Q9Y6M7 · S4A7_HUMAN
- ProteinSodium bicarbonate cotransporter 3
- GeneSLC4A7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1214 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mediates the sodium-dependent bicarbonate transport important for pH recovery after acid load as well as for regulation of steady-state pH in the duodenum and vascular smooth muscle cells (By similarity).
Plays a key role in macrophage acidification, mediating bicarbonate import into the cytoplasm which is crucial for net acid extrusion and maintenance of cytoplasmic pH during phagocytosis (PubMed:29779931).
Provides cellular bicarbonate for de novo purine and pyrimidine synthesis and is a key mediator of de novo nucleotide synthesis downstream of mTORC1 signaling in proliferating cells (PubMed:35772404).
Isoform 6
Catalytic activity
- hydrogencarbonate(in) + Na+(in) = hydrogencarbonate(out) + Na+(out)hydrogencarbonate (in)CHEBI:17544
+ Na+ (in)CHEBI:29101= hydrogencarbonate (out)CHEBI:17544+ Na+ (out)CHEBI:29101 Isoform 6
hydrogencarbonate(in) + Na+(in) = hydrogencarbonate(out) + Na+(out)hydrogencarbonate (in)CHEBI:17544+ Na+ (in)CHEBI:29101= hydrogencarbonate (out)CHEBI:17544+ Na+ (out)CHEBI:29101
Activity regulation
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
24 mM | external sodium |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | basolateral plasma membrane | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Cellular Component | stereocilium | |
Molecular Function | monoatomic anion transmembrane transporter activity | |
Molecular Function | sodium:bicarbonate symporter activity | |
Molecular Function | solute:inorganic anion antiporter activity | |
Biological Process | auditory receptor cell development | |
Biological Process | bicarbonate transport | |
Biological Process | cellular response to growth factor stimulus | |
Biological Process | phagosome acidification | |
Biological Process | purine nucleotide biosynthetic process | |
Biological Process | pyrimidine nucleotide biosynthetic process | |
Biological Process | regulation of intracellular pH | |
Biological Process | transmembrane transport |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSodium bicarbonate cotransporter 3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y6M7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 6
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-608 | Extracellular | ||||
Sequence: MERFRLEKKLPGPDEEAVVDLGKTSSTVNTKFEKEELESHRAVYIGVHVPFSKESRRRHRHRGHKHHHRRRKDKESDKEDGRESPSYDTPSQRVQFILGTEDDDEEHIPHDLFTEMDELCYRDGEEYEWKETARWLKFEEDVEDGGDRWSKPYVATLSLHSLFELRSCILNGTVMLDMRASTLDEIADMVLDNMIASGQLDESIRENVREALLKRHHHQNEKRFTSRIPLVRSFADIGKKHSDPHLLERNGEGLSASRHSLRTGLSASNLSLRGESPLSLLLGHLLPSSRAGTPAGSRCTTPVPTPQNSPPSSPSISRLTSRSSQESQRQAPELLVSPASDDIPTVVIHPPEEDLEAALKGEEQKNEENVDLTPGILASPQSAPGNLDNSKSGEIKGNGSGGSRENSTVDFSKVDMNFMRKIPTGAEASNVLVGEVDFLERPIIAFVRLAPAVLLTGLTEVPVPTRFLFLLLGPAGKAPQYHEIGRSIATLMTDEIFHDVAYKAKDRNDLLSGIDEFLDQVTVLPPGEWDPSIRIEPPKSVPSQEKRKIPVFHNGSTPTLGETPKEAAHHAGPELQRTGRLFGGLILDIKRKAPFFLSDFKDALSLQC | ||||||
Transmembrane | 609-629 | Helical | ||||
Sequence: LASILFLYCACMSPVITFGGL | ||||||
Topological domain | 630-637 | Cytoplasmic | ||||
Sequence: LGEATEGR | ||||||
Transmembrane | 638-658 | Helical | ||||
Sequence: ISAIESLFGASLTGIAYSLFA | ||||||
Topological domain | 659-695 | Extracellular | ||||
Sequence: GQPLTILGSTGPVLVFEKILYKFCRDYQLSYLSLRTS | ||||||
Transmembrane | 696-716 | Helical | ||||
Sequence: IGLWTSFLCIVLVATDASSLV | ||||||
Topological domain | 717-725 | Cytoplasmic | ||||
Sequence: CYITRFTEE | ||||||
Transmembrane | 726-746 | Helical | ||||
Sequence: AFAALICIIFIYEALEKLFDL | ||||||
Topological domain | 747-817 | Extracellular | ||||
Sequence: GETYAFNMHNNLDKLTSYSCVCTEPPNPSNETLAQWKKDNITAHNISWRNLTVSECKKLRGVFLGSACGHH | ||||||
Transmembrane | 818-838 | Helical | ||||
Sequence: GPYIPDVLFWCVILFFTTFFL | ||||||
Topological domain | 839-861 | Cytoplasmic | ||||
Sequence: SSFLKQFKTKRYFPTKVRSTISD | ||||||
Transmembrane | 862-882 | Helical | ||||
Sequence: FAVFLTIVIMVTIDYLVGVPS | ||||||
Topological domain | 883-908 | Extracellular | ||||
Sequence: PKLHVPEKFEPTHPERGWIISPLGDN | ||||||
Transmembrane | 909-929 | Helical | ||||
Sequence: PWWTLLIAAIPALLCTILIFM | ||||||
Topological domain | 930-954 | Cytoplasmic | ||||
Sequence: DQQITAVIINRKEHKLKKGAGYHLD | ||||||
Transmembrane | 955-975 | Helical | ||||
Sequence: LLMVGVMLGVCSVMGLPWFVA | ||||||
Topological domain | 976-1011 | Extracellular | ||||
Sequence: ATVLSISHVNSLKVESECSAPGEQPKFLGIREQRVT | ||||||
Transmembrane | 1012-1032 | Helical | ||||
Sequence: GLMIFILMGLSVFMTSVLKFI | ||||||
Topological domain | 1033-1034 | Cytoplasmic | ||||
Sequence: PM | ||||||
Transmembrane | 1035-1055 | Helical | ||||
Sequence: PVLYGVFLYMGVSSLKGIQLF | ||||||
Topological domain | 1056-1092 | Extracellular | ||||
Sequence: DRIKLFGMPAKHQPDLIYLRYVPLWKVHIFTVIQLTC | ||||||
Transmembrane | 1093-1113 | Helical | ||||
Sequence: LVLLWVIKVSAAAVVFPMMVL | ||||||
Topological domain | 1114-1214 | Cytoplasmic | ||||
Sequence: ALVFVRKLMDLCFTKRELSWLDDLMPESKKKKEDDKKKKEKEEAERMLQDDDDTVHLPFEGGSLLQIPVKALKYSPDKPVSVKISFEDEPRKKYVDAETSL |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_055317 | 326 | in dbSNP:rs3755652 | |||
Sequence: E → K | ||||||
Mutagenesis | 549 | In isoform Q9Y6M7-6; No effect on cell membrane localization. Unable to rescue phagocyte deficient acidification phenotype of SLC4A7 knockout. | ||||
Sequence: T → I | ||||||
Mutagenesis | 811 | In isoform Q9Y6M7-6; No effect on cell membrane localization. Unable to rescue phagocyte deficient acidification phenotype of SLC4A7 knockout. | ||||
Sequence: D → A | ||||||
Mutagenesis | 1008-1131 | In isoform Q9Y6M7-6; Loss of cell membrane localization. Unable to rescue phagocyte deficient acidification phenotype of SLC4A7 knockout. | ||||
Sequence: Missing | ||||||
Mutagenesis | 1127-1214 | Loss of cell membrane localization. Significant reduction in transport activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 1135-1136 | Loss of interaction with CA2. Loss of regulation by CA2. | ||||
Sequence: DD → NN | ||||||
Mutagenesis | 1163-1165 | No effect on interaction with CA2. No effect on regulation by CA2. | ||||
Sequence: DDD → NNN | ||||||
Mutagenesis | 1214 | Loss of interaction with ATP6V1B1. | ||||
Sequence: L → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,362 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 (large scale data), modified residue, glycosylation, disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000079233 | 1-1214 | UniProt | Sodium bicarbonate cotransporter 3 | |||
Sequence: MERFRLEKKLPGPDEEAVVDLGKTSSTVNTKFEKEELESHRAVYIGVHVPFSKESRRRHRHRGHKHHHRRRKDKESDKEDGRESPSYDTPSQRVQFILGTEDDDEEHIPHDLFTEMDELCYRDGEEYEWKETARWLKFEEDVEDGGDRWSKPYVATLSLHSLFELRSCILNGTVMLDMRASTLDEIADMVLDNMIASGQLDESIRENVREALLKRHHHQNEKRFTSRIPLVRSFADIGKKHSDPHLLERNGEGLSASRHSLRTGLSASNLSLRGESPLSLLLGHLLPSSRAGTPAGSRCTTPVPTPQNSPPSSPSISRLTSRSSQESQRQAPELLVSPASDDIPTVVIHPPEEDLEAALKGEEQKNEENVDLTPGILASPQSAPGNLDNSKSGEIKGNGSGGSRENSTVDFSKVDMNFMRKIPTGAEASNVLVGEVDFLERPIIAFVRLAPAVLLTGLTEVPVPTRFLFLLLGPAGKAPQYHEIGRSIATLMTDEIFHDVAYKAKDRNDLLSGIDEFLDQVTVLPPGEWDPSIRIEPPKSVPSQEKRKIPVFHNGSTPTLGETPKEAAHHAGPELQRTGRLFGGLILDIKRKAPFFLSDFKDALSLQCLASILFLYCACMSPVITFGGLLGEATEGRISAIESLFGASLTGIAYSLFAGQPLTILGSTGPVLVFEKILYKFCRDYQLSYLSLRTSIGLWTSFLCIVLVATDASSLVCYITRFTEEAFAALICIIFIYEALEKLFDLGETYAFNMHNNLDKLTSYSCVCTEPPNPSNETLAQWKKDNITAHNISWRNLTVSECKKLRGVFLGSACGHHGPYIPDVLFWCVILFFTTFFLSSFLKQFKTKRYFPTKVRSTISDFAVFLTIVIMVTIDYLVGVPSPKLHVPEKFEPTHPERGWIISPLGDNPWWTLLIAAIPALLCTILIFMDQQITAVIINRKEHKLKKGAGYHLDLLMVGVMLGVCSVMGLPWFVAATVLSISHVNSLKVESECSAPGEQPKFLGIREQRVTGLMIFILMGLSVFMTSVLKFIPMPVLYGVFLYMGVSSLKGIQLFDRIKLFGMPAKHQPDLIYLRYVPLWKVHIFTVIQLTCLVLLWVIKVSAAAVVFPMMVLALVFVRKLMDLCFTKRELSWLDDLMPESKKKKEDDKKKKEKEEAERMLQDDDDTVHLPFEGGSLLQIPVKALKYSPDKPVSVKISFEDEPRKKYVDAETSL | |||||||
Modified residue (large scale data) | 26 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 52 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 55 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 76 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 84 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 87 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 89 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 150 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 150 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 165 | UniProt | In isoform Q9Y6M7-3; Phosphoserine | ||||
Sequence: L | |||||||
Modified residue | 165 | UniProt | In isoform Q9Y6M7-4; Phosphoserine | ||||
Sequence: L | |||||||
Modified residue | 168 | UniProt | In isoform Q9Y6M7-3; Phosphoserine | ||||
Sequence: C | |||||||
Modified residue | 168 | UniProt | In isoform Q9Y6M7-4; Phosphoserine | ||||
Sequence: C | |||||||
Glycosylation | 171 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 233 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 233 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 242 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 242 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 255 | UniProt | In isoform Q9Y6M7-2; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 258 | UniProt | In isoform Q9Y6M7-2; Phosphoserine | ||||
Sequence: R | |||||||
Modified residue | 260 | UniProt | In isoform Q9Y6M7-6; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 260 | UniProt | In isoform Q9Y6M7-9; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 260 | UniProt | In isoform Q9Y6M7-11; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 263 | UniProt | In isoform Q9Y6M7-6; Phosphoserine | ||||
Sequence: T | |||||||
Modified residue | 263 | UniProt | In isoform Q9Y6M7-9; Phosphoserine | ||||
Sequence: T | |||||||
Modified residue | 263 | UniProt | In isoform Q9Y6M7-11; Phosphoserine | ||||
Sequence: T | |||||||
Modified residue | 264 | UniProt | In isoform Q9Y6M7-13; Phosphoserine | ||||
Sequence: G | |||||||
Modified residue | 264 | UniProt | In isoform Q9Y6M7-14; Phosphoserine | ||||
Sequence: G | |||||||
Modified residue | 267 | UniProt | In isoform Q9Y6M7-13; Phosphoserine | ||||
Sequence: A | |||||||
Modified residue | 267 | UniProt | In isoform Q9Y6M7-14; Phosphoserine | ||||
Sequence: A | |||||||
Glycosylation | 269 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 382 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 398 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 400 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 400 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 403 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 403 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 406 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 407 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 407 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 408 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 556 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 556 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 557 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 557 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 559 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 563 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 742 | UniProt | In isoform Q9Y6M7-5; Phosphoserine | ||||
Sequence: K | |||||||
Disulfide bond | 766↔768 | UniProt | |||||
Sequence: CVC | |||||||
Modified residue | 771 | UniProt | In isoform Q9Y6M7-5; Phosphoserine | ||||
Sequence: P | |||||||
Modified residue | 774 | UniProt | In isoform Q9Y6M7-5; Phosphoserine | ||||
Sequence: P | |||||||
Glycosylation | 776 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 780 | UniProt | In isoform Q9Y6M7-5; Phosphoserine | ||||
Sequence: A | |||||||
Glycosylation | 786 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 791 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 802↔814 | UniProt | |||||
Sequence: CKKLRGVFLGSAC | |||||||
Modified residue | 1007 | UniProt | In isoform Q9Y6M7-3; Phosphoserine | ||||
Sequence: E | |||||||
Modified residue | 1010 | UniProt | In isoform Q9Y6M7-3; Phosphoserine | ||||
Sequence: V | |||||||
Modified residue | 1016 | UniProt | In isoform Q9Y6M7-3; Phosphoserine | ||||
Sequence: F | |||||||
Modified residue | 1073 | UniProt | In isoform Q9Y6M7-6; Phosphoserine | ||||
Sequence: Y | |||||||
Modified residue | 1077 | UniProt | In isoform Q9Y6M7-13; Phosphoserine | ||||
Sequence: V | |||||||
Modified residue | 1102 | UniProt | In isoform Q9Y6M7-6; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1105 | UniProt | In isoform Q9Y6M7-6; Phosphoserine | ||||
Sequence: A | |||||||
Modified residue | 1106 | UniProt | In isoform Q9Y6M7-13; Phosphoserine | ||||
Sequence: V | |||||||
Modified residue | 1109 | UniProt | In isoform Q9Y6M7-13; Phosphoserine | ||||
Sequence: P | |||||||
Modified residue | 1111 | UniProt | In isoform Q9Y6M7-6; Phosphoserine | ||||
Sequence: M | |||||||
Modified residue | 1115 | UniProt | In isoform Q9Y6M7-13; Phosphoserine | ||||
Sequence: L | |||||||
Modified residue | 1167 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1167 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1176 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1188 | UniProt | In isoform Q9Y6M7-8; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1188 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1198 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1201 | UniProt | In isoform Q9Y6M7-7; Phosphoserine | ||||
Sequence: D | |||||||
Modified residue (large scale data) | 1207 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1213 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1213 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1217 | UniProt | In isoform Q9Y6M7-8; Phosphoserine | ||||
Modified residue | 1220 | UniProt | In isoform Q9Y6M7-8; Phosphoserine | ||||
Modified residue | 1226 | UniProt | In isoform Q9Y6M7-8; Phosphoserine | ||||
Modified residue | 1230 | UniProt | In isoform Q9Y6M7-7; Phosphoserine | ||||
Modified residue | 1233 | UniProt | In isoform Q9Y6M7-7; Phosphoserine | ||||
Modified residue | 1239 | UniProt | In isoform Q9Y6M7-7; Phosphoserine |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 1
Induction
Strongly induced upon macrophage differentiation (PubMed:29779931).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y6M7 | CIAO1 O76071 | 3 | EBI-1044546, EBI-725145 | |
BINARY | Q9Y6M7 | KRTAP4-5 Q9BYR2 | 3 | EBI-1044546, EBI-11993254 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Basic and acidic residues | ||||
Sequence: MERFRLEKKLPGPDEE | ||||||
Region | 1-22 | Disordered | ||||
Sequence: MERFRLEKKLPGPDEEAVVDLG | ||||||
Region | 52-93 | Disordered | ||||
Sequence: SKESRRRHRHRGHKHHHRRRKDKESDKEDGRESPSYDTPSQR | ||||||
Compositional bias | 53-72 | Basic residues | ||||
Sequence: KESRRRHRHRGHKHHHRRRK | ||||||
Region | 289-346 | Disordered | ||||
Sequence: SRAGTPAGSRCTTPVPTPQNSPPSSPSISRLTSRSSQESQRQAPELLVSPASDDIPTV | ||||||
Compositional bias | 312-334 | Polar residues | ||||
Sequence: SSPSISRLTSRSSQESQRQAPEL | ||||||
Region | 362-408 | Disordered | ||||
Sequence: EEQKNEENVDLTPGILASPQSAPGNLDNSKSGEIKGNGSGGSRENST | ||||||
Compositional bias | 375-408 | Polar residues | ||||
Sequence: GILASPQSAPGNLDNSKSGEIKGNGSGGSRENST | ||||||
Region | 552-572 | Disordered | ||||
Sequence: FHNGSTPTLGETPKEAAHHAG | ||||||
Region | 1008-1131 | In isoform Q9Y6M7-6; Essential for cell membrane localization and transport activity | ||||
Sequence: QRVTGLMIFILMGLSVFMTSVLKFIPMPVLYGVFLYMGVSSLKGIQLFDRIKLFGMPAKHQPDLIYLRYVPLWKVHIFTVIQLTCLVLLWVIKVSAAAVVFPMMVLALVFVRKLMDLCFTKREL | ||||||
Region | 1127-1214 | Essential for cell membrane localization and transport activity | ||||
Sequence: TKRELSWLDDLMPESKKKKEDDKKKKEKEEAERMLQDDDDTVHLPFEGGSLLQIPVKALKYSPDKPVSVKISFEDEPRKKYVDAETSL | ||||||
Region | 1134-1136 | CA2-binding | ||||
Sequence: LDD | ||||||
Region | 1144-1169 | Disordered | ||||
Sequence: KKEDDKKKKEKEEAERMLQDDDDTVH | ||||||
Motif | 1211-1214 | PDZ-binding | ||||
Sequence: ETSL |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 14 isoforms produced by Alternative splicing.
Q9Y6M7-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsmNBC3, NBCn1-A
- Length1,214
- Mass (Da)136,044
- Last updated2009-05-05 v2
- Checksum7B4ADA1E3F26813C
Q9Y6M7-2
- Name2
- SynonymsNBCn1-F
- Differences from canonical
- 251-374: Missing
Q9Y6M7-3
- Name3
- Differences from canonical
- 1-90: Missing
- 91-118: SQRVQFILGTEDDDEEHIPHDLFTEMDE → MAVTQFIHFREEIMGNMFFIIIFSTKDK
- 251-374: Missing
- 1189-1214: PDKPVSVKISFEDEPRKKYVDAETSL → GDPSIGNISDEMAKTAQWKALSMNTENAKVTRSNMSPDKPVSVK
Q9Y6M7-4
- Name4
Q9Y6M7-5
- Name5
- Differences from canonical
- 1-450: Missing
- 451-465: PAVLLTGLTEVPVPT → MEVVEAEKIVLLTSA
- 1188-1188: S → SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS
Q9Y6M7-6
- Name6
- SynonymsNBCn1-G
- Differences from canonical
- 1-11: MERFRLEKKLP → MEADGAGEQMRPLLTR
- 251-374: Missing
- 1188-1188: S → SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS
Q9Y6M7-7
- Name7
- SynonymsNBCn1-D
- Differences from canonical
- 1-11: MERFRLEKKLP → MEADGAGEQMRPLLTRVTSR
- 1188-1188: S → SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS
Q9Y6M7-8
- Name8
- SynonymsNBCn1-C
- Differences from canonical
- 1-11: MERFRLEKKLP → MEADGAGEQMRPLLTRVTSR
- 238-250: Missing
- 1188-1188: S → SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS
Q9Y6M7-9
- Name9
- SynonymsNBCn1-E
Q9Y6M7-10
- Name10
Q9Y6M7-11
- Name11
Q9Y6M7-12
- Name12
- SynonymsNBCn1-H
Q9Y6M7-13
- Name13
- Differences from canonical
- 1-11: MERFRLEKKLP → MEADGAGEQMRPLLTRVTSR
- 251-374: Missing
- 1188-1188: S → SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS
Q9Y6M7-14
- Name14
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047840 | 1-11 | in isoform 6, isoform 9, isoform 10, isoform 11 and isoform 12 | |||
Sequence: MERFRLEKKLP → MEADGAGEQMRPLLTR | ||||||
Alternative sequence | VSP_047841 | 1-11 | in isoform 7, isoform 8, isoform 13 and isoform 14 | |||
Sequence: MERFRLEKKLP → MEADGAGEQMRPLLTRVTSR | ||||||
Compositional bias | 1-16 | Basic and acidic residues | ||||
Sequence: MERFRLEKKLPGPDEE | ||||||
Alternative sequence | VSP_047839 | 1-90 | in isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047838 | 1-450 | in isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 53-72 | Basic residues | ||||
Sequence: KESRRRHRHRGHKHHHRRRK | ||||||
Alternative sequence | VSP_047842 | 91-118 | in isoform 3 and isoform 4 | |||
Sequence: SQRVQFILGTEDDDEEHIPHDLFTEMDE → MAVTQFIHFREEIMGNMFFIIIFSTKDK | ||||||
Alternative sequence | VSP_047843 | 238-250 | in isoform 8, isoform 10 and isoform 12 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047844 | 251-374 | in isoform 2, isoform 3, isoform 4, isoform 6, isoform 9, isoform 11, isoform 13 and isoform 14 | |||
Sequence: Missing | ||||||
Compositional bias | 312-334 | Polar residues | ||||
Sequence: SSPSISRLTSRSSQESQRQAPEL | ||||||
Compositional bias | 375-408 | Polar residues | ||||
Sequence: GILASPQSAPGNLDNSKSGEIKGNGSGGSRENST | ||||||
Alternative sequence | VSP_047845 | 451-465 | in isoform 5 | |||
Sequence: PAVLLTGLTEVPVPT → MEVVEAEKIVLLTSA | ||||||
Alternative sequence | VSP_047846 | 581-582 | in isoform 10, isoform 11 and isoform 14 | |||
Sequence: LF → VQ | ||||||
Alternative sequence | VSP_047847 | 583-1214 | in isoform 10, isoform 11 and isoform 14 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047848 | 1188 | in isoform 5, isoform 6, isoform 7, isoform 8 and isoform 13 | |||
Sequence: S → SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS | ||||||
Alternative sequence | VSP_047849 | 1189-1214 | in isoform 3 | |||
Sequence: PDKPVSVKISFEDEPRKKYVDAETSL → GDPSIGNISDEMAKTAQWKALSMNTENAKVTRSNMSPDKPVSVK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB012130 EMBL· GenBank· DDBJ | BAA25898.1 EMBL· GenBank· DDBJ | mRNA | ||
AF047033 EMBL· GenBank· DDBJ | AAD38322.1 EMBL· GenBank· DDBJ | mRNA | ||
AF089726 EMBL· GenBank· DDBJ | AAG16773.1 EMBL· GenBank· DDBJ | mRNA | ||
AF053755 EMBL· GenBank· DDBJ | AAF21720.1 EMBL· GenBank· DDBJ | mRNA | ||
EU499349 EMBL· GenBank· DDBJ | ACB47400.1 EMBL· GenBank· DDBJ | mRNA | ||
EU934246 EMBL· GenBank· DDBJ | ACH61958.1 EMBL· GenBank· DDBJ | mRNA | ||
EU934248 EMBL· GenBank· DDBJ | ACH61960.1 EMBL· GenBank· DDBJ | mRNA | ||
EU934249 EMBL· GenBank· DDBJ | ACH61961.1 EMBL· GenBank· DDBJ | mRNA | ||
EU934250 EMBL· GenBank· DDBJ | ACH61962.1 EMBL· GenBank· DDBJ | mRNA | ||
FJ178574 EMBL· GenBank· DDBJ | ACI24740.1 EMBL· GenBank· DDBJ | mRNA | ||
FJ178575 EMBL· GenBank· DDBJ | ACI24741.1 EMBL· GenBank· DDBJ | mRNA | ||
FJ178576 EMBL· GenBank· DDBJ | ACI24742.1 EMBL· GenBank· DDBJ | mRNA | ||
GU354307 EMBL· GenBank· DDBJ | ADC32649.1 EMBL· GenBank· DDBJ | mRNA | ||
GU354308 EMBL· GenBank· DDBJ | ADC32650.1 EMBL· GenBank· DDBJ | mRNA | ||
GU354309 EMBL· GenBank· DDBJ | ADC32651.1 EMBL· GenBank· DDBJ | mRNA | ||
GU354310 EMBL· GenBank· DDBJ | ADC32652.1 EMBL· GenBank· DDBJ | mRNA | ||
CR627428 EMBL· GenBank· DDBJ | CAH10515.1 EMBL· GenBank· DDBJ | mRNA | ||
AC099535 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471055 EMBL· GenBank· DDBJ | EAW64382.1 EMBL· GenBank· DDBJ | Genomic DNA |