Q9Y653 · AGRG1_HUMAN
- ProteinAdhesion G-protein coupled receptor G1
- GeneADGRG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids693 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binding to the COL3A1 ligand inhibits neuronal migration and activates the RhoA pathway by coupling to GNA13 and possibly GNA12 (PubMed:22238662).
Plays a role in the maintenance of hematopoietic stem cells and/or leukemia stem cells in bone marrow niche (By similarity).
Plays a critical role in cancer progression by inhibiting VEGFA production threreby inhibiting angiogenesis through a signaling pathway mediated by PRKCA (PubMed:16757564, PubMed:21724588).
Plays an essential role in testis development (By similarity).
ADGRG1 N-terminal fragment
Activity regulation
Following ligand binding to the N-terminal fragment, the N-terminal fragment is released from the seven-transmembrane C-terminal fragment to unveil a new N-terminal stalk, which then stimulates G-protein-dependent signaling activity (PubMed:25918380).
The N-terminal stalk has also been shown to be dispensable for at least some G-protein-dependent signaling (PubMed:26710850).
Features
Showing features for binding site, site.
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAdhesion G-protein coupled receptor G1
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y653
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
ADGRG1 N-terminal fragment
ADGRG1 C-terminal fragment
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 26-402 | Extracellular | ||||
Sequence: RGHREDFRFCSQRNQTHRSSLHYKPTPDLRISIENSEEALTVHAPFPAAHPASRSFPDPRGLYHFCLYWNRHAGRLHLLYGKRDFLLSDKASSLLCFQHQEESLAQGPPLLATSVTSWWSPQNISLPSAASFTFSFHSPPHTAAHNASVDMCELKRDLQLLSQFLKHPQKASRRPSAAPASQQLQSLESKLTSVRFMGDMVSFEEDRINATVWKLQPTAGLQDLHIHSRQEEEQSEIMEYSVLLPRTLFQRTKGRSGEAEKRLLLVDFSSQALFQDKNSSQVLGEKVLGIVVQNTKVANLTEPVVLTFQHQLQPKNVTLQCVFWVEDPTLSSPGHWSSAGCETVRRETQTSCFCNHLTYFAVLMVSSVEVDAVHKHY | ||||||
Transmembrane | 403-423 | Helical; Name=1 | ||||
Sequence: LSLLSYVGCVVSALACLVTIA | ||||||
Topological domain | 424-448 | Cytoplasmic | ||||
Sequence: AYLCSRVPLPCRRKPRDYTIKVHMN | ||||||
Transmembrane | 449-469 | Helical; Name=2 | ||||
Sequence: LLLAVFLLDTSFLLSEPVALT | ||||||
Topological domain | 470-476 | Extracellular | ||||
Sequence: GSEAGCR | ||||||
Transmembrane | 477-497 | Helical; Name=3 | ||||
Sequence: ASAIFLHFSLLTCLSWMGLEG | ||||||
Topological domain | 498-518 | Cytoplasmic | ||||
Sequence: YNLYRLVVEVFGTYVPGYLLK | ||||||
Transmembrane | 519-539 | Helical; Name=4 | ||||
Sequence: LSAMGWGFPIFLVTLVALVDV | ||||||
Topological domain | 540-576 | Extracellular | ||||
Sequence: DNYGPIILAVHRTPEGVIYPSMCWIRDSLVSYITNLG | ||||||
Transmembrane | 577-597 | Helical; Name=5 | ||||
Sequence: LFSLVFLFNMAMLATMVVQIL | ||||||
Topological domain | 598-609 | Cytoplasmic | ||||
Sequence: RLRPHTQKWSHV | ||||||
Transmembrane | 610-630 | Helical; Name=6 | ||||
Sequence: LTLLGLSLVLGLPWALIFFSF | ||||||
Topological domain | 631-636 | Extracellular | ||||
Sequence: ASGTFQ | ||||||
Transmembrane | 637-657 | Helical; Name=7 | ||||
Sequence: LVVLYLFSIITSFQGFLIFIW | ||||||
Topological domain | 658-693 | Cytoplasmic | ||||
Sequence: YWSMRLQARGGPSPLKSNSDSARLPISSGSTSSSRI |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cortical dysplasia, complex, with other brain malformations 14A (bilateral frontoparietal) (CDCBM14A)
- Note
- DescriptionAn autosomal recessive disorder characterized by global developmental delay with impaired intellectual development, motor delay, poor speech, cerebellar and pyramidal signs, truncal ataxia, and early-onset seizures. Brain imaging shows bilateral frontoparietal polymicrogyria, a malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. Polymicrogyria is considered to be the result of postmigratory abnormal cortical organization.
- See alsoMIM:606854
Natural variants in CDCBM14A
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_069581 | 38 | R>Q | in CDCBM14A; abolishes interaction with COL3A1; dbSNP:rs764367185 | |
VAR_026242 | 38 | R>W | in CDCBM14A; abolishes interaction with COL3A1; reduces cell surface localization; dbSNP:rs121908462 | |
VAR_026243 | 88 | Y>C | in CDCBM14A; abolishes interaction with COL3A1; reduces cell surface localization; dbSNP:rs121908466 | |
VAR_026244 | 91 | C>S | in CDCBM14A; abolishes interaction with COL3A1; reduces cell surface localization; dbSNP:rs121908465 | |
VAR_026245 | 346 | C>S | in CDCBM14A; abolishes autoproteolytic cleavage; reduces cell surface localization; dbSNP:rs121908463 | |
VAR_069582 | 349 | W>S | in CDCBM14A; abolishes autoproteolytic cleavage; reduces cell surface localization | |
VAR_069583 | 496 | E>K | in CDCBM14A; reduces cell surface localization; dbSNP:rs556518689 | |
VAR_026246 | 565 | R>W | in CDCBM14A; reduces cell surface localization; dbSNP:rs121908464 | |
VAR_069584 | 640 | L>R | in CDCBM14A; unclear effects on cell surface localization; blocks downstream RhoA activation |
Cortical dysplasia, complex, with other brain malformations 14B (bilateral perisylvian) (CDCBM14B)
- Note
- DescriptionAn autosomal recessive disorder characterized by strikingly restricted polymicrogyria limited to the cortex surrounding the Sylvian fissure. Affected individuals have intellectual and language difficulty and seizures, but no motor disability. Polymicrogyria is a malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. It is considered to be the result of postmigratory abnormal cortical organization.
- See alsoMIM:615752
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 28 | Abolishes heparin-binding; when associated with A-29 and A-33. | ||||
Sequence: H → A | ||||||
Mutagenesis | 29 | Abolishes heparin-binding; when associated with A-28 and A-33. | ||||
Sequence: R → A | ||||||
Mutagenesis | 33 | Reduces heparin-binding. Abolishes heparin-binding; when associated with A-28 and A-29. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_069581 | 38 | in CDCBM14A; abolishes interaction with COL3A1; dbSNP:rs764367185 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_026242 | 38 | in CDCBM14A; abolishes interaction with COL3A1; reduces cell surface localization; dbSNP:rs121908462 | |||
Sequence: R → W | ||||||
Natural variant | VAR_026243 | 88 | in CDCBM14A; abolishes interaction with COL3A1; reduces cell surface localization; dbSNP:rs121908466 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_026244 | 91 | in CDCBM14A; abolishes interaction with COL3A1; reduces cell surface localization; dbSNP:rs121908465 | |||
Sequence: C → S | ||||||
Natural variant | VAR_017910 | 281 | in dbSNP:rs1801257 | |||
Sequence: S → R | ||||||
Natural variant | VAR_017911 | 306 | in dbSNP:rs1801255 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_026245 | 346 | in CDCBM14A; abolishes autoproteolytic cleavage; reduces cell surface localization; dbSNP:rs121908463 | |||
Sequence: C → S | ||||||
Natural variant | VAR_069582 | 349 | in CDCBM14A; abolishes autoproteolytic cleavage; reduces cell surface localization | |||
Sequence: W → S | ||||||
Mutagenesis | 381 | Abolishes cleavage. | ||||
Sequence: H → S | ||||||
Mutagenesis | 383 | Abolishes cleavage but does not affect cell membrane localization or signaling activity. | ||||
Sequence: T → G | ||||||
Natural variant | VAR_049457 | 493 | in dbSNP:rs17379472 | |||
Sequence: M → T | ||||||
Natural variant | VAR_069583 | 496 | in CDCBM14A; reduces cell surface localization; dbSNP:rs556518689 | |||
Sequence: E → K | ||||||
Natural variant | VAR_049458 | 527 | in dbSNP:rs16958679 | |||
Sequence: P → L | ||||||
Natural variant | VAR_026246 | 565 | in CDCBM14A; reduces cell surface localization; dbSNP:rs121908464 | |||
Sequence: R → W | ||||||
Natural variant | VAR_069584 | 640 | in CDCBM14A; unclear effects on cell surface localization; blocks downstream RhoA activation | |||
Sequence: L → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 906 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue (large scale data), disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-25 | UniProt | |||||
Sequence: MTPQSLLQTTLFLLSLLFLVQGAHG | |||||||
Chain | PRO_0000423086 | 26-?382 | UniProt | ADGRG1 N-terminal fragment | |||
Sequence: RGHREDFRFCSQRNQTHRSSLHYKPTPDLRISIENSEEALTVHAPFPAAHPASRSFPDPRGLYHFCLYWNRHAGRLHLLYGKRDFLLSDKASSLLCFQHQEESLAQGPPLLATSVTSWWSPQNISLPSAASFTFSFHSPPHTAAHNASVDMCELKRDLQLLSQFLKHPQKASRRPSAAPASQQLQSLESKLTSVRFMGDMVSFEEDRINATVWKLQPTAGLQDLHIHSRQEEEQSEIMEYSVLLPRTLFQRTKGRSGEAEKRLLLVDFSSQALFQDKNSSQVLGEKVLGIVVQNTKVANLTEPVVLTFQHQLQPKNVTLQCVFWVEDPTLSSPGHWSSAGCETVRRETQTSCFCNHL | |||||||
Chain | PRO_0000012880 | 26-693 | UniProt | Adhesion G-protein coupled receptor G1 | |||
Sequence: RGHREDFRFCSQRNQTHRSSLHYKPTPDLRISIENSEEALTVHAPFPAAHPASRSFPDPRGLYHFCLYWNRHAGRLHLLYGKRDFLLSDKASSLLCFQHQEESLAQGPPLLATSVTSWWSPQNISLPSAASFTFSFHSPPHTAAHNASVDMCELKRDLQLLSQFLKHPQKASRRPSAAPASQQLQSLESKLTSVRFMGDMVSFEEDRINATVWKLQPTAGLQDLHIHSRQEEEQSEIMEYSVLLPRTLFQRTKGRSGEAEKRLLLVDFSSQALFQDKNSSQVLGEKVLGIVVQNTKVANLTEPVVLTFQHQLQPKNVTLQCVFWVEDPTLSSPGHWSSAGCETVRRETQTSCFCNHLTYFAVLMVSSVEVDAVHKHYLSLLSYVGCVVSALACLVTIAAYLCSRVPLPCRRKPRDYTIKVHMNLLLAVFLLDTSFLLSEPVALTGSEAGCRASAIFLHFSLLTCLSWMGLEGYNLYRLVVEVFGTYVPGYLLKLSAMGWGFPIFLVTLVALVDVDNYGPIILAVHRTPEGVIYPSMCWIRDSLVSYITNLGLFSLVFLFNMAMLATMVVQILRLRPHTQKWSHVLTLLGLSLVLGLPWALIFFSFASGTFQLVVLYLFSIITSFQGFLIFIWYWSMRLQARGGPSPLKSNSDSARLPISSGSTSSSRI | |||||||
Glycosylation | 39 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 148 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 171 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 201 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 234 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 303 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 324 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 341 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 346↔377 | UniProt | |||||
Sequence: CVFWVEDPTLSSPGHWSSAGCETVRRETQTSC | |||||||
Disulfide bond | 366↔379 | UniProt | |||||
Sequence: CETVRRETQTSCFC | |||||||
Chain | PRO_0000423087 | ?383-693 | UniProt | ADGRG1 C-terminal fragment | |||
Sequence: TYFAVLMVSSVEVDAVHKHYLSLLSYVGCVVSALACLVTIAAYLCSRVPLPCRRKPRDYTIKVHMNLLLAVFLLDTSFLLSEPVALTGSEAGCRASAIFLHFSLLTCLSWMGLEGYNLYRLVVEVFGTYVPGYLLKLSAMGWGFPIFLVTLVALVDVDNYGPIILAVHRTPEGVIYPSMCWIRDSLVSYITNLGLFSLVFLFNMAMLATMVVQILRLRPHTQKWSHVLTLLGLSLVLGLPWALIFFSFASGTFQLVVLYLFSIITSFQGFLIFIWYWSMRLQARGGPSPLKSNSDSARLPISSGSTSSSRI | |||||||
Modified residue (large scale data) | 670 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 676 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 678 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 684 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 685 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 687 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 688 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 689 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 690 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 691 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Part of a GPCR-tetraspanin complex at least consisting of ADGRG1, CD81, eventually CD9, and GNA11 in which CD81 is enhancing the association of ADGRG1 with GNA11. Interacts with heparin; leading to the reduction of ADGRG1 shedding (PubMed:27068534).
Interacts with COL3A1 (PubMed:28258187).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 224-395 | GAIN-B | ||||
Sequence: DMVSFEEDRINATVWKLQPTAGLQDLHIHSRQEEEQSEIMEYSVLLPRTLFQRTKGRSGEAEKRLLLVDFSSQALFQDKNSSQVLGEKVLGIVVQNTKVANLTEPVVLTFQHQLQPKNVTLQCVFWVEDPTLSSPGHWSSAGCETVRRETQTSCFCNHLTYFAVLMVSSVEV | ||||||
Region | 346-395 | GPS | ||||
Sequence: CVFWVEDPTLSSPGHWSSAGCETVRRETQTSCFCNHLTYFAVLMVSSVEV | ||||||
Region | 670-693 | Disordered | ||||
Sequence: SPLKSNSDSARLPISSGSTSSSRI |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group 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.
Q9Y653-1
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
- Length693
- Mass (Da)77,738
- Last updated2004-03-15 v2
- Checksum801C8E62666A5155
Q9Y653-2
- Name2
- SynonymsS1
- Differences from canonical
- 429-434: Missing
Q9Y653-3
- Name3
- SynonymsS2
Q9Y653-4
- Name4
- SynonymsS3
- Differences from canonical
- 38-207: Missing
Q9Y653-5
- Name5
- SynonymsS4
- NoteHas no predictable signal peptide.
- Differences from canonical
- 1-175: Missing
Computationally mapped potential isoform sequences
There are 48 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BV72 | H3BV72_HUMAN | ADGRG1 | 110 | ||
H3BV84 | H3BV84_HUMAN | ADGRG1 | 68 | ||
H3BUU6 | H3BUU6_HUMAN | ADGRG1 | 164 | ||
H3BV52 | H3BV52_HUMAN | ADGRG1 | 199 | ||
H3BVA0 | H3BVA0_HUMAN | ADGRG1 | 144 | ||
H3BVD3 | H3BVD3_HUMAN | ADGRG1 | 162 | ||
H3BVE9 | H3BVE9_HUMAN | ADGRG1 | 84 | ||
H3BTK9 | H3BTK9_HUMAN | ADGRG1 | 100 | ||
H3BTH7 | H3BTH7_HUMAN | ADGRG1 | 153 | ||
H3BUH2 | H3BUH2_HUMAN | ADGRG1 | 122 | ||
H3BUF5 | H3BUF5_HUMAN | ADGRG1 | 97 | ||
H3BSR1 | H3BSR1_HUMAN | ADGRG1 | 77 | ||
H3BSP5 | H3BSP5_HUMAN | ADGRG1 | 103 | ||
H3BSN3 | H3BSN3_HUMAN | ADGRG1 | 49 | ||
H3BSN7 | H3BSN7_HUMAN | ADGRG1 | 107 | ||
H3BSJ6 | H3BSJ6_HUMAN | ADGRG1 | 187 | ||
H3BSF7 | H3BSF7_HUMAN | ADGRG1 | 125 | ||
H3BTD2 | H3BTD2_HUMAN | ADGRG1 | 56 | ||
H3BT88 | H3BT88_HUMAN | ADGRG1 | 113 | ||
H3BS14 | H3BS14_HUMAN | ADGRG1 | 42 | ||
H3BRH0 | H3BRH0_HUMAN | ADGRG1 | 256 | ||
H3BRI2 | H3BRI2_HUMAN | ADGRG1 | 118 | ||
H3BRI7 | H3BRI7_HUMAN | ADGRG1 | 154 | ||
H3BSB8 | H3BSB8_HUMAN | ADGRG1 | 116 | ||
H3BRZ4 | H3BRZ4_HUMAN | ADGRG1 | 140 | ||
H3BS98 | H3BS98_HUMAN | ADGRG1 | 90 | ||
H3BS94 | H3BS94_HUMAN | ADGRG1 | 131 | ||
H3BS54 | H3BS54_HUMAN | ADGRG1 | 118 | ||
H3BQJ9 | H3BQJ9_HUMAN | ADGRG1 | 90 | ||
H3BRA1 | H3BRA1_HUMAN | ADGRG1 | 111 | ||
H3BRB4 | H3BRB4_HUMAN | ADGRG1 | 70 | ||
H3BQZ1 | H3BQZ1_HUMAN | ADGRG1 | 159 | ||
H3BQW4 | H3BQW4_HUMAN | ADGRG1 | 54 | ||
H3BPC0 | H3BPC0_HUMAN | ADGRG1 | 97 | ||
H3BPA6 | H3BPA6_HUMAN | ADGRG1 | 98 | ||
H3BQ11 | H3BQ11_HUMAN | ADGRG1 | 95 | ||
H3BQ46 | H3BQ46_HUMAN | ADGRG1 | 167 | ||
H3BP94 | H3BP94_HUMAN | ADGRG1 | 78 | ||
H3BP67 | H3BP67_HUMAN | ADGRG1 | 168 | ||
H3BNH4 | H3BNH4_HUMAN | ADGRG1 | 198 | ||
H3BNN3 | H3BNN3_HUMAN | ADGRG1 | 94 | ||
H3BMC2 | H3BMC2_HUMAN | ADGRG1 | 81 | ||
H3BMF8 | H3BMF8_HUMAN | ADGRG1 | 119 | ||
H3BMY9 | H3BMY9_HUMAN | ADGRG1 | 146 | ||
H3BM73 | H3BM73_HUMAN | ADGRG1 | 125 | ||
A0A1B0GX62 | A0A1B0GX62_HUMAN | ADGRG1 | 118 | ||
A0A5F9ZHT7 | A0A5F9ZHT7_HUMAN | ADGRG1 | 670 | ||
A0A5F9ZH94 | A0A5F9ZH94_HUMAN | ADGRG1 | 690 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047554 | 1-175 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047555 | 21 | in isoform 3 | |||
Sequence: Q → QASASS | ||||||
Alternative sequence | VSP_047556 | 38-207 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 329 | in Ref. 8 | ||||
Sequence: V → A | ||||||
Alternative sequence | VSP_035068 | 429-434 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 561 | in Ref. 5; BAD18684 | ||||
Sequence: M → R | ||||||
Sequence conflict | 678 | in Ref. 1; AAD30545 | ||||
Sequence: S → C |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF106858 EMBL· GenBank· DDBJ | AAD30545.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ011001 EMBL· GenBank· DDBJ | CAB37294.1 EMBL· GenBank· DDBJ | mRNA | ||
EU432119 EMBL· GenBank· DDBJ | ABY87918.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358400 EMBL· GenBank· DDBJ | AAQ88766.1 EMBL· GenBank· DDBJ | mRNA | ||
AK131550 EMBL· GenBank· DDBJ | BAD18684.1 EMBL· GenBank· DDBJ | mRNA | ||
AK299110 EMBL· GenBank· DDBJ | BAG61166.1 EMBL· GenBank· DDBJ | mRNA | ||
AB065909 EMBL· GenBank· DDBJ | BAC06124.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT007311 EMBL· GenBank· DDBJ | AAP35975.1 EMBL· GenBank· DDBJ | mRNA | ||
CR936747 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AC018552 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471092 EMBL· GenBank· DDBJ | EAW82939.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471092 EMBL· GenBank· DDBJ | EAW82940.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC008770 EMBL· GenBank· DDBJ | AAH08770.1 EMBL· GenBank· DDBJ | mRNA |