P35348 · ADA1A_HUMAN
- ProteinAlpha-1A adrenergic receptor
- GeneADRA1A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids466 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G11 proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes.
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
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-1A adrenergic receptor
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP35348
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Nucleus membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Note: Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-27 | Extracellular | ||||
Sequence: MVFLSGNASDSSNCTQPPAPVNISKAI | ||||||
Transmembrane | 28-51 | Helical; Name=1 | ||||
Sequence: LLGVILGGLILFGVLGNILVILSV | ||||||
Topological domain | 52-64 | Cytoplasmic | ||||
Sequence: ACHRHLHSVTHYY | ||||||
Transmembrane | 65-88 | Helical; Name=2 | ||||
Sequence: IVNLAVADLLLTSTVLPFSAIFEV | ||||||
Topological domain | 89-99 | Extracellular | ||||
Sequence: LGYWAFGRVFC | ||||||
Transmembrane | 100-122 | Helical; Name=3 | ||||
Sequence: NIWAAVDVLCCTASIMGLCIISI | ||||||
Topological domain | 123-143 | Cytoplasmic | ||||
Sequence: DRYIGVSYPLRYPTIVTQRRG | ||||||
Transmembrane | 144-167 | Helical; Name=4 | ||||
Sequence: LMALLCVWALSLVISIGPLFGWRQ | ||||||
Topological domain | 168-181 | Extracellular | ||||
Sequence: PAPEDETICQINEE | ||||||
Transmembrane | 182-205 | Helical; Name=5 | ||||
Sequence: PGYVLFSALGSFYLPLAIILVMYC | ||||||
Topological domain | 206-273 | Cytoplasmic | ||||
Sequence: RVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGMASAKTKTHFSVRLLKFSREKKAAKT | ||||||
Transmembrane | 274-297 | Helical; Name=6 | ||||
Sequence: LGIVVGCFVLCWLPFFLVMPIGSF | ||||||
Topological domain | 298-305 | Extracellular | ||||
Sequence: FPDFKPSE | ||||||
Transmembrane | 306-329 | Helical; Name=7 | ||||
Sequence: TVFKIVFWLGYLNSCINPIIYPCS | ||||||
Topological domain | 330-466 | Cytoplasmic | ||||
Sequence: SQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035756 | 40 | in a breast cancer sample; somatic mutation | |||
Sequence: G → W | ||||||
Natural variant | VAR_049370 | 200 | in dbSNP:rs2229125 | |||
Sequence: I → S | ||||||
Mutagenesis | 334 | Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-335; A-342; A-348 and A-349. | ||||
Sequence: K → A | ||||||
Mutagenesis | 335 | Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-342; A-348 and A-349. | ||||
Sequence: K → A | ||||||
Mutagenesis | 342 | Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-348 and A-349. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_019509 | 347 | in dbSNP:rs1048101 | |||
Sequence: C → R | ||||||
Mutagenesis | 348 | Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-342 and A-349. | ||||
Sequence: R → A | ||||||
Mutagenesis | 349 | Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-342 and A-348. | ||||
Sequence: K → A | ||||||
Natural variant | VAR_049371 | 414 | in dbSNP:rs3730247 | |||
Sequence: K → R | ||||||
Natural variant | VAR_049372 | 465 | in dbSNP:rs2229126 | |||
Sequence: E → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 732 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond, modified residue, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000069063 | 1-466 | Alpha-1A adrenergic receptor | |||
Sequence: MVFLSGNASDSSNCTQPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEVLGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYLPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGMASAKTKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV | ||||||
Glycosylation | 7 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 13 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 22 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 99↔176 | |||||
Sequence: CNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGLMALLCVWALSLVISIGPLFGWRQPAPEDETIC | ||||||
Modified residue | 215 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Lipidation | 345 | S-palmitoyl cysteine | ||||
Sequence: C |
Post-translational modification
C-terminal Ser or Thr residues may be phosphorylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in heart, brain, liver and prostate, but not in kidney, lung, adrenal, aorta and pituitary. Within the prostate, expressed in the apex, base, periurethral and lateral lobe. Isoform 4 is the most abundant isoform expressed in the prostate with high levels also detected in liver and heart.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homo- and heterooligomer. Heterooligomerizes with ADRA1B homooligomers in cardiac myocytes (PubMed:22120526).
Interacts with CAVIN4 (PubMed:24567387).
Interacts with CAVIN4 (PubMed:24567387).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P35348-1 | CRELD1 Q96HD1 | 3 | EBI-21288891, EBI-713009 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 334-349 | Nuclear localization signal | ||||
Sequence: KKAFQNVLRIQCLCRK |
Sequence similarities
Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA1A sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 9 isoforms produced by Alternative splicing.
P35348-1
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
- SynonymsAlpha 1c-1, Alpha(1A-1)
- Length466
- Mass (Da)51,487
- Last updated1995-11-01 v2
- Checksum1A50487531DECDF0
P35348-2
- Name2
- SynonymsAlpha 1c-2, Alpha(1A-2)
- Differences from canonical
- 424-466: VRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV → TKSRSVTRLECSGMILAHCNLRLPGSRDSPASASQAAGTTGMCHQADATRPS
P35348-3
- Name3
- SynonymsAlpha 1c-3, Alpha(1A-3)
P35348-4
- Name4
- SynonymsAlpha(1A-4)
- Differences from canonical
- 424-466: VRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV → RGMDCRYFTKNCREHIKHVNFMMPPWRKGSEC
P35348-5
- Name5
P35348-6
- Name6
P35348-7
- Name7
- Synonyms2b/3b
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
P35348-8
- Name8
- Synonyms2c
- Differences from canonical
- 295-466: GSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV → DEVSLCHQAGVQWHDLGSLQPPPPGFKRFSCLSLPSSWDYRDVPPGRRHQAQLIFVFLVETGFHHVGQDDLDLLTS
P35348-9
- Name9
- Synonyms3c
- Differences from canonical
- 296-466: SFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV → THTHDMKPASRPRLLSLLPKEGEHETHHWSCDPLSLESTPGAQEPCLTLGFTSLSSIHLTKAQIQHVTVTDTGKTVT
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E7EW16 | E7EW16_HUMAN | ADRA1A | 427 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 43 | in Ref. 4; AAA93114 | ||||
Sequence: G → C | ||||||
Sequence conflict | 129 | in Ref. 4; AAA93114 | ||||
Sequence: S → T | ||||||
Sequence conflict | 130 | in Ref. 9; AAK77197 | ||||
Sequence: Y → H | ||||||
Sequence conflict | 185 | in Ref. 14; AAH95512 | ||||
Sequence: V → A | ||||||
Alternative sequence | VSP_011053 | 295-342 | in isoform 6 | |||
Sequence: GSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLR → DEETEAQEGKNDSPSFKQPVHHAAVLGLEVMEKENLEGVSRKDTCGVW | ||||||
Alternative sequence | VSP_011046 | 295-466 | in isoform 8 | |||
Sequence: GSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV → DEVSLCHQAGVQWHDLGSLQPPPPGFKRFSCLSLPSSWDYRDVPPGRRHQAQLIFVFLVETGFHHVGQDDLDLLTS | ||||||
Alternative sequence | VSP_011051 | 296-297 | in isoform 5 | |||
Sequence: SF → KS | ||||||
Alternative sequence | VSP_011047 | 296-324 | in isoform 7 | |||
Sequence: SFFPDFKPSETVFKIVFWLGYLNSCINPI → TYILKYDVLFWRKGLSVCTRLRERKEIKN | ||||||
Alternative sequence | VSP_011049 | 296-466 | in isoform 9 | |||
Sequence: SFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV → THTHDMKPASRPRLLSLLPKEGEHETHHWSCDPLSLESTPGAQEPCLTLGFTSLSSIHLTKAQIQHVTVTDTGKTVT | ||||||
Alternative sequence | VSP_011052 | 298-466 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 302 | In isoform P35348-6; in Ref. 8; AAR84650 | ||||
Sequence: E → Q | ||||||
Alternative sequence | VSP_011048 | 325-466 | in isoform 7 | |||
Sequence: Missing | ||||||
Sequence conflict | 338 | in Ref. 2 | ||||
Sequence: Q → C | ||||||
Alternative sequence | VSP_011054 | 343-466 | in isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 359 | in Ref. 4; AAA93114 | ||||
Sequence: T → P | ||||||
Sequence conflict | 384 | in Ref. 9; AAK77197 | ||||
Sequence: T → A | ||||||
Sequence conflict | 387 | in Ref. 9; AAK77197 | ||||
Sequence: R → G | ||||||
Sequence conflict | 390 | in Ref. 9; AAK77197 | ||||
Sequence: K → R | ||||||
Alternative sequence | VSP_011044 | 424-429 | in isoform 3 | |||
Sequence: VRSKSF → GHTPMT | ||||||
Alternative sequence | VSP_011055 | 424-466 | in isoform 2 | |||
Sequence: VRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV → TKSRSVTRLECSGMILAHCNLRLPGSRDSPASASQAAGTTGMCHQADATRPS | ||||||
Alternative sequence | VSP_011050 | 424-466 | in isoform 4 | |||
Sequence: VRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV → RGMDCRYFTKNCREHIKHVNFMMPPWRKGSEC | ||||||
Alternative sequence | VSP_011045 | 430-466 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 431 | in Ref. 1; BAA04960 | ||||
Sequence: Q → E | ||||||
Sequence conflict | 437 | in Ref. 9; AAK77197 | ||||
Sequence: G → E | ||||||
Sequence conflict | 442 | in Ref. 4; AAA93114 | ||||
Sequence: S → C | ||||||
Sequence conflict | 453 | In isoform P35348-4; in Ref. 7; AAC06138 | ||||
Sequence: S → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D25235 EMBL· GenBank· DDBJ | BAA04960.1 EMBL· GenBank· DDBJ | mRNA | ||
U03866 EMBL· GenBank· DDBJ | AAB60353.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U02569 EMBL· GenBank· DDBJ | AAA93114.1 EMBL· GenBank· DDBJ | mRNA | ||
D32201 EMBL· GenBank· DDBJ | BAA06900.1 EMBL· GenBank· DDBJ | mRNA | ||
D32202 EMBL· GenBank· DDBJ | BAA06901.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
L31774 EMBL· GenBank· DDBJ | AAB59486.1 EMBL· GenBank· DDBJ | mRNA | ||
AF013261 EMBL· GenBank· DDBJ | AAC06138.1 EMBL· GenBank· DDBJ | mRNA | ||
AY491775 EMBL· GenBank· DDBJ | AAR84644.1 EMBL· GenBank· DDBJ | mRNA | ||
AY491776 EMBL· GenBank· DDBJ | AAR84645.1 EMBL· GenBank· DDBJ | mRNA | ||
AY491777 EMBL· GenBank· DDBJ | AAR84646.1 EMBL· GenBank· DDBJ | mRNA | ||
AY491778 EMBL· GenBank· DDBJ | AAR84647.1 EMBL· GenBank· DDBJ | mRNA | ||
AY491779 EMBL· GenBank· DDBJ | AAR84648.1 EMBL· GenBank· DDBJ | mRNA | ||
AY491780 EMBL· GenBank· DDBJ | AAR84649.1 EMBL· GenBank· DDBJ | mRNA | ||
AY491781 EMBL· GenBank· DDBJ | AAR84650.1 EMBL· GenBank· DDBJ | mRNA | ||
AF395806 EMBL· GenBank· DDBJ | AAK77197.1 EMBL· GenBank· DDBJ | mRNA | ||
AB065703 EMBL· GenBank· DDBJ | BAC05926.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY389505 EMBL· GenBank· DDBJ | AAQ91331.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK289548 EMBL· GenBank· DDBJ | BAF82237.1 EMBL· GenBank· DDBJ | mRNA | ||
EU326301 EMBL· GenBank· DDBJ | ACA05899.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EU326301 EMBL· GenBank· DDBJ | ACA05900.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
EU326301 EMBL· GenBank· DDBJ | ACA05902.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EU326301 EMBL· GenBank· DDBJ | ACA05903.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EU326301 EMBL· GenBank· DDBJ | ACA05904.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EU326301 EMBL· GenBank· DDBJ | ACA05905.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EU326301 EMBL· GenBank· DDBJ | ACA05906.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EU326301 EMBL· GenBank· DDBJ | ACA05907.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC095512 EMBL· GenBank· DDBJ | AAH95512.1 EMBL· GenBank· DDBJ | mRNA |