Primary Information |
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| BoMiProt ID | Bomi9286 |
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| Protein Name | Sodium-dependent noradrenaline transporter/Norepinephrine transporter/NET/Solute carrier family 6 member 2 |
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| Organism | Bos taurus |
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| Uniprot ID | P51143 |
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| Milk Fraction | whey |
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| Ref Sequence ID | NP_777033.1 |
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| Aminoacid Length | 615 |
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| Molecular Weight | 68900 |
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| FASTA Sequence |
Download |
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| Gene Name | SLC6A2/NORADR |
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| Gene ID | 282363 |
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| Protein Existence Status | Reviewed |
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Secondary Information |
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| Protein Function | It is an amine transporter. It terminates the action of noradrenaline by its high affinity sodium-dependent reuptake into presynaptic terminals.It involves the coupling the influx of sodium and chloride (Na+/Cl−) with the transport of norepinephrine in a fixed ratio of 1:1:1. |
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| Biochemical Properties | 12 transmembrane domains(TMD).The sequence from bovine predicts a protein of 615 amino acids (M(r) 68,900). The bovine transporter shares 93% amino acid identity with the human sequence, but displays two more consensus sites for phosphorylation by protein kinase C.In comparisons with other members of the Na+/Cl- cotransporter gene family, the bovine NA transporter is most closely related to the bovine, human and rat dopamine transporters (about 65% homology).Bovine transporter also has three consensus glycosylation sites.The amino acid sequence of the bovine NA transporter indicates three potential intracellular protein kinase C phosphorylation sites, whereas the human transporter has only one. Two of these sites are located at the C-terminal end, and one within the loop connecting TM4 and TM5.Cultured bovine chromaffin cells exhibit a robust decrease in NA transport in response to intracellular increase in CAMP by cholera toxin treatment. |
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| PTMs | Phosphorylation,Glycosylation and Disulphide bond |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P51143|SC6A2_BOVIN Sodium-dependent noradrenaline transporter OS=Bos taurus OX=9913 GN=SLC6A2 PE=2 SV=1
MLLARMNPQVQPENGGAGPGSEQPPRKRKEVLVVKERNGVQCLLASRDGDEQPRETWGKK
IDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQYNRE
GAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFSSFTPTLPWTDCGHAWNS
PN*182CTDPKLLN*190SSVLGN*196HTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLI
IVVIVLFFSLWKGVKTSGKVVWITATLPYLVLFVLLVHGITLPGASNGINAYLHIDFYRL
KEATVWIDAATQIFFSLGAGFGVLIAFASYNKFDNNCYRDALLTSTINCVTSFISGFAIF
SILGYMAHEHKVNIEDVATEGAGLVFILYPEAISTLSGSTFWAIVFFIMLLALGIDSSMG
GMEAVITGLADDFQVLKRHRKLFTFAVSFGTFLLALFCITKGGIYVLTLLDTFAAGTSIL
FAVLMEAIGVSWFYGVDRFSNDIQQMMGFKPGLYWRLCWKFVSPAFLLFVVIVSIINFKP
LTYDDYIFPLWANWVGWGIAGSSMVLVPAYIVYKFFSTRGSIRERLAYGITPASEHHLVA
QRDIRQFQLQHWLAI |
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| Predicted Disorder Regions | 1-33, 46-54 |
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| DisProt Annotation | |
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| TM Helix Prediction | 12TMHs; (63-81), (93-115), (135-157), (233-251), (258-280), (306-328), (341-363), (393-415), (443-465), (474-496), (517-535),& (554-576) |
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| Significance of PTMs | Phosphorylation plays imp role in the regulation of transporter |
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| Bibliography | 1.Lingen B, Brüss M, Bönisch H. Cloning and expression of the bovine sodium- and chloride-dependent noradrenaline transporter. FEBS Lett. 1994 Apr 11;342(3):235-8. doi: 10.1016/0014-5793(94)80508-3. PMID: 8150077. 2.Jursky, F., Tamura, S., Tamura, A., Mandiyan, S., Nelson, H., & Nelson, N. (1994). Structure, function and brain localization of neurotransmitter transporters. The Journal of experimental biology, 196, 283–295. |
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