Search by BoMiProt ID - Bomi333

Primary Information

BoMiProt ID Bomi333
Protein Name Solute carrier family 29 (Nucleoside transporters), member 1
Organism Bos taurus
Uniprot IDQ3ZC83
Milk FractionMFGM, Exosome
Ref Sequence ID NP_001029570.2
Aminoacid Length 456
Molecular Weight 49882
FASTA Sequence Download
Gene Name SLC29A1
Gene ID 510932
Protein Existence Status Unreviewed: Experimental evidence at protein level

Secondary Information

Presence in other biological fluids/tissue/cells hENT1 protein expression is highest in the adrenal gland, ovary, stomach, duodenum, small intestine, and colon while mRNA was most abundant in the adrenal gland. hENT2 protein expression was highest across a broader range of tissue types including various neurological tissues, segments of the gastrointestinal tract, skin, placenta, parathyroid gland, appendix, testis, urinary bladder, heart muscle, nasopharynx, pancreas, and gallbladder with mRNA being most abundant in skeletal muscle. Protein expression of hENT3 predominates in cerebral cortex, lateral ventricle, ovary, adrenal gland, and testis with higher levels of mRNA expression in placenta, urinary bladder, and ovary
Protein Function facilitate cross-membrane transport of nucleosides and nucleoside-derived drugs; play an important role in the salvage pathways of nucleotide synthesis, cancer chemotherapy, and treatment for virus infections; polytopic integral membrane proteins that mediate the transport of nucleosides, nucleobases, and therapeutic analogs
Biochemical Properties As found in humans, competitively inhibited by nitrobenzylmercaptopurine ribonucleoside (NBMPR), nucleosides, deoxynucleosides, and nucleoside-derived anti-cancer and anti-viral drugs; human ENTs consist of 11 transmembrane segments (TMs), a cytoplasmic N-terminus and an extracellular C-terminus, a large extracellular loop between TM1 and TM2, and a large cytoplasmic loop between TM6 and TM7; calculated dissociation constant (Kd) between hENT1 and adenosine is approximately 0.45 ± 0.03 mmol/L; activity of the human ENT3 and ENT4 transporters have been shown to be stimulated at lower pH
Significance in milk nutrient transport systems for milk precursors and constituents
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Bibliography 1. Uhlen, M. et al. (2015) ‘Tissue-based map of the human proteome’, Science, 347(6220), pp. 1260419–1260419. doi: 10.1126/science.1260419.
2. Huang, W. et al. (2017) ‘Functional characterization of human equilibrative nucleoside transporter 1’, Protein & Cell, 8(4), pp. 284–295. doi: 10.1007/s13238-016-0350-x.