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9JCZ

Cryo-EM structure of human TauT in presence of taurine, determined in an inward-facing occluded conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0005283molecular_functionamino acid:sodium symporter activity
A0005332molecular_functiongamma-aminobutyric acid:sodium:chloride symporter activity
A0005368molecular_functiontaurine transmembrane transporter activity
A0005369molecular_functiontaurine:sodium symporter activity
A0005886cellular_componentplasma membrane
A0006836biological_processneurotransmitter transport
A0006865biological_processamino acid transport
A0015171molecular_functionamino acid transmembrane transporter activity
A0015185molecular_functiongamma-aminobutyric acid transmembrane transporter activity
A0015293molecular_functionsymporter activity
A0015734biological_processtaurine transmembrane transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0022858molecular_functionalanine transmembrane transporter activity
A0030425cellular_componentdendrite
A0031528cellular_componentmicrovillus membrane
A0032328biological_processalanine transport
A0035725biological_processsodium ion transmembrane transport
A0042995cellular_componentcell projection
A0043025cellular_componentneuronal cell body
A0045211cellular_componentpostsynaptic membrane
A0045597biological_processpositive regulation of cell differentiation
A0050804biological_processmodulation of chemical synaptic transmission
A0051939biological_processgamma-aminobutyric acid import
A0089718biological_processamino acid import across plasma membrane
A0098739biological_processimport across plasma membrane
A0098982cellular_componentGABA-ergic synapse
A0150104biological_processtransport across blood-brain barrier
Functional Information from PROSITE/UniProt
site_idPS00610
Number of Residues15
DetailsNA_NEUROTRAN_SYMP_1 Sodium:neurotransmitter symporter family signature 1. WRFPYlcykNGGGaF
ChainResidueDetails
ATRP65-PHE79

site_idPS00754
Number of Residues21
DetailsNA_NEUROTRAN_SYMP_2 Sodium:neurotransmitter symporter family signature 2. YLfqSFQkeLPWahCnhswNT
ChainResidueDetails
ATYR148-THR168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-ASP49

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
APHE50-LEU70

site_idSWS_FT_FI3
Number of Residues19
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
AALA78-LEU97

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
AGLY122-LEU142

site_idSWS_FT_FI5
Number of Residues74
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AALA143-LYS217

site_idSWS_FT_FI6
Number of Residues18
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
ATRP218-TRP236

site_idSWS_FT_FI7
Number of Residues17
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
AVAL245-VAL262

site_idSWS_FT_FI8
Number of Residues17
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
AILE298-TYR315

site_idSWS_FT_FI9
Number of Residues21
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
AMET327-LEU348

site_idSWS_FT_FI10
Number of Residues19
DetailsTRANSMEM: Helical; Name=8 => ECO:0000255
ChainResidueDetails
AMET381-LEU400

site_idSWS_FT_FI11
Number of Residues18
DetailsTRANSMEM: Helical; Name=9 => ECO:0000255
ChainResidueDetails
AILE430-THR448

site_idSWS_FT_FI12
Number of Residues20
DetailsTRANSMEM: Helical; Name=10 => ECO:0000255
ChainResidueDetails
AGLY465-GLY485

site_idSWS_FT_FI13
Number of Residues19
DetailsTRANSMEM: Helical; Name=11 => ECO:0000255
ChainResidueDetails
ATYR506-VAL525

site_idSWS_FT_FI14
Number of Residues18
DetailsTRANSMEM: Helical; Name=12 => ECO:0000255
ChainResidueDetails
ALEU545-ILE563

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q00589
ChainResidueDetails
ASER322

site_idSWS_FT_FI16
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN163
AASN179

site_idSWS_FT_FI17
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
AASN190

236620

PDB entries from 2025-05-28

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