Search by BoMiProt ID - Bomi9286


Primary Information

BoMiProt ID Bomi9286
Protein Name Sodium-dependent noradrenaline transporter/Norepinephrine transporter/NET/Solute carrier family 6 member 2
Organism Bos taurus
Uniprot IdP51143
Milk Fractionwhey
Ref Sequence Id NP_777033.1
Aminoacid Length 615
Molecular Weight 68900
Fasta Sequence https://www.uniprot.org/uniprot/P51143.fasta
Gene Name SLC6A2/NORADR
Gene Id 282363
Protein Existence Status Reviewed

Secondary Information

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.
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.
PTMs Phosphorylation,Glycosylation and Disulphide bond
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
Predicted Disorder Regions 1-33, 46-54
DisProt Annotation
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)
Significance of PTMs Phosphorylation plays imp role in the regulation of transporter
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.