glu-Leu, known to be responsible for preventing secretion of proteins from the lumen of the ER in eukaryotic cells.[2][3]
References
- ↑ Woo EJ, Marshall J, Bauly J, Chen JG, Venis M, Napier RM; et al. (2002). "Crystal structure of auxin-binding protein 1 in complex with auxin.". EMBO J 21 (12): 2877–85. doi:10.1093/emboj/cdf291. PMC 126050. PMID 12065401.
- 1 2 Hesse T, Feldwisch J, Balshusemann D, Bauw G, Puype M, Vandekerckhove J, Lobler M, Klambt D, Schell J, Palme K (September 1989). "Molecular cloning and structural analysis of a gene from Zea mays (L.) coding for a putative receptor for the plant hormone auxin". EMBO J. 8 (9): 2453–61. PMC 401229. PMID 2555179.
- 1 2 3 Palme K, Hesse T, Campos N, Garbers C, Yanofsky MF, Schell J (February 1992). "Molecular analysis of an auxin binding protein gene located on chromosome 4 of Arabidopsis". Plant Cell 4 (2): 193–201. doi:10.1105/tpc.4.2.193. PMC 160120. PMID 1321684.
This article incorporates text from the public domain Pfam and InterPro IPR000526