Q28620 · NPT2A_RABIT
- ProteinSodium-dependent phosphate transport protein 2A
- GeneSLC34A1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids642 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Involved in actively transporting phosphate into cells via Na+ cotransport in the renal brush border membrane (PubMed:7733319).
The cotransport has a Na+:Pi stoichiometry of 3:1 and is electrogenic (By similarity).
The cotransport has a Na+:Pi stoichiometry of 3:1 and is electrogenic (By similarity).
Catalytic activity
- 3 Na+(out) + phosphate(out) = 3 Na+(in) + phosphate(in)This reaction proceeds in the forward direction.
3 Na+ (out)CHEBI:29101+ phosphate (out)CHEBI:43474= 3 Na+ (in)CHEBI:29101+ phosphate (in)CHEBI:43474
Activity regulation
Transport activity is significantly increased in response to dietary phosphate deprivation.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | brush border | |
Cellular Component | plasma membrane | |
Cellular Component | vesicle | |
Molecular Function | sodium:phosphate symporter activity | |
Biological Process | cellular response to phosphate starvation | |
Biological Process | intracellular phosphate ion homeostasis | |
Biological Process | phosphate ion homeostasis | |
Biological Process | phosphate ion transport | |
Biological Process | sodium-dependent phosphate transport |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameSodium-dependent phosphate transport protein 2A
- Short namesSodium-phosphate transport protein 2A
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionQ28620
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Apical cell membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Note: Localized at the brush border membranes of the proximal tubules. Internalized from the cell surface upon PTH stimulation.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-106 | Cytoplasmic | ||||
Sequence: MISYGEQLSSPAVSPPLVRAGLRGPMMHGATFAYVPSPQALHRIPGTSAYAFPSLSPVALTEHGCPYGEARERHEPLPAKLALEEEQKPESGWAQELRRTAMTLLK | ||||||
Transmembrane | 107-128 | Helical; Name=M1 | ||||
Sequence: LPLMVTFLYLFVCSLDVLSSAF | ||||||
Topological domain | 129-148 | Extracellular | ||||
Sequence: QLAGGKVAGDIFKDNAILAN | ||||||
Transmembrane | 149-166 | Helical; Name=M2 | ||||
Sequence: PVAGLVVGILVTVLVQSS | ||||||
Topological domain | 167-168 | Cytoplasmic | ||||
Sequence: ST | ||||||
Transmembrane | 169-188 | Helical; Name=M3 | ||||
Sequence: ATSIIVSMVSSGLLEVSSAI | ||||||
Topological domain | 189-350 | Extracellular | ||||
Sequence: PIIMGSNIGTSVTNTIVALMQAGDRTDFRRAFAGATVHDCFNWLSVLVLLPLEAATGYLHHVTGLVVASFNIRGGRDAPDLLKTITEPFTKLIIQLDRSVITSIATGDESLRNHSLIRIWCHRDPVEASTSMARAETNISRTHGNATMEKCNHIFVDTQLPD | ||||||
Transmembrane | 351-373 | Helical; Name=M4 | ||||
Sequence: LAVGLILLAGSLVLLCTCLILLV | ||||||
Topological domain | 374-415 | Cytoplasmic | ||||
Sequence: KMLNSLLKGQVAKVIQKVINTDLPAPFTWVTGYFAMVVGAAM | ||||||
Transmembrane | 416-439 | Helical; Name=M5 | ||||
Sequence: TFIVQSSSVFTSAITPLVGLGVIS | ||||||
Topological domain | 440-469 | Extracellular | ||||
Sequence: IERAYPLTLGSNIGTTTTAILAALASPREK | ||||||
Transmembrane | 470-490 | Helical; Name=M6 | ||||
Sequence: LSSSFQIALCHFFFNISGILL | ||||||
Topological domain | 491-516 | Cytoplasmic | ||||
Sequence: WYPLPCTRLPIRMAKALGKRTAKYRW | ||||||
Transmembrane | 517-537 | Helical; Name=M7 | ||||
Sequence: FAVLYLLVCFLLLPSLVFGIS | ||||||
Topological domain | 538-542 | Extracellular | ||||
Sequence: MAGWR | ||||||
Transmembrane | 543-564 | Helical; Name=M8 | ||||
Sequence: AMVGVGAPFGALLAFVVLINVL | ||||||
Topological domain | 565-642 | Cytoplasmic | ||||
Sequence: QSRSPGRLPKWLQTWDFLPHWMHSLQPLDHLITHATLCCSRSEPRSPQLPARVFLEELPPATPSPRLALPAHHNATRL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000068609 | 1-642 | Sodium-dependent phosphate transport protein 2A | |||
Sequence: MISYGEQLSSPAVSPPLVRAGLRGPMMHGATFAYVPSPQALHRIPGTSAYAFPSLSPVALTEHGCPYGEARERHEPLPAKLALEEEQKPESGWAQELRRTAMTLLKLPLMVTFLYLFVCSLDVLSSAFQLAGGKVAGDIFKDNAILANPVAGLVVGILVTVLVQSSSTATSIIVSMVSSGLLEVSSAIPIIMGSNIGTSVTNTIVALMQAGDRTDFRRAFAGATVHDCFNWLSVLVLLPLEAATGYLHHVTGLVVASFNIRGGRDAPDLLKTITEPFTKLIIQLDRSVITSIATGDESLRNHSLIRIWCHRDPVEASTSMARAETNISRTHGNATMEKCNHIFVDTQLPDLAVGLILLAGSLVLLCTCLILLVKMLNSLLKGQVAKVIQKVINTDLPAPFTWVTGYFAMVVGAAMTFIVQSSSVFTSAITPLVGLGVISIERAYPLTLGSNIGTTTTAILAALASPREKLSSSFQIALCHFFFNISGILLWYPLPCTRLPIRMAKALGKRTAKYRWFAVLYLLVCFLLLPSLVFGISMAGWRAMVGVGAPFGALLAFVVLINVLQSRSPGRLPKWLQTWDFLPHWMHSLQPLDHLITHATLCCSRSEPRSPQLPARVFLEELPPATPSPRLALPAHHNATRL | ||||||
Modified residue | 14 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 37 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 228↔525 | |||||
Sequence: CFNWLSVLVLLPLEAATGYLHHVTGLVVASFNIRGGRDAPDLLKTITEPFTKLIIQLDRSVITSIATGDESLRNHSLIRIWCHRDPVEASTSMARAETNISRTHGNATMEKCNHIFVDTQLPDLAVGLILLAGSLVLLCTCLILLVKMLNSLLKGQVAKVIQKVINTDLPAPFTWVTGYFAMVVGAAMTFIVQSSSVFTSAITPLVGLGVISIERAYPLTLGSNIGTTTTAILAALASPREKLSSSFQIALCHFFFNISGILLWYPLPCTRLPIRMAKALGKRTAKYRWFAVLYLLVC | ||||||
Glycosylation | 301 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 309↔339 | |||||
Sequence: CHRDPVEASTSMARAETNISRTHGNATMEKC | ||||||
Glycosylation | 326 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 333 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 511 | Phosphothreonine; by PKC | ||||
Sequence: T | ||||||
Modified residue | 610 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 626 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 628 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the kidney cortex.
Induction
Up-regulated by a low-phosphate diet.
Gene expression databases
Interaction
Subunit
Interacts via its C-terminal region with NHERF4. Interacts with NHERF1. Interacts with TMEM174; regulates SLC34A1 internalization by PTH and FGF23 (By similarity).
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length642
- Mass (Da)69,432
- Last updated1997-11-01 v1
- ChecksumA48B85C001642A8B
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5F9DM94 | A0A5F9DM94_RABIT | SLC34A1 | 635 | ||
A0A5F9D7V8 | A0A5F9D7V8_RABIT | SLC34A1 | 671 | ||
A0A5F9CT06 | A0A5F9CT06_RABIT | SLC34A1 | 342 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U20793 EMBL· GenBank· DDBJ | AAA77682.1 EMBL· GenBank· DDBJ | mRNA |