Q03720 · SLO_DROME
- ProteinCalcium-activated potassium channel slowpoke
- Geneslo
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1200 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Potassium channel activated by both membrane depolarization or increase in cytosolic Ca2+ that mediates export of K+. Its activation dampens the excitatory events that elevate the cytosolic Ca2+ concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Kinetics are determined by alternative splicing, phosphorylation status and its combination interaction with Slob and 14-3-3-zeta. While the interaction with Slob1 alone increases its activity, its interaction with both Slob1 and 14-3-3-zeta decreases its activity.
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 | membrane | |
Cellular Component | monoatomic ion channel complex | |
Cellular Component | neuron projection | |
Cellular Component | neuronal cell body | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic membrane | |
Molecular Function | calcium-activated potassium channel activity | |
Molecular Function | large conductance calcium-activated potassium channel activity | |
Biological Process | circadian behavior | |
Biological Process | circadian rhythm | |
Biological Process | male courtship behavior, veined wing generated song production | |
Biological Process | negative regulation of neuromuscular synaptic transmission | |
Biological Process | potassium ion transmembrane transport | |
Biological Process | potassium ion transport | |
Biological Process | regulation of synaptic assembly at neuromuscular junction | |
Biological Process | response to xenobiotic stimulus |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCalcium-activated potassium channel slowpoke
- Short namesdSlo
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ03720
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-48 | Extracellular | ||||
Sequence: MASGLIDTNFSSTLANGMSGCDQSTVESLADDPTDSPFDADDCLKVRK | ||||||
Transmembrane | 49-69 | Helical; Name=Segment S0 | ||||
Sequence: YWCFLLSSIFTFLAGLLVVLL | ||||||
Topological domain | 70-127 | Cytoplasmic | ||||
Sequence: WRAFAFVCCRKEPDLGPNDPKQKEQKASRNKQEFEGTFMTEAKDWAGELISGQTTTGR | ||||||
Transmembrane | 128-149 | Helical; Name=Segment S1 | ||||
Sequence: ILVVLVFILSIASLIIYFVDAS | ||||||
Topological domain | 150-164 | Extracellular | ||||
Sequence: SEEVERCQKWSNNIT | ||||||
Transmembrane | 165-185 | Helical; Name=Segment S2 | ||||
Sequence: QQIDLAFNIFFMVYFFIRFIA | ||||||
Topological domain | 186-189 | Cytoplasmic | ||||
Sequence: ASDK | ||||||
Transmembrane | 190-210 | Helical; Name=Segment S3 | ||||
Sequence: LWFMLEMYSFVDYFTIPPSFV | ||||||
Topological domain | 211-214 | Extracellular | ||||
Sequence: SIYL | ||||||
Transmembrane | 215-235 | Helical; Voltage-sensor; Name=Segment S4 | ||||
Sequence: DRTWIGLRFLRALRLMTVPDI | ||||||
Topological domain | 236-250 | Cytoplasmic | ||||
Sequence: LQYLNVLKTSSSIRL | ||||||
Transmembrane | 251-271 | Helical; Name=Segment S5 | ||||
Sequence: AQLVSIFISVWLTAAGIIHLL | ||||||
Topological domain | 272-284 | Extracellular | ||||
Sequence: ENSGDPLDFNNAH | ||||||
Intramembrane | 285-307 | Pore-forming; Name=P region | ||||
Sequence: RLSYWTCVYFLIVTMSTVGYGDV | ||||||
Topological domain | 308-316 | Extracellular | ||||
Sequence: YCETVLGRT | ||||||
Transmembrane | 317-337 | Helical; Name=Segment S6 | ||||
Sequence: FLVFFLLVGLAMFASSIPEII | ||||||
Topological domain | 338-1200 | Cytoplasmic | ||||
Sequence: ELVGSGNKYGGELKREHGKRHIVVCGHITYESVSHFLKDFLHEDREDVDVEVVFLHRKPPDLELEGLFKRHFTTVEFFQGTIMNPIDLQRVKVHEADACLVLANKYCQDPDAEDAANIMRVISIKNYSDDIRVIIQLMQYHNKAYLLNIPSWDWKQGDDVICLAELKLGFIAQSCLAPGFSTMMANLFAMRSFKTSPDMQSWTNDYLRGTGMEMYTETLSPTFIGIPFAQATELCFSKLKLLLLAIEIKGAEEGADSKISINPRGAKIQANTQGFFIAQSADEVKRAWFYCKACHEDIKDETLIKKCKCKNLTVQPRSKFDDLDEHHPAPTFTPPELPKRVHVRGSVSGDITRDREDTNLLNRNVRRPNGTGNGTGGMHHMNNTAAAAAAAAAAGKQVNKVKPTVNVSRQVEGQVISPSQYNRPTSRSSGTGTQNQNGGVSLPAGIADDQSKDFDFEKTEMKYDSTGMFHWSPAKSLEDCILDRNQAAMTVLNGHVVVCLFADPDSPLIGLRNLVMPLRASNFHYHELKHVVIVGSVDYIRREWKMLQNLPKISVLNGSPLSRADLRAVNVNLCDMCCILSAKVPSNDDPTLADKEAILASLNIKAMTFDDTIGVLSQRGPEFDNLSATAGSPIVLQRRGSVYGANVPMITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSTTYFNQNALTLIRSLITGGATPELELILAEGAGLRGGYSTVESLSNRDRCRVGQISLYDGPLAQFGECGKYGDLFVAALKSYGMLCIGLYRFRDTSSSCDASSKRYVITNPPDDFSLLPTDQVFVLMQFDPGLEYKPPAVRAPAGGRGTNTQGSGVGGGGSNKDDNS |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 552 | Affects the interaction with SRC. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 978 | Does not affect activation of channel. | ||||
Sequence: S → A | ||||||
Mutagenesis | 1002-1006 | Alters calcium binding. | ||||
Sequence: DDDDD → NNNNN | ||||||
Mutagenesis | 1012 | Affects the interaction with SRC. | ||||
Sequence: Y → F |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000054141 | 1-1200 | Calcium-activated potassium channel slowpoke | |||
Sequence: MASGLIDTNFSSTLANGMSGCDQSTVESLADDPTDSPFDADDCLKVRKYWCFLLSSIFTFLAGLLVVLLWRAFAFVCCRKEPDLGPNDPKQKEQKASRNKQEFEGTFMTEAKDWAGELISGQTTTGRILVVLVFILSIASLIIYFVDASSEEVERCQKWSNNITQQIDLAFNIFFMVYFFIRFIAASDKLWFMLEMYSFVDYFTIPPSFVSIYLDRTWIGLRFLRALRLMTVPDILQYLNVLKTSSSIRLAQLVSIFISVWLTAAGIIHLLENSGDPLDFNNAHRLSYWTCVYFLIVTMSTVGYGDVYCETVLGRTFLVFFLLVGLAMFASSIPEIIELVGSGNKYGGELKREHGKRHIVVCGHITYESVSHFLKDFLHEDREDVDVEVVFLHRKPPDLELEGLFKRHFTTVEFFQGTIMNPIDLQRVKVHEADACLVLANKYCQDPDAEDAANIMRVISIKNYSDDIRVIIQLMQYHNKAYLLNIPSWDWKQGDDVICLAELKLGFIAQSCLAPGFSTMMANLFAMRSFKTSPDMQSWTNDYLRGTGMEMYTETLSPTFIGIPFAQATELCFSKLKLLLLAIEIKGAEEGADSKISINPRGAKIQANTQGFFIAQSADEVKRAWFYCKACHEDIKDETLIKKCKCKNLTVQPRSKFDDLDEHHPAPTFTPPELPKRVHVRGSVSGDITRDREDTNLLNRNVRRPNGTGNGTGGMHHMNNTAAAAAAAAAAGKQVNKVKPTVNVSRQVEGQVISPSQYNRPTSRSSGTGTQNQNGGVSLPAGIADDQSKDFDFEKTEMKYDSTGMFHWSPAKSLEDCILDRNQAAMTVLNGHVVVCLFADPDSPLIGLRNLVMPLRASNFHYHELKHVVIVGSVDYIRREWKMLQNLPKISVLNGSPLSRADLRAVNVNLCDMCCILSAKVPSNDDPTLADKEAILASLNIKAMTFDDTIGVLSQRGPEFDNLSATAGSPIVLQRRGSVYGANVPMITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSTTYFNQNALTLIRSLITGGATPELELILAEGAGLRGGYSTVESLSNRDRCRVGQISLYDGPLAQFGECGKYGDLFVAALKSYGMLCIGLYRFRDTSSSCDASSKRYVITNPPDDFSLLPTDQVFVLMQFDPGLEYKPPAVRAPAGGRGTNTQGSGVGGGGSNKDDNS | ||||||
Modified residue | 978 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated. Phosphorylation may be mediated by both PKA and SRC kinases, which activate the channel activity. Phosphorylation by PKA is however unclear. Indeed, although modulation of channel activity requires Pka-C1, it does not interact with the whole PKA holoenzyme. Moreover, modulation of activity does not depend upon phosphorylation of Ser-978.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in muscle cells, neurons of the CNS and PNS, mushroom bodies, a limited number of cells in embryonic and larval midgut and in epithelial-derived tracheal cells. During pupariation and embryogenesis, it is expressed in muscles many hours prior to the appearance of functional channels.
Gene expression databases
Interaction
Subunit
Homotetramer; which constitutes the calcium-activated potassium channel (By similarity).
Interacts with Slip1. Interacts with Slob, and, indirectly with 14-3-3-zeta via its interaction with Slob. Interacts with Pka-C1 and Src kinases, which can bind simultaneously to it
Interacts with Slip1. Interacts with Slob, and, indirectly with 14-3-3-zeta via its interaction with Slob. Interacts with Pka-C1 and Src kinases, which can bind simultaneously to it
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q03720 | Pka-C1 P12370 | 5 | EBI-426805, EBI-82224 | |
BINARY | Q03720 | Slip1 Q8MR31 | 5 | EBI-426805, EBI-123875 | |
BINARY | Q03720 | Slob Q8IPH9-1 | 2 | EBI-426805, EBI-424896 | |
BINARY | Q03720 | Src64B P00528 | 3 | EBI-426805, EBI-87092 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 301-304 | Selectivity for potassium | ||||
Sequence: TVGY | ||||||
Domain | 356-498 | RCK N-terminal 1 | ||||
Sequence: KRHIVVCGHITYESVSHFLKDFLHEDREDVDVEVVFLHRKPPDLELEGLFKRHFTTVEFFQGTIMNPIDLQRVKVHEADACLVLANKYCQDPDAEDAANIMRVISIKNYSDDIRVIIQLMQYHNKAYLLNIPSWDWKQGDDVI | ||||||
Region | 505-525 | Segment S7 | ||||
Sequence: LGFIAQSCLAPGFSTMMANLF | ||||||
Region | 563-583 | Segment S8 | ||||
Sequence: IPFAQATELCFSKLKLLLLAI | ||||||
Region | 681-713 | Disordered | ||||
Sequence: RGSVSGDITRDREDTNLLNRNVRRPNGTGNGTG | ||||||
Compositional bias | 683-699 | Basic and acidic residues | ||||
Sequence: SVSGDITRDREDTNLLN | ||||||
Compositional bias | 746-778 | Polar residues | ||||
Sequence: RQVEGQVISPSQYNRPTSRSSGTGTQNQNGGVS | ||||||
Region | 746-785 | Disordered | ||||
Sequence: RQVEGQVISPSQYNRPTSRSSGTGTQNQNGGVSLPAGIAD | ||||||
Region | 828-848 | Segment S9 | ||||
Sequence: VLNGHVVVCLFADPDSPLIGL | ||||||
Domain | 830-974 | RCK N-terminal 2 | ||||
Sequence: NGHVVVCLFADPDSPLIGLRNLVMPLRASNFHYHELKHVVIVGSVDYIRREWKMLQNLPKISVLNGSPLSRADLRAVNVNLCDMCCILSAKVPSNDDPTLADKEAILASLNIKAMTFDDTIGVLSQRGPEFDNLSATAGSPIVLQ | ||||||
Motif | 988-1010 | Calcium bowl | ||||
Sequence: TELVNDSNVQFLDQDDDDDPDTE | ||||||
Region | 1017-1037 | Segment S10 | ||||
Sequence: FACGTAFAVSVLDSLMSTTYF | ||||||
Region | 1170-1200 | Disordered | ||||
Sequence: PPAVRAPAGGRGTNTQGSGVGGGGSNKDDNS | ||||||
Compositional bias | 1180-1200 | Polar residues | ||||
Sequence: RGTNTQGSGVGGGGSNKDDNS |
Domain
The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor.
The pore-forming domain (also referred as P region) is imbedded into the membrane, and forms the selectivity filter of the pore. It contains the signature sequence of potassium channels that displays selectivity to potassium (By similarity).
The RCK N-terminal domain mediates the homotetramerization, thereby promoting the assembly of monomers into functional potassium channel. It includes binding sites for Ca2+ and Mg2+ (By similarity).
The calcium bowl constitutes one of the Ca2+ sensors and probably acts as a Ca2+-binding site.
Sequence similarities
Belongs to the potassium channel family. Calcium-activated (TC 1.A.1.3) subfamily. Slo sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 20 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
Q03720-1
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.
- NameN
- Length1,200
- Mass (Da)133,102
- Last updated2006-09-19 v3
- Checksum306A12234C63AD0D
Q03720-2
- Name2
Q03720-4
- Name3
- Differences from canonical
- 761-761: P → PPENDANPYAGYQLAYEVKKLMP
Q03720-6
- Name5
Q03720-3
- Name6
Q03720-5
- NameA
- SynonymsG
- Differences from canonical
- 661-685: Missing
Q03720-7
- NameB
- Differences from canonical
- 1-17: Missing
Q03720-8
- NameC
Q03720-9
- NameD
Q03720-10
- NameE
Q03720-11
- NameF
Q03720-12
- NameH
Q03720-13
- NameI
- Differences from canonical
- 650-661: TVQPRSKFDDLD → ATFRKGVRAVQMVGRAKDDEYSLSN
Q03720-14
- NameJ
- Differences from canonical
- 650-686: TVQPRSKFDDLDEHHPAPTFTPPELPKRVHVRGSVSG → ATFRKGVRAVQMVGRAS
Q03720-15
- NameK
- Differences from canonical
- 661-697: DEHHPAPTFTPPELPKRVHVRGSVSGDITRDREDTNL → V
Q03720-16
- NameL
- Differences from canonical
- 649-685: LTVQPRSKFDDLDEHHPAPTFTPPELPKRVHVRGSVS → YVGMIMMQTGMVNQGITSVMNTME
Q03720-17
- NameM
Q03720-18
- NameO
Q03720-19
- NameP
Q03720-20
- NameQ
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0B4KGV3 | A0A0B4KGV3_DROME | slo | 1135 | ||
A0A0B4KGZ3 | A0A0B4KGZ3_DROME | slo | 1191 | ||
A0A0B4KHF8 | A0A0B4KHF8_DROME | slo | 1159 | ||
A0A0B4KI08 | A0A0B4KI08_DROME | slo | 1152 | ||
A0A0B4KHT2 | A0A0B4KHT2_DROME | slo | 1217 | ||
E1JIV7 | E1JIV7_DROME | slo | 1210 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_009999 | 1-17 | in isoform 6, isoform B and isoform C | |||
Sequence: Missing | ||||||
Sequence conflict | 81 | in Ref. 6; AAC47020/AAC47021 | ||||
Sequence: E → R | ||||||
Sequence conflict | 281 | in Ref. 1; AAA28902, 2; AAA28651 and 5; AAO45232 | ||||
Sequence: N → D | ||||||
Alternative sequence | VSP_020625 | 328-355 | in isoform D | |||
Sequence: MFASSIPEIIELVGSGNKYGGELKREHG → VFASWIPEITELAAQRSKYGGTYSKDPR | ||||||
Alternative sequence | VSP_010000 | 328-356 | in isoform 6, isoform E, isoform P and isoform Q | |||
Sequence: MFASSIPEIIELVGSGNKYGGELKREHGK → IFASCIPEIIDLIGTRAKYGGTLKNEKGR | ||||||
Alternative sequence | VSP_010001 | 396-426 | in isoform 5, isoform 6 and isoform F | |||
Sequence: PPDLELEGLFKRHFTTVEFFQGTIMNPIDLQ → EPDLELEGLLKRHYTTVAFFQGTMMNAVDLE | ||||||
Alternative sequence | VSP_010002 | 536-569 | in isoform 5, isoform C, isoform H, isoform O, isoform P and isoform Q | |||
Sequence: MQSWTNDYLRGTGMEMYTETLSPTFIGIPFAQAT → TQAWQNDYLQGTGCEMYTETLSPSFTGMTFPQAS | ||||||
Alternative sequence | VSP_020626 | 649-685 | in isoform L | |||
Sequence: LTVQPRSKFDDLDEHHPAPTFTPPELPKRVHVRGSVS → YVGMIMMQTGMVNQGITSVMNTME | ||||||
Alternative sequence | VSP_050267 | 650-661 | in isoform 2, isoform 5 and isoform I | |||
Sequence: TVQPRSKFDDLD → ATFRKGVRAVQMVGRAKDDEYSLSN | ||||||
Alternative sequence | VSP_010003 | 650-661 | in isoform 6 | |||
Sequence: TVQPRSKFDDLD → ATFRKGVRAVQMVGRAN | ||||||
Alternative sequence | VSP_020627 | 650-686 | in isoform J | |||
Sequence: TVQPRSKFDDLDEHHPAPTFTPPELPKRVHVRGSVSG → ATFRKGVRAVQMVGRAS | ||||||
Alternative sequence | VSP_010004 | 661-685 | in isoform A, isoform D, isoform E, isoform F, isoform H, isoform M and isoform Q | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_020628 | 661-697 | in isoform K, isoform O and isoform P | |||
Sequence: DEHHPAPTFTPPELPKRVHVRGSVSGDITRDREDTNL → V | ||||||
Compositional bias | 683-699 | Basic and acidic residues | ||||
Sequence: SVSGDITRDREDTNLLN | ||||||
Compositional bias | 746-778 | Polar residues | ||||
Sequence: RQVEGQVISPSQYNRPTSRSSGTGTQNQNGGVS | ||||||
Alternative sequence | VSP_050268 | 761 | in isoform 2, isoform 3, isoform 5, isoform 6 and isoform M | |||
Sequence: P → PPENDANPYAGYQLAYEVKKLMP | ||||||
Sequence conflict | 994 | in Ref. 1; AAA28902, 2; AAA28651 and 5; AAO45232 | ||||
Sequence: S → G | ||||||
Compositional bias | 1180-1200 | Polar residues | ||||
Sequence: RGTNTQGSGVGGGGSNKDDNS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M69053 EMBL· GenBank· DDBJ | AAA28902.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
M96840 EMBL· GenBank· DDBJ | AAA28651.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014297 EMBL· GenBank· DDBJ | AAF56324.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAN14013.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAS65211.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52977.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52978.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52979.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52980.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52981.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52982.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52983.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52984.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52985.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52986.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52987.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52988.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52989.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAX52990.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT004876 EMBL· GenBank· DDBJ | AAO45232.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
U40315 EMBL· GenBank· DDBJ | AAC47020.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U40315 EMBL· GenBank· DDBJ | AAC47021.1 EMBL· GenBank· DDBJ | Genomic DNA |