P48356 · LEPR_MOUSE
- ProteinLeptin receptor
- GeneLepr
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1162 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
On ligand binding, mediates LEP central and peripheral effects through the activation of different signaling pathways such as JAK2/STAT3 and MAPK cascade/FOS (PubMed:10799542, PubMed:11861497, PubMed:11923481, PubMed:25383904).
In the hypothalamus, LEP acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones (PubMed:10660043, PubMed:12594516).
In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic and affects innate and adaptive immunity (PubMed:11923481, PubMed:25383904).
Control of energy homeostasis and melanocortin production (stimulation of POMC and full repression of AgRP transcription) is mediated by STAT3 signaling, whereas distinct signals regulate NPY and the control of fertility, growth and glucose homeostasis (PubMed:12594516).
Involved in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus (PubMed:25383904).
Has a specific effect on T lymphocyte responses, differentially regulating the proliferation of naive and memory T-cells. Leptin increases Th1 and suppresses Th2 cytokine production (PubMed:9732873).
Isoform A
Does not induce phosphorylation of and activate STAT3 (PubMed:11923481, PubMed:20223942).
Isoform E
GO annotations
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameLeptin receptor
- Short namesLEP-R
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP48356
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform E
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 22-839 | Extracellular | ||||
Sequence: LNLAYPISPWKFKLFCGPPNTTDDSFLSPAGAPNNASALKGASEAIVEAKFNSSGIYVPELSKTVFHCCFGNEQGQNCSALTDNTEGKTLASVVKASVFRQLGVNWDIECWMKGDLTLFICHMEPLPKNPFKNYDSKVHLLYDLPEVIDDSPLPPLKDSFQTVQCNCSLRGCECHVPVPRAKLNYALLMYLEITSAGVSFQSPLMSLQPMLVVKPDPPLGLHMEVTDDGNLKISWDSQTMAPFPLQYQVKYLENSTIVREAAEIVSATSLLVDSVLPGSSYEVQVRSKRLDGSGVWSDWSSPQVFTTQDVVYFPPKILTSVGSNASFHCIYKNENQIISSKQIVWWRNLAEKIPEIQYSIVSDRVSKVTFSNLKATRPRGKFTYDAVYCCNEQACHHRYAELYVIDVNINISCETDGYLTKMTCRWSPSTIQSLVGSTVQLRYHRRSLYCPDSPSIHPTSEPKNCVLQRDGFYECVFQPIFLLSGYTMWIRINHSLGSLDSPPTCVLPDSVVKPLPPSNVKAEITVNTGLLKVSWEKPVFPENNLQFQIRYGLSGKEIQWKTHEVFDAKSKSASLLVSDLCAVYVVQVRCRRLDGLGYWSNWSSPAYTLVMDVKVPMRGPEFWRKMDGDVTKKERNVTLLWKPLTKNDSLCSVRRYVVKHRTAHNGTWSEDVGNRTNLTFLWTEPAHTVTVLAVNSLGASLVNFNLTFSWPMSKVSAVESLSAYPLSSSCVILSWTLSPDDYSLLYLVIEWKILNEDDGMKWLRIPSNVKKFYIHDNFIPIEKYQFSLYPVFMEGVGKPKIINGFTKDAIDKQQNDAG | ||||||
Transmembrane | 840-860 | Helical | ||||
Sequence: LYVIVPIIISSCVLLLGTLLI | ||||||
Topological domain | 861-1162 | Cytoplasmic | ||||
Sequence: SHQRMKKLFWDDVPNPKNCSWAQGLNFQKPETFEHLFTKHAESVIFGPLLLEPEPISEEISVDTAWKNKDEMVPAAMVSLLLTTPDPESSSICISDQCNSANFSGSQSTQVTCEDECQRQPSVKYATLVSNDKLVETDEEQGFIHSPVSNCISSNHSPLRQSFSSSSWETEAQTFFLLSDQQPTMISPQLSFSGLDELLELEGSFPEENHREKSVCYLGVTSVNRRESGVLLTGEAGILCTFPAQCLFSDIRILQERCSHFVENNLSLGTSGENFVPYMPQFQTCSTHSHKIMENKMCDLTV |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Have wet brain weight significantly lower than controls. Brain uptake of leptin is also reduced (PubMed:11861497).
Animals have an increased bone formation leading to high bone mass (PubMed:10660043).
Have impaired T-cell immunity, Th2 responses are favoured in mutants (PubMed:9732873).
Conditional knockout in parabrachial nucleus CCK-expressing neurons, treated with 2-deoxyglucose, have increased levels of glucagon, corticosterone and epinephrin concentrations compared to wild-types (PubMed:25383904).
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 541 | in strain: NZO | ||||
Sequence: V → I | ||||||
Natural variant | 600 | in strain: KKObese | ||||
Sequence: D → N | ||||||
Natural variant | 651 | in strain: NZO | ||||
Sequence: V → I | ||||||
Mutagenesis | 891 | No effect on STAT3 phosphorylation. | ||||
Sequence: E → A | ||||||
Mutagenesis | 894 | No effect on STAT3 phosphorylation. | ||||
Sequence: E → A | ||||||
Mutagenesis | 896-897 | Abrogates STAT3 phosphorylation. | ||||
Sequence: LF → AA | ||||||
Mutagenesis | 899-900 | No effect on STAT3 phosphorylation. | ||||
Sequence: KH → AA | ||||||
Mutagenesis | 902 | No effect on STAT3 phosphorylation. | ||||
Sequence: E → A | ||||||
Mutagenesis | 908 | No effect on STAT3 phosphorylation. | ||||
Sequence: P → A | ||||||
Mutagenesis | 985 | No change in EPO-induced JAK2 activation and EPO-induced tyrosine phosphorylation. No phosphorylation; when associated with S-1138. No phosphorylation; when associated with both S-1138 and F-1077. No change in STAT3 activation. No PTPN11 binding. No SOCS3 binding nor inhibition of signaling. Greatly reduced ERK/FOS activation. Mutants are hyperphagic, obese and hyperglycaemic, females show a defect in lactation. | ||||
Sequence: Y → L | ||||||
Natural variant | 1044 | in strain: NZO | ||||
Sequence: T → I | ||||||
Mutagenesis | 1077 | No effect on EPO-induced tyrosine phosphorylation. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1138 | No change in EPO-induced JAK2 activation and EPO-induced tyrosine phosphorylation. No phosphorylation; when associated with L-985. No phosphorylation; when associated with L-985 and F-1077. No STAT3 activation. No change in SOCS3 binding nor signaling inhibition. No effect on ERK/FOS activation. | ||||
Sequence: Y → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 59 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Chemistry
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MMCQKFYVVLLHWEFLYVIAA | ||||||
Chain | PRO_0000010906 | 22-1162 | Leptin receptor | |||
Sequence: LNLAYPISPWKFKLFCGPPNTTDDSFLSPAGAPNNASALKGASEAIVEAKFNSSGIYVPELSKTVFHCCFGNEQGQNCSALTDNTEGKTLASVVKASVFRQLGVNWDIECWMKGDLTLFICHMEPLPKNPFKNYDSKVHLLYDLPEVIDDSPLPPLKDSFQTVQCNCSLRGCECHVPVPRAKLNYALLMYLEITSAGVSFQSPLMSLQPMLVVKPDPPLGLHMEVTDDGNLKISWDSQTMAPFPLQYQVKYLENSTIVREAAEIVSATSLLVDSVLPGSSYEVQVRSKRLDGSGVWSDWSSPQVFTTQDVVYFPPKILTSVGSNASFHCIYKNENQIISSKQIVWWRNLAEKIPEIQYSIVSDRVSKVTFSNLKATRPRGKFTYDAVYCCNEQACHHRYAELYVIDVNINISCETDGYLTKMTCRWSPSTIQSLVGSTVQLRYHRRSLYCPDSPSIHPTSEPKNCVLQRDGFYECVFQPIFLLSGYTMWIRINHSLGSLDSPPTCVLPDSVVKPLPPSNVKAEITVNTGLLKVSWEKPVFPENNLQFQIRYGLSGKEIQWKTHEVFDAKSKSASLLVSDLCAVYVVQVRCRRLDGLGYWSNWSSPAYTLVMDVKVPMRGPEFWRKMDGDVTKKERNVTLLWKPLTKNDSLCSVRRYVVKHRTAHNGTWSEDVGNRTNLTFLWTEPAHTVTVLAVNSLGASLVNFNLTFSWPMSKVSAVESLSAYPLSSSCVILSWTLSPDDYSLLYLVIEWKILNEDDGMKWLRIPSNVKKFYIHDNFIPIEKYQFSLYPVFMEGVGKPKIINGFTKDAIDKQQNDAGLYVIVPIIISSCVLLLGTLLISHQRMKKLFWDDVPNPKNCSWAQGLNFQKPETFEHLFTKHAESVIFGPLLLEPEPISEEISVDTAWKNKDEMVPAAMVSLLLTTPDPESSSICISDQCNSANFSGSQSTQVTCEDECQRQPSVKYATLVSNDKLVETDEEQGFIHSPVSNCISSNHSPLRQSFSSSSWETEAQTFFLLSDQQPTMISPQLSFSGLDELLELEGSFPEENHREKSVCYLGVTSVNRRESGVLLTGEAGILCTFPAQCLFSDIRILQERCSHFVENNLSLGTSGENFVPYMPQFQTCSTHSHKIMENKMCDLTV | ||||||
Disulfide bond | 37↔90 | |||||
Sequence: CGPPNTTDDSFLSPAGAPNNASALKGASEAIVEAKFNSSGIYVPELSKTVFHCC | ||||||
Glycosylation | 41 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 56 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 73 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 89↔99 | |||||
Sequence: CCFGNEQGQNC | ||||||
Glycosylation | 98 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 131↔142 | |||||
Sequence: CWMKGDLTLFIC | ||||||
Disulfide bond | 186↔195 | |||||
Sequence: CNCSLRGCEC | ||||||
Glycosylation | 187 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 188↔193 | |||||
Sequence: CSLRGC | ||||||
Glycosylation | 275 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 345 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 350↔410 | |||||
Sequence: CIYKNENQIISSKQIVWWRNLAEKIPEIQYSIVSDRVSKVTFSNLKATRPRGKFTYDAVYC | ||||||
Disulfide bond | 411↔416 | |||||
Sequence: CNEQAC | ||||||
Glycosylation | 431 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 434↔445 | |||||
Sequence: CETDGYLTKMTC | ||||||
Disulfide bond | 471↔526 | |||||
Sequence: CPDSPSIHPTSEPKNCVLQRDGFYECVFQPIFLLSGYTMWIRINHSLGSLDSPPTC | ||||||
Disulfide bond | 486↔496 | |||||
Sequence: CVLQRDGFYEC | ||||||
Glycosylation | 514 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 622 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 657 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 668 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 686 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 695 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 698 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 726 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 880 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 985 | Phosphotyrosine; by JAK2 | ||||
Sequence: Y | ||||||
Modified residue | 1077 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1138 | Phosphotyrosine; by JAK2 | ||||
Sequence: Y |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed by peripheral blood mononuclear cells and CD4+ T-cells (PubMed:9732873).
Isoform E: expressed in adipose tissue, liver, hypothalamus, cerebral microvessels, heart, and testes (PubMed:17620316).
Gene expression databases
Interaction
Subunit
Interaction with SOCS3 inhibits JAK/STAT signaling and MAPK cascade (PubMed:11018044).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P48356 | Jak2 Q62120 | 3 | EBI-2257257, EBI-646604 | |
BINARY | P48356 | Lep P41160 | 6 | EBI-2257257, EBI-16108810 | |
BINARY | P48356 | Lrp1 Q91ZX7 | 2 | EBI-2257257, EBI-300955 | |
BINARY | P48356 | Plcg1 Q62077 | 2 | EBI-2257257, EBI-300133 | |
XENO | P48356-1 | BBS1 Q8NFJ9 | 3 | EBI-6143588, EBI-1805484 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 238-331 | Fibronectin type-III 1 | ||||
Sequence: PPLGLHMEVTDDGNLKISWDSQTMAPFPLQYQVKYLENSTIVREAAEIVSATSLLVDSVLPGSSYEVQVRSKRLDGSGVWSDWSSPQVFTTQDV | ||||||
Domain | 329-427 | Ig-like | ||||
Sequence: QDVVYFPPKILTSVGSNASFHCIYKNENQIISSKQIVWWRNLAEKIPEIQYSIVSDRVSKVTFSNLKATRPRGKFTYDAVYCCNEQACHHRYAELYVID | ||||||
Region | 465-482 | Leptin-binding | ||||
Sequence: HRRSLYCPDSPSIHPTSE | ||||||
Domain | 537-632 | Fibronectin type-III 2 | ||||
Sequence: PPSNVKAEITVNTGLLKVSWEKPVFPENNLQFQIRYGLSGKEIQWKTHEVFDAKSKSASLLVSDLCAVYVVQVRCRRLDGLGYWSNWSSPAYTLVM | ||||||
Motif | 620-624 | WSXWS motif | ||||
Sequence: WSNWS | ||||||
Domain | 637-729 | Fibronectin type-III 3 | ||||
Sequence: PMRGPEFWRKMDGDVTKKERNVTLLWKPLTKNDSLCSVRRYVVKHRTAHNGTWSEDVGNRTNLTFLWTEPAHTVTVLAVNSLGASLVNFNLTF | ||||||
Domain | 738-832 | Fibronectin type-III 4 | ||||
Sequence: AVESLSAYPLSSSCVILSWTLSPDDYSLLYLVIEWKILNEDDGMKWLRIPSNVKKFYIHDNFIPIEKYQFSLYPVFMEGVGKPKIINGFTKDAID | ||||||
Motif | 869-877 | Box 1 motif | ||||
Sequence: FWDDVPNPK | ||||||
Region | 891-896 | Required for JAK2 activation | ||||
Sequence: ETFEHL | ||||||
Region | 896-904 | Required for STAT3 phosphorylation | ||||
Sequence: LFTKHAESV |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 5 isoforms produced by Alternative splicing.
P48356-1
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.
- NameB
- Length1,162
- Mass (Da)130,789
- Last updated1996-02-01 v1
- Checksum0E1E75B076BA60A2
P48356-2
- NameA
P48356-3
- NameC
P48356-4
- NameD
P48356-5
- NameE
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A2AV66 | A2AV66_MOUSE | Lepr | 30 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 140 | in Ref. 5; AAC52705/AAC52706/AAC52707 | ||||
Sequence: F → I | ||||||
Sequence conflict | 720 | in Ref. 6; CAA71343 | ||||
Sequence: A → T | ||||||
Alternative sequence | VSP_001703 | 797-805 | in isoform E | |||
Sequence: DNFIPIEKY → GMCTVLFMD | ||||||
Alternative sequence | VSP_001704 | 806-1162 | in isoform E | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_001699 | 890-892 | in isoform C | |||
Sequence: PET → VTV | ||||||
Alternative sequence | VSP_001697 | 890-894 | in isoform A | |||
Sequence: PETFE → RTDTL | ||||||
Alternative sequence | VSP_001701 | 890-900 | in isoform D | |||
Sequence: PETFEHLFTKH → DISFHEVFIFR | ||||||
Alternative sequence | VSP_001700 | 893-1162 | in isoform C | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_001698 | 895-1162 | in isoform A | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_001702 | 901-1162 | in isoform D | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U42467 EMBL· GenBank· DDBJ | AAA93014.1 EMBL· GenBank· DDBJ | mRNA | ||
U46135 EMBL· GenBank· DDBJ | AAC52408.1 EMBL· GenBank· DDBJ | mRNA | ||
U49106 EMBL· GenBank· DDBJ | AAC52420.1 EMBL· GenBank· DDBJ | mRNA | ||
U49107 EMBL· GenBank· DDBJ | AAC52421.1 EMBL· GenBank· DDBJ | mRNA | ||
U49108 EMBL· GenBank· DDBJ | AAC52422.1 EMBL· GenBank· DDBJ | mRNA | ||
U49109 EMBL· GenBank· DDBJ | AAC52423.1 EMBL· GenBank· DDBJ | mRNA | ||
U49110 EMBL· GenBank· DDBJ | AAC52424.1 EMBL· GenBank· DDBJ | mRNA | ||
U52915 EMBL· GenBank· DDBJ | AAC52599.1 EMBL· GenBank· DDBJ | mRNA | ||
U58861 EMBL· GenBank· DDBJ | AAC52705.1 EMBL· GenBank· DDBJ | mRNA | ||
U58862 EMBL· GenBank· DDBJ | AAC52706.1 EMBL· GenBank· DDBJ | mRNA | ||
U58863 EMBL· GenBank· DDBJ | AAC52707.1 EMBL· GenBank· DDBJ | mRNA | ||
Y10298 EMBL· GenBank· DDBJ | CAA71343.1 EMBL· GenBank· DDBJ | mRNA | ||
AF039456 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039443 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039444 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039445 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039446 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039447 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039448 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039449 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039450 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039451 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039452 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039453 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039454 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039455 EMBL· GenBank· DDBJ | AAB95334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039461 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039443 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039444 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039445 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039446 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039447 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039448 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039449 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039450 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039451 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039452 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039453 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039454 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039455 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039456 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039457 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039458 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039459 EMBL· GenBank· DDBJ | AAB95333.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
AF039459 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039443 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039444 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039445 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039446 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039447 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039448 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039449 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039450 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039451 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039452 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039453 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039454 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039455 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039456 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039457 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039458 EMBL· GenBank· DDBJ | AAB95335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039460 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039443 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039444 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039445 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039446 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039447 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039448 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039449 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039450 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039451 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039452 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039453 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039454 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039455 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039456 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039457 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039458 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039459 EMBL· GenBank· DDBJ | AAB95332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y10296 EMBL· GenBank· DDBJ | CAA71342.1 EMBL· GenBank· DDBJ | mRNA | ||
AF098792 EMBL· GenBank· DDBJ | AAD13218.1 EMBL· GenBank· DDBJ | Genomic DNA |