O35889 · AFAD_RAT
- ProteinAfadin
- GeneAfdn
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1829 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs) (PubMed:9334353).
Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton (PubMed:9334353).
May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity).
Essential for the organization of adherens junctions (By similarity).
Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton (PubMed:9334353).
May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity).
Essential for the organization of adherens junctions (By similarity).
Miscellaneous
Isoform 1 increases the viscosity of F-actin in a dose-dependent manner. Isoform 1 causes F-actin to associate into bundles and meshworks.
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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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAfadin
- 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 accessionO35889
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Not found at cell-matrix AJs.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000215920 | 1-1829 | Afadin | |||
Sequence: MSAGGRDEERRKLADIIHHWNANRLDLFEISQPTEDLEFHGVMRFYFQDKAAGNFATKCIRVSSTATTQDVIETLAEKFRPDMRMLSSPKYSLYEVHVSGERRLDIDEKPLVVQLNWNKDDREGRFVLKNENDAIPAKKAQSNGPEKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKEERPSQGDDSENSRLAAEVYKDMPETSFTRTISNPEVVMKRRRQQKLEKRMQEFRSSDGRPDSGGTLRIYADSLKPNIPYKTILLSTTDPADFAVAESLEKYGLEKENPKDYCIARVMLPPGAQHSDERGAKEIILDDDECPLQIFREWPSDKGILVFQLKRRPPDYIPKKMKKHVEGKPLKGKDRADGSGYGSALPPEKLPYLVELSPGRRNHFAYYSYHTYEDGSDSRDKPKLYRLQLSVTEVGTEKFDDNSIQLFGPGIQPHHCDLTNMDGVVTVTPRSMDAETYVDGQRISETTMLQSGMRLQFGTSHVFKFVDPIQDHVLSKRSVDGGLMVKGPRHKPGAVQETTFELGGDIHSGTALPASRSTTRLDSDRVSSASSTAERGMVKPMIRLDQEQDYRRRESRTQDAAGPELMLPASIEFRESSEDSFLSAIINYTNSSTVHFKLSPTYVLYMACRYVLSSQHRPDISPTERTHKAIAVVNKMVSMMEGVIQEVDQVDQKQKNIAGALAFWMANASELLNFIKQDRDLSRITLDAQDVLAHLVQMAFKYLVHCLQSELNNYMPAFLDDPEENSLQRPKIDDVLHTLTGAMSLLRRCRVNAALTIQLFSQLFHFINMWLFNRLVTDPDSGLCSHYWGAIIRQQLGHIEAWAEKQGLELAADCHLSRIVQATTLLTMDKYVPDDIPNINSTCFKLNSLQLQALLQNYHCAPDEPFIPTDLIENVVAVAENTADELARSDGRDVQLEEDPDLQLPFLLPEDGYSCDVVRNIPNGLQEFLDPLCQRGFCRLVPHTRSPGTWTIYFEGADYESHLMRENTELTQPLRKEPEVITVTLKKQNGMGLSIVAAKGAGQDKLGIYVKSVVKGGAADVDGRLAAGDQLLSVDGRSLVGLSQERAAELMTRTSSVVTLEVAKQGAIYHGLATLLNQPSPMMQRISDRRGSGKPRPKSEGFELYNNSAQNGSPESPQMPWTEYSEPKKLPGDDRLMKNRADHRSSPNVANQPPSPGGKSPYTSGTAAKITSVSTGNLCTEEQTPPPRPEAYPIPTQTYTREYFTFPASKSQDRMAPVQNQWPNYEEKPHMHTESDHASIAIQRVTRSQEELREEKVYQLERHRVESGMDRKCDSDMWINQSSSVESSTSSQEHLNHSSKSVTPASTLTKSGPGRWKTPAAVLPTPVAVSQPIRTDLPPPPPPPPAHYTSDFDGISMDLPLPPPPANQAAPQSAQVAAAERKKREEHQRWYEKEKARLEEERERKRREQERKLGQMRTQSLNPASFSPLATQAKPEKPSTLQRPQETVIRELQPQQQPRTIERRDLQYITISKEELSSGDSLSPDPWKRDAREKLEKQQQMHIVDMLSKEIHELQNKGDRTAEESDRLRKLMLEWQFQKRLQESKQKDEDDDEEEDDDVDTMLIMQRLEAERRARLQDEERRRQQQLEEMRKREVEDRVRQEEDGRHQEEERVKRDAEEKRRQEEGYYSRLEAERRRQHEEAARRLLEPEEPGLSRPPLPQDYEPPSQSSAPSAPPPPPQRNASYLKTQVLSPDSLFTAKFVAYDDDDEEENYVPAGPNSYSGSAGTTAGTYDAPRDTREKLSRSQDADLPGSSGAPENLTFRERQRLFSQGQDVSDKVKASRKLTELENELNTK | ||||||
Modified residue | 216 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 246 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 256 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 391 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 424 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 512 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 557 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 562 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 589 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 655 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1090 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1114 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1133 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1147 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1150 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1179 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1180 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1189 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1206 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1218 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1239 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1245 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1282 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1335 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1337 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1506 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1517 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1701 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1726 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1779 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1804 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1812 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer. Interacts with F-actin, nectin and NECTIN3. Essential for the association of nectin and E-cadherin. Isoform 2/s-afadin does not interact with F-actin. Interacts with ZO-1 and occludin, but probably in an indirect manner. Interacts with RIT1, RIT2, NRXN1 and BCR (By similarity).
Interacts with ADAM10; the interaction locks ADAM10 at adherens junctions following ADAM10 recruitment to adherens junctions by TSPAN33 (PubMed:30463011).
Interacts with ADAM10; the interaction locks ADAM10 at adherens junctions following ADAM10 recruitment to adherens junctions by TSPAN33 (PubMed:30463011).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | O35889 | Ctnna1 P26231 | 2 | EBI-6654073, EBI-647895 | |
XENO | O35889 | DBN1 Q16643 | 3 | EBI-6654073, EBI-351394 | |
XENO | O35889 | Ssx2ip Q8VC66 | 4 | EBI-6654073, EBI-6654049 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 39-133 | Ras-associating 1 | ||||
Sequence: FHGVMRFYFQDKAAGNFATKCIRVSSTATTQDVIETLAEKFRPDMRMLSSPKYSLYEVHVSGERRLDIDEKPLVVQLNWNKDDREGRFVLKNEND | ||||||
Region | 129-196 | Disordered | ||||
Sequence: KNENDAIPAKKAQSNGPEKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKEERPSQGDDSENS | ||||||
Compositional bias | 143-196 | Basic and acidic residues | ||||
Sequence: NGPEKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKEERPSQGDDSENS | ||||||
Coiled coil | 146-186 | |||||
Sequence: EKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKEER | ||||||
Domain | 246-348 | Ras-associating 2 | ||||
Sequence: SGGTLRIYADSLKPNIPYKTILLSTTDPADFAVAESLEKYGLEKENPKDYCIARVMLPPGAQHSDERGAKEIILDDDECPLQIFREWPSDKGILVFQLKRRPP | ||||||
Region | 356-377 | Disordered | ||||
Sequence: KKHVEGKPLKGKDRADGSGYGS | ||||||
Domain | 441-507 | FHA | ||||
Sequence: FGPGIQPHHCDLTNMDGVVTVTPRSMDAETYVDGQRISETTMLQSGMRLQFGTSHVFKFVDPIQDHV | ||||||
Region | 539-595 | Disordered | ||||
Sequence: DIHSGTALPASRSTTRLDSDRVSSASSTAERGMVKPMIRLDQEQDYRRRESRTQDAA | ||||||
Compositional bias | 545-568 | Polar residues | ||||
Sequence: ALPASRSTTRLDSDRVSSASSTAE | ||||||
Compositional bias | 574-593 | Basic and acidic residues | ||||
Sequence: PMIRLDQEQDYRRRESRTQD | ||||||
Domain | 668-915 | Dilute | ||||
Sequence: NKMVSMMEGVIQEVDQVDQKQKNIAGALAFWMANASELLNFIKQDRDLSRITLDAQDVLAHLVQMAFKYLVHCLQSELNNYMPAFLDDPEENSLQRPKIDDVLHTLTGAMSLLRRCRVNAALTIQLFSQLFHFINMWLFNRLVTDPDSGLCSHYWGAIIRQQLGHIEAWAEKQGLELAADCHLSRIVQATTLLTMDKYVPDDIPNINSTCFKLNSLQLQALLQNYHCAPDEPFIPTDLIENVVAVAEN | ||||||
Domain | 1014-1100 | PDZ | ||||
Sequence: VITVTLKKQNGMGLSIVAAKGAGQDKLGIYVKSVVKGGAADVDGRLAAGDQLLSVDGRSLVGLSQERAAELMTRTSSVVTLEVAKQG | ||||||
Region | 1114-1230 | Disordered | ||||
Sequence: SPMMQRISDRRGSGKPRPKSEGFELYNNSAQNGSPESPQMPWTEYSEPKKLPGDDRLMKNRADHRSSPNVANQPPSPGGKSPYTSGTAAKITSVSTGNLCTEEQTPPPRPEAYPIPT | ||||||
Compositional bias | 1137-1154 | Polar residues | ||||
Sequence: ELYNNSAQNGSPESPQMP | ||||||
Compositional bias | 1161-1176 | Basic and acidic residues | ||||
Sequence: PKKLPGDDRLMKNRAD | ||||||
Compositional bias | 1178-1216 | Polar residues | ||||
Sequence: RSSPNVANQPPSPGGKSPYTSGTAAKITSVSTGNLCTEE | ||||||
Region | 1300-1533 | Disordered | ||||
Sequence: ESGMDRKCDSDMWINQSSSVESSTSSQEHLNHSSKSVTPASTLTKSGPGRWKTPAAVLPTPVAVSQPIRTDLPPPPPPPPAHYTSDFDGISMDLPLPPPPANQAAPQSAQVAAAERKKREEHQRWYEKEKARLEEERERKRREQERKLGQMRTQSLNPASFSPLATQAKPEKPSTLQRPQETVIRELQPQQQPRTIERRDLQYITISKEELSSGDSLSPDPWKRDAREKLEKQQ | ||||||
Compositional bias | 1310-1347 | Polar residues | ||||
Sequence: DMWINQSSSVESSTSSQEHLNHSSKSVTPASTLTKSGP | ||||||
Compositional bias | 1367-1382 | Pro residues | ||||
Sequence: IRTDLPPPPPPPPAHY | ||||||
Compositional bias | 1412-1448 | Basic and acidic residues | ||||
Sequence: AAERKKREEHQRWYEKEKARLEEERERKRREQERKLG | ||||||
Coiled coil | 1417-1454 | |||||
Sequence: KREEHQRWYEKEKARLEEERERKRREQERKLGQMRTQS | ||||||
Compositional bias | 1449-1497 | Polar residues | ||||
Sequence: QMRTQSLNPASFSPLATQAKPEKPSTLQRPQETVIRELQPQQQPRTIER | ||||||
Compositional bias | 1519-1533 | Basic and acidic residues | ||||
Sequence: DPWKRDAREKLEKQQ | ||||||
Coiled coil | 1530-1564 | |||||
Sequence: EKQQQMHIVDMLSKEIHELQNKGDRTAEESDRLRK | ||||||
Region | 1574-1724 | Disordered | ||||
Sequence: RLQESKQKDEDDDEEEDDDVDTMLIMQRLEAERRARLQDEERRRQQQLEEMRKREVEDRVRQEEDGRHQEEERVKRDAEEKRRQEEGYYSRLEAERRRQHEEAARRLLEPEEPGLSRPPLPQDYEPPSQSSAPSAPPPPPQRNASYLKTQV | ||||||
Compositional bias | 1595-1685 | Basic and acidic residues | ||||
Sequence: TMLIMQRLEAERRARLQDEERRRQQQLEEMRKREVEDRVRQEEDGRHQEEERVKRDAEEKRRQEEGYYSRLEAERRRQHEEAARRLLEPEE | ||||||
Coiled coil | 1600-1672 | |||||
Sequence: QRLEAERRARLQDEERRRQQQLEEMRKREVEDRVRQEEDGRHQEEERVKRDAEEKRRQEEGYYSRLEAERRRQ | ||||||
Compositional bias | 1687-1716 | Pro residues | ||||
Sequence: GLSRPPLPQDYEPPSQSSAPSAPPPPPQRN | ||||||
Region | 1742-1829 | Disordered | ||||
Sequence: DEEENYVPAGPNSYSGSAGTTAGTYDAPRDTREKLSRSQDADLPGSSGAPENLTFRERQRLFSQGQDVSDKVKASRKLTELENELNTK | ||||||
Compositional bias | 1751-1765 | Polar residues | ||||
Sequence: GPNSYSGSAGTTAGT | ||||||
Compositional bias | 1811-1829 | Basic and acidic residues | ||||
Sequence: DKVKASRKLTELENELNTK |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O35889-1
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
- Synonymsl-afadin, p205
- Length1,829
- Mass (Da)207,678
- Last updated1998-01-01 v1
- Checksum45C597A82F109D6F
O35889-2
- Name2
- Synonymss-afadin, p190
- Differences from canonical
- 679-685: Missing
- 1609-1609: R → RQTAMPAISVLDL
- 1655-1658: RRQE → VMVL
- 1659-1829: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AL62 | A0A8I6AL62_RAT | Afdn | 1758 | ||
A0A8I5ZNL2 | A0A8I5ZNL2_RAT | Afdn | 1772 | ||
A0A8I5ZLU6 | A0A8I5ZLU6_RAT | Afdn | 1885 | ||
F1LT10 | F1LT10_RAT | Afdn | 1670 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 143-196 | Basic and acidic residues | ||||
Sequence: NGPEKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKEERPSQGDDSENS | ||||||
Compositional bias | 545-568 | Polar residues | ||||
Sequence: ALPASRSTTRLDSDRVSSASSTAE | ||||||
Compositional bias | 574-593 | Basic and acidic residues | ||||
Sequence: PMIRLDQEQDYRRRESRTQD | ||||||
Alternative sequence | VSP_011726 | 679-685 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 1137-1154 | Polar residues | ||||
Sequence: ELYNNSAQNGSPESPQMP | ||||||
Compositional bias | 1161-1176 | Basic and acidic residues | ||||
Sequence: PKKLPGDDRLMKNRAD | ||||||
Compositional bias | 1178-1216 | Polar residues | ||||
Sequence: RSSPNVANQPPSPGGKSPYTSGTAAKITSVSTGNLCTEE | ||||||
Compositional bias | 1310-1347 | Polar residues | ||||
Sequence: DMWINQSSSVESSTSSQEHLNHSSKSVTPASTLTKSGP | ||||||
Compositional bias | 1367-1382 | Pro residues | ||||
Sequence: IRTDLPPPPPPPPAHY | ||||||
Compositional bias | 1412-1448 | Basic and acidic residues | ||||
Sequence: AAERKKREEHQRWYEKEKARLEEERERKRREQERKLG | ||||||
Compositional bias | 1449-1497 | Polar residues | ||||
Sequence: QMRTQSLNPASFSPLATQAKPEKPSTLQRPQETVIRELQPQQQPRTIER | ||||||
Compositional bias | 1519-1533 | Basic and acidic residues | ||||
Sequence: DPWKRDAREKLEKQQ | ||||||
Compositional bias | 1595-1685 | Basic and acidic residues | ||||
Sequence: TMLIMQRLEAERRARLQDEERRRQQQLEEMRKREVEDRVRQEEDGRHQEEERVKRDAEEKRRQEEGYYSRLEAERRRQHEEAARRLLEPEE | ||||||
Alternative sequence | VSP_011727 | 1609 | in isoform 2 | |||
Sequence: R → RQTAMPAISVLDL | ||||||
Alternative sequence | VSP_011728 | 1655-1658 | in isoform 2 | |||
Sequence: RRQE → VMVL | ||||||
Alternative sequence | VSP_011729 | 1659-1829 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 1687-1716 | Pro residues | ||||
Sequence: GLSRPPLPQDYEPPSQSSAPSAPPPPPQRN | ||||||
Compositional bias | 1751-1765 | Polar residues | ||||
Sequence: GPNSYSGSAGTTAGT | ||||||
Compositional bias | 1811-1829 | Basic and acidic residues | ||||
Sequence: DKVKASRKLTELENELNTK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U83231 EMBL· GenBank· DDBJ | AAC53391.1 EMBL· GenBank· DDBJ | mRNA | ||
U83230 EMBL· GenBank· DDBJ | AAC53390.1 EMBL· GenBank· DDBJ | mRNA |