Q99884 · SC6A7_HUMAN
- ProteinSodium-dependent proline transporter
- GeneSLC6A7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids636 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Brain specific sodium (and chloride)-dependent proline transporter (PubMed:7651355).
Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals (Probable)
Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals (Probable)
Catalytic activity
- chloride(out) + L-proline(out) + 2 Na+(out) = chloride(in) + L-proline(in) + 2 Na+(in)chloride (out)CHEBI:17996
+ L-proline (out)CHEBI:60039+ 2 Na+ (out)CHEBI:29101= chloride (in)CHEBI:17996+ L-proline (in)CHEBI:60039+ 2 Na+ (in)CHEBI:29101 - chloride(out) + L-pipecolate(out) + 2 Na+(out) = chloride(in) + L-pipecolate(in) + 2 Na+(in)
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
6.2 μM | L-proline |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Cellular Component | synapse | |
Cellular Component | synaptic membrane | |
Molecular Function | L-proline transmembrane transporter activity | |
Molecular Function | proline:sodium symporter activity | |
Biological Process | amino acid import across plasma membrane | |
Biological Process | neurotransmitter transport | |
Biological Process | proline transport | |
Biological Process | protein catabolic process | |
Biological Process | sodium ion transmembrane transport |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSodium-dependent proline transporter
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ99884
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Synaptic cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-45 | Cytoplasmic | ||||
Sequence: MKKLQGAHLRKPVTPDLLMTPSDQGDVDLDVDFAAHRGNWTGKLD | ||||||
Transmembrane | 46-66 | Helical; Name=1 | ||||
Sequence: FLLSCIGYCVGLGNVWRFPYR | ||||||
Transmembrane | 74-93 | Helical; Name=2 | ||||
Sequence: AFLVPYFLMLAICGIPLFFL | ||||||
Transmembrane | 117-137 | Helical; Name=3 | ||||
Sequence: GAGAAMLLIVGLVAIYYNMII | ||||||
Topological domain | 138-214 | Extracellular | ||||
Sequence: AYVLFYLFASLTSDLPWEHCGNWWNTELCLEHRVSKDGNGALPLNLTCTVSPSEEYWSRYVLHIQGSQGIGSPGEIR | ||||||
Transmembrane | 215-233 | Helical; Name=4 | ||||
Sequence: WNLCLCLLLAWVIVFLCIL | ||||||
Transmembrane | 242-259 | Helical; Name=5 | ||||
Sequence: VVYFTATFPYLILLMLLV | ||||||
Transmembrane | 295-312 | Helical; Name=6 | ||||
Sequence: IFYSLGVGFGGLLTFASY | ||||||
Transmembrane | 324-345 | Helical; Name=7 | ||||
Sequence: FIVTLGNAITSILAGFAIFSVL | ||||||
Transmembrane | 378-397 | Helical; Name=8 | ||||
Sequence: LPLSPFWSFLFFFMLLTLGL | ||||||
Transmembrane | 425-443 | Helical; Name=9 | ||||
Sequence: VFSGLICVAMYLMGLILTT | ||||||
Transmembrane | 459-479 | Helical; Name=10 | ||||
Sequence: SFGLMVVVITTCLAVTRVYGI | ||||||
Transmembrane | 500-519 | Helical; Name=11 | ||||
Sequence: ACWLFLSPATLLALMVYSIV | ||||||
Transmembrane | 538-556 | Helical; Name=12 | ||||
Sequence: LGILMGLLSCLMIPAGMLV | ||||||
Topological domain | 557-636 | Cytoplasmic | ||||
Sequence: AVLREEGSLWERLQQASRPAMDWGPSLEENRTGMYVATLAGSQSPKPLMVHMRKYGGITSFENTAIEVDREIAEEEESMM |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_011390 | 345 | in dbSNP:rs1468564 | |||
Sequence: L → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 744 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000214770 | 1-636 | UniProt | Sodium-dependent proline transporter | |||
Sequence: MKKLQGAHLRKPVTPDLLMTPSDQGDVDLDVDFAAHRGNWTGKLDFLLSCIGYCVGLGNVWRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGAAMLLIVGLVAIYYNMIIAYVLFYLFASLTSDLPWEHCGNWWNTELCLEHRVSKDGNGALPLNLTCTVSPSEEYWSRYVLHIQGSQGIGSPGEIRWNLCLCLLLAWVIVFLCILKGVKSSGKVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLGVGFGGLLTFASYNTFHQNIYRDTFIVTLGNAITSILAGFAIFSVLGYMSQELGVPVDQVAKAGPGLAFVVYPQAMTMLPLSPFWSFLFFFMLLTLGLDSQFAFLETIVTAVTDEFPYYLRPKKAVFSGLICVAMYLMGLILTTDGGMYWLVLLDDYSASFGLMVVVITTCLAVTRVYGIQRFCRDIHMMLGFKPGLYFRACWLFLSPATLLALMVYSIVKYQPSEYGSYRFPPWAELLGILMGLLSCLMIPAGMLVAVLREEGSLWERLQQASRPAMDWGPSLEENRTGMYVATLAGSQSPKPLMVHMRKYGGITSFENTAIEVDREIAEEEESMM | |||||||
Modified residue | 20 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 22 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 182 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 573 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 582 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 588 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 591 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 598 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 600 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 600 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Brain specific (at protein level) (PubMed:7651355).
Highly expressed in hippocampus, corpus striatum and temporal cortex. Also expressed in frontal cortex, occipital cortex and, at lower levels, in cerebellum and parietal cortex (at protein level) (PubMed:7651355).
Highly expressed in hippocampus, corpus striatum and temporal cortex. Also expressed in frontal cortex, occipital cortex and, at lower levels, in cerebellum and parietal cortex (at protein level) (PubMed:7651355).
Gene expression databases
Organism-specific databases
Structure
Sequence
- Sequence statusComplete
- Length636
- Mass (Da)70,911
- Last updated2010-05-18 v2
- Checksum9B9D10C1F49E409B
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E5RJL1 | E5RJL1_HUMAN | SLC6A7 | 666 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 514 | in Ref. 1; AAB47007 and 3; AAH69631/AAH93785/AAI13426 | ||||
Sequence: M → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S80071 EMBL· GenBank· DDBJ | AAB47007.2 EMBL· GenBank· DDBJ | mRNA | ||
AC005895 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC069631 EMBL· GenBank· DDBJ | AAH69631.1 EMBL· GenBank· DDBJ | mRNA | ||
BC093785 EMBL· GenBank· DDBJ | AAH93785.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113425 EMBL· GenBank· DDBJ | AAI13426.1 EMBL· GenBank· DDBJ | mRNA |