P34158 · CFTR_RAT
- ProteinCystic fibrosis transmembrane conductance regulator
- GeneCftr
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1476 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis. Mediates the transport of chloride ions across the cell membrane (By similarity).
Possesses an intrinsic ATPase activity and utilizes ATP to gate its channel; the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains (By similarity).
The ion channel is also permeable to HCO3-; selectivity depends on the extracellular chloride concentration. Exerts its function also by modulating the activity of other ion channels and transporters. Contributes to the regulation of the pH and the ion content of the epithelial fluid layer. Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7. Can inhibit the chloride channel activity of ANO1 (By similarity).
Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (By similarity).
Possesses an intrinsic ATPase activity and utilizes ATP to gate its channel; the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains (By similarity).
The ion channel is also permeable to HCO3-; selectivity depends on the extracellular chloride concentration. Exerts its function also by modulating the activity of other ion channels and transporters. Contributes to the regulation of the pH and the ion content of the epithelial fluid layer. Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7. Can inhibit the chloride channel activity of ANO1 (By similarity).
Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (By similarity).
Catalytic activity
- chloride(in) = chloride(out)
- hydrogencarbonate(in) = hydrogencarbonate(out)
- ATP + H2O = ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 401 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 458-465 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: GSTGAGKT | ||||||
Binding site | 458-465 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GSTGAGKT | ||||||
Binding site | 493 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 1215 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 1240-1247 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: GRTGSGKS | ||||||
Binding site | 1240-1247 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GRTGSGKS |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCystic fibrosis transmembrane conductance regulator
- Short namesCFTR
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP34158
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Apical cell membrane ; Multi-pass membrane protein
Early endosome membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Recycling endosome membrane ; Multi-pass membrane protein
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Note: The channel is internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (By similarity).
In the oviduct and bronchus, detected on the apical side of epithelial cells, but not associated with cilia (By similarity).
In Sertoli cells, a processed product is detected in the nucleus (PubMed:29453757).
ER stress induces GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity).
In the oviduct and bronchus, detected on the apical side of epithelial cells, but not associated with cilia (By similarity).
In Sertoli cells, a processed product is detected in the nucleus (PubMed:29453757).
ER stress induces GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-77 | Cytoplasmic | ||||
Sequence: MQKSPLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSSDSADHLSEKLEREWDREQASKKKPQLIHALRRCF | ||||||
Transmembrane | 78-98 | Helical; Name=1 | ||||
Sequence: VWRFVFYGVLLYLGEVTKAVQ | ||||||
Topological domain | 99-122 | Extracellular | ||||
Sequence: PVLLGRIIASYDPDNTEERSIAIY | ||||||
Transmembrane | 123-146 | Helical; Name=2 | ||||
Sequence: LGIGLCLLFIVRTLLLHPAIFGLH | ||||||
Topological domain | 147-195 | Cytoplasmic | ||||
Sequence: HIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGL | ||||||
Transmembrane | 196-216 | Helical; Name=3 | ||||
Sequence: ALAHFIWIAPLQVVLLMGLLW | ||||||
Topological domain | 217-222 | Extracellular | ||||
Sequence: DLLQFS | ||||||
Transmembrane | 223-243 | Helical; Name=4 | ||||
Sequence: AFCGLGLLIVLVIFQAILGKM | ||||||
Topological domain | 244-298 | Cytoplasmic | ||||
Sequence: MVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRR | ||||||
Transmembrane | 299-319 | Helical; Name=5 | ||||
Sequence: SAYMRFFTSSAFFFSGFFVVF | ||||||
Topological domain | 320-339 | Extracellular | ||||
Sequence: LSVLPYTVINGIVLRKIFTT | ||||||
Transmembrane | 340-358 | Helical; Name=6 | ||||
Sequence: ISFCIVLRMSVTRQFPTAV | ||||||
Topological domain | 359-853 | Cytoplasmic | ||||
Sequence: QIWYDSLGMIRKIQDFLQTQEYKVLEYNLMFTGLVMENVTAFWEEGFQELLEKVQLNNDDRKTSNGENHLSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFTEERRSSILTETLRRFSVDDASTTWNKAKQSFRQTGEFGEKRKNSILSSFSSVKKISIVQKTPLSIEGESDDLQERRLSLVPDSEHGEAALPRSNMITAGPTFPGRRRQSVLDLMTFTPSSVSSSLQRTRASIRKISLAPRISLKEEDIYSRRLSQDSTLNITEEINEEDLKECFFDDMVKIPTVTTWNTYLRYFTLHRG | ||||||
Transmembrane | 854-874 | Helical; Name=7 | ||||
Sequence: LFAVLIWCVLVFLVEVAASLF | ||||||
Topological domain | 875-913 | Extracellular | ||||
Sequence: VLWLLKNNPVNGGNNGTKIANTSYVVVITSSSFYYIFYI | ||||||
Transmembrane | 914-934 | Discontinuously helical; Name=8 | ||||
Sequence: YVGVADTLLALSLFRGLPLVH | ||||||
Topological domain | 935-985 | Cytoplasmic | ||||
Sequence: TLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLT | ||||||
Transmembrane | 986-1006 | Helical; Name=9 | ||||
Sequence: IFDFIQLLFIVVGAIIVVSAL | ||||||
Topological domain | 1007-1008 | Extracellular | ||||
Sequence: QP | ||||||
Transmembrane | 1009-1029 | Helical; Name=10 | ||||
Sequence: YIFLATVPGLAVFILLRAYFL | ||||||
Topological domain | 1030-1090 | Cytoplasmic | ||||
Sequence: HTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLAT | ||||||
Transmembrane | 1091-1111 | Helical; Name=11 | ||||
Sequence: LRWFQMRIDMIFVLFFIVVTF | ||||||
Topological domain | 1112-1125 | Extracellular | ||||
Sequence: ISILTTGEGEGTTG | ||||||
Transmembrane | 1126-1146 | Helical; Name=12 | ||||
Sequence: IILTLAMNIMSTLQWAVNSSI | ||||||
Topological domain | 1147-1476 | Cytoplasmic | ||||
Sequence: DTDSLMRSVSRVFKFIDIQTEESICTKIMKELHSEDSPNALVIKNEHVKKCDTWPSGGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRALSSSEKMKLFHGRHSSKQKPRTQITAVKEETEEEVQETRL |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, lipidation, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000093428 | 1-1476 | Cystic fibrosis transmembrane conductance regulator | |||
Sequence: MQKSPLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSSDSADHLSEKLEREWDREQASKKKPQLIHALRRCFVWRFVFYGVLLYLGEVTKAVQPVLLGRIIASYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVFLSVLPYTVINGIVLRKIFTTISFCIVLRMSVTRQFPTAVQIWYDSLGMIRKIQDFLQTQEYKVLEYNLMFTGLVMENVTAFWEEGFQELLEKVQLNNDDRKTSNGENHLSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFTEERRSSILTETLRRFSVDDASTTWNKAKQSFRQTGEFGEKRKNSILSSFSSVKKISIVQKTPLSIEGESDDLQERRLSLVPDSEHGEAALPRSNMITAGPTFPGRRRQSVLDLMTFTPSSVSSSLQRTRASIRKISLAPRISLKEEDIYSRRLSQDSTLNITEEINEEDLKECFFDDMVKIPTVTTWNTYLRYFTLHRGLFAVLIWCVLVFLVEVAASLFVLWLLKNNPVNGGNNGTKIANTSYVVVITSSSFYYIFYIYVGVADTLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTTGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFIDIQTEESICTKIMKELHSEDSPNALVIKNEHVKKCDTWPSGGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRALSSSEKMKLFHGRHSSKQKPRTQITAVKEETEEEVQETRL | ||||||
Lipidation | 524 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 549 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 660 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 670 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Modified residue | 684 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 698 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 710 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 715 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 732 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 763 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 785 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 790 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 808 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 889 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 895 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 1391 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 1440 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1452 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
N-glycosylated.
Phosphorylated; cAMP treatment promotes phosphorylation and activates the channel. Dephosphorylation decreases the ATPase activity (in vitro). Phosphorylation at PKA sites activates the channel. Phosphorylation at PKC sites enhances the response to phosphorylation by PKA. Phosphorylated by AMPK; this inhibits channel activity.
Ubiquitinated, leading to its degradation in the lysosome. Deubiquitination by USP10 in early endosomes enhances its endocytic recycling to the cell membrane. Ubiquitinated by RNF185 during ER stress. Ubiquitinated by MARCHF2 (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in epithelial cells in nasopharynx, submandibular gland, pancreas and ileum (at protein level) (PubMed:12519745).
Expressed in the epididymis (PubMed:30659401).
In the caput section of the epididymis, expressed uniformly on both the luminal and basolateral sides of the ducts and on sperm in the caput lumen (at protein level) (PubMed:30659401).
In the cauda, detected along the luminal border but not continuously and is also expressed on the basolateral surface (PubMed:30659401).
Within the caudal lumen, detected on sperm (PubMed:30659401).
Expressed in the epididymis (PubMed:30659401).
In the caput section of the epididymis, expressed uniformly on both the luminal and basolateral sides of the ducts and on sperm in the caput lumen (at protein level) (PubMed:30659401).
In the cauda, detected along the luminal border but not continuously and is also expressed on the basolateral surface (PubMed:30659401).
Within the caudal lumen, detected on sperm (PubMed:30659401).
Interaction
Subunit
Monomer; does not require oligomerization for channel activity. May form oligomers in the membrane (By similarity).
Interacts with SLC4A7 through NHERF1 (By similarity).
Interacts with SHANK2 (PubMed:14679199).
Interacts with NHERF1 and MYO6. Interacts (via C-terminus) with GOPC (via PDZ domain); this promotes CFTR internalization and thereby decreases channel activity (PubMed:11707463).
Interacts with SLC4A7 through NHERF1. Found in a complex with MYO5B and RAB11A. Interacts with ANO1. Interacts with SLC26A8 (By similarity).
Interacts with AHCYL1; the interaction increases CFTR activity (By similarity).
Interacts with CSE1L (By similarity).
The core-glycosylated form interacts with GORASP2 (via PDZ GRASP-type 1 domain) in respone to ER stress (By similarity).
Interacts with MARCHF2; the interaction leads to CFTR ubiqtuitination and degradation (By similarity).
Interacts with SLC4A7 through NHERF1 (By similarity).
Interacts with SHANK2 (PubMed:14679199).
Interacts with NHERF1 and MYO6. Interacts (via C-terminus) with GOPC (via PDZ domain); this promotes CFTR internalization and thereby decreases channel activity (PubMed:11707463).
Interacts with SLC4A7 through NHERF1. Found in a complex with MYO5B and RAB11A. Interacts with ANO1. Interacts with SLC26A8 (By similarity).
Interacts with AHCYL1; the interaction increases CFTR activity (By similarity).
Interacts with CSE1L (By similarity).
The core-glycosylated form interacts with GORASP2 (via PDZ GRASP-type 1 domain) in respone to ER stress (By similarity).
Interacts with MARCHF2; the interaction leads to CFTR ubiqtuitination and degradation (By similarity).
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 81-365 | ABC transmembrane type-1 1 | ||||
Sequence: FVFYGVLLYLGEVTKAVQPVLLGRIIASYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVFLSVLPYTVINGIVLRKIFTTISFCIVLRMSVTRQFPTAVQIWYDSL | ||||||
Domain | 412-646 | ABC transporter 1 | ||||
Sequence: VQLNNDDRKTSNGENHLSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMG | ||||||
Region | 654-826 | Disordered R region | ||||
Sequence: TEERRSSILTETLRRFSVDDASTTWNKAKQSFRQTGEFGEKRKNSILSSFSSVKKISIVQKTPLSIEGESDDLQERRLSLVPDSEHGEAALPRSNMITAGPTFPGRRRQSVLDLMTFTPSSVSSSLQRTRASIRKISLAPRISLKEEDIYSRRLSQDSTLNITEEINEEDLKE | ||||||
Domain | 854-1153 | ABC transmembrane type-1 2 | ||||
Sequence: LFAVLIWCVLVFLVEVAASLFVLWLLKNNPVNGGNNGTKIANTSYVVVITSSSFYYIFYIYVGVADTLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTTGIILTLAMNIMSTLQWAVNSSIDTDSLMR | ||||||
Domain | 1208-1439 | ABC transporter 2 | ||||
Sequence: VKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRALSS | ||||||
Region | 1382-1476 | Interaction with GORASP2 | ||||
Sequence: RVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRALSSSEKMKLFHGRHSSKQKPRTQITAVKEETEEEVQETRL | ||||||
Region | 1445-1476 | Disordered | ||||
Sequence: LFHGRHSSKQKPRTQITAVKEETEEEVQETRL | ||||||
Compositional bias | 1459-1476 | Basic and acidic residues | ||||
Sequence: QITAVKEETEEEVQETRL | ||||||
Motif | 1474-1476 | PDZ-binding | ||||
Sequence: TRL |
Domain
Binds and hydrolyzes ATP via the two cytoplasmic ABC transporter nucleotide-binding domains. The two ATP-binding domains interact with each other, forming a head-to-tail dimer. Normal ATPase activity requires interaction between the two domains. The first ABC transporter nucleotide-binding domain has no ATPase activity by itself.
The PDZ-binding motif mediates interactions with GOPC and with the SLC4A7, NHERF1/EBP50 complex.
The disordered R region mediates channel activation when it is phosphorylated, but not in the absence of phosphorylation.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,476
- Mass (Da)167,830
- Last updated2007-06-12 v3
- ChecksumB2B2A25EB5107640
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AKE9 | A0A8I6AKE9_RAT | Cftr | 1662 | ||
A0A8I6AKF6 | A0A8I6AKF6_RAT | Cftr | 1446 | ||
A0A0G2K3B1 | A0A0G2K3B1_RAT | Cftr | 1665 | ||
A0A8I6AU15 | A0A8I6AU15_RAT | Cftr | 530 | ||
A0A8I6A376 | A0A8I6A376_RAT | Cftr | 1499 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 987-988 | in Ref. 3; AAA40918 | ||||
Sequence: FD → LT | ||||||
Compositional bias | 1459-1476 | Basic and acidic residues | ||||
Sequence: QITAVKEETEEEVQETRL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DP000027 EMBL· GenBank· DDBJ | AAR16315.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L26098 EMBL· GenBank· DDBJ | AAA73561.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M89906 EMBL· GenBank· DDBJ | AAA40918.1 EMBL· GenBank· DDBJ | mRNA |