P01009 · A1AT_HUMAN
- ProteinAlpha-1-antitrypsin
- GeneSERPINA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids418 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.
Short peptide from AAT
Reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).
Miscellaneous
The aberrant form is found in the plasma of chronic smokers, and persists after smoking is ceased. It can still be found ten years after smoking has ceased.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 352-353 | (Microbial infection) Cleavage; by Staphylococcus aureus aureolysin/Aur | ||||
Sequence: KL | ||||||
Site | 354-355 | (Microbial infection) Cleavage; by Staphylococcus aureus serine and cysteine proteinases | ||||
Sequence: SK | ||||||
Site | 382-383 | Reactive bond | ||||
Sequence: MS |
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 | collagen-containing extracellular matrix | |
Cellular Component | COPII-coated ER to Golgi transport vesicle | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | endoplasmic reticulum-Golgi intermediate compartment membrane | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | ficolin-1-rich granule lumen | |
Cellular Component | Golgi apparatus | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | platelet alpha granule lumen | |
Molecular Function | identical protein binding | |
Molecular Function | protease binding | |
Molecular Function | serine-type endopeptidase inhibitor activity | |
Biological Process | acute-phase response | |
Biological Process | blood coagulation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-1-antitrypsin
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP01009
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum.
Short peptide from AAT
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Alpha-1-antitrypsin deficiency (A1ATD)
- Note
- DescriptionA disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.
- See alsoMIM:613490
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_006978 | 4 | in Z-Wrexham | |||
Sequence: S → L | ||||||
Natural variant | VAR_006979 | 26 | in V-Munich; dbSNP:rs199422212 | |||
Sequence: D → A | ||||||
Natural variant | VAR_051938 | 37 | in dbSNP:rs11558262 | |||
Sequence: T → A | ||||||
Natural variant | VAR_006980 | 58 | in M5-Karlsruhe; dbSNP:rs149319176 | |||
Sequence: A → T | ||||||
Natural variant | VAR_006981 | 63 | in I; dbSNP:rs28931570 | |||
Sequence: R → C | ||||||
Natural variant | VAR_006982 | 65 | in M-Procida; dbSNP:rs28931569 | |||
Sequence: L → P | ||||||
Natural variant | VAR_006983 | 69 | in M6-Bonn; dbSNP:rs199687431 | |||
Sequence: S → F | ||||||
Natural variant | VAR_006984 | 75 | in M-Malton, M-Nichinan and M-Palermo; associated with very low serum levels of AAT; homozygosity for allele M-Malton may be associated with a risk for chronic emphysema or infantile liver cirrhosis | |||
Sequence: Missing | ||||||
Natural variant | VAR_006985 | 77 | in S-Iiyama; dbSNP:rs55819880 | |||
Sequence: S → F | ||||||
Natural variant | VAR_006986 | 84 | in M6-Passau; dbSNP:rs111850950 | |||
Sequence: A → T | ||||||
Natural variant | VAR_006987 | 91 | in M-Mineral springs; causes reduced AAT secretion; dbSNP:rs28931568 | |||
Sequence: G → E | ||||||
Natural variant | VAR_006988 | 92 | in QO-Lisbon; deficient AAT with very low serum levels; dbSNP:rs1490133295 | |||
Sequence: T → I | ||||||
Natural variant | VAR_011620 | 109 | in Z-Bristol; deficient AA; disrupts the N-glycosylation site N-107; dbSNP:rs199422213 | |||
Sequence: T → M | ||||||
Natural variant | VAR_006989 | 112 | in M5-Berlin; dbSNP:rs886044322 | |||
Sequence: P → T | ||||||
Natural variant | VAR_006990 | 116 | in QO-Ludwigshafen; dbSNP:rs28931572 | |||
Sequence: I → N | ||||||
Natural variant | VAR_006991 | 125 | in M2; associated with D-400; dbSNP:rs709932 | |||
Sequence: R → H | ||||||
Natural variant | VAR_006992 | 139 | in QO-Newport; dbSNP:rs11558261 | |||
Sequence: G → S | ||||||
Natural variant | VAR_006993 | 172 | in V and M-Nichinan; dbSNP:rs112030253 | |||
Sequence: G → R | ||||||
Natural variant | VAR_006994 | 172 | in M2-Obernburg; dbSNP:rs112030253 | |||
Sequence: G → W | ||||||
Natural variant | VAR_006995 | 180 | in L-Frankfurt; dbSNP:rs864622051 | |||
Sequence: Q → E | ||||||
Natural variant | VAR_036746 | 190-198 | in Aberrant form | |||
Sequence: QGKIVDLVK → GFQNAILVR | ||||||
Natural variant | VAR_006996 | 228 | in X; dbSNP:rs199422208 | |||
Sequence: E → K | ||||||
Natural variant | VAR_006997 | 237 | in M1A and Z; associated with K-366 in Z; dbSNP:rs6647 | |||
Sequence: V → A | ||||||
Natural variant | VAR_006998 | 247 | in F; dbSNP:rs28929470 | |||
Sequence: R → C | ||||||
Natural variant | VAR_006999 | 280 | in P-Duarte/P-Cardiff/P-Lowell; associated with H-415 in Y-Barcelona; dbSNP:rs121912714 | |||
Sequence: D → V | ||||||
Natural variant | VAR_007000 | 288 | in S and T; dbSNP:rs17580 | |||
Sequence: E → V | ||||||
Natural variant | VAR_009216 | 305 | in Basque | |||
Sequence: Missing | ||||||
Natural variant | VAR_007001 | 354 | in S-Munich; dbSNP:rs201788603 | |||
Sequence: S → F | ||||||
Natural variant | VAR_007002 | 360 | in W-Bethesda; dbSNP:rs1802959 | |||
Sequence: A → T | ||||||
Natural variant | VAR_007003 | 365 | in P-St.Albans/P-Donauwoerth; dbSNP:rs143370956 | |||
Sequence: D → N | ||||||
Natural variant | VAR_007004 | 366 | in Z/Z-Augsburg/Z-Tun; associated with A-237 in Z; dbSNP:rs28929474 | |||
Sequence: E → K | ||||||
Natural variant | VAR_007005 | 382 | in Pittsburgh; has antithrombin activity; inhibits factor VIIa activity; causes fatal bleeding diathesis; dbSNP:rs121912713 | |||
Sequence: M → R | ||||||
Mutagenesis | 382 | Oxidation-resistant inhibitor of therapeutic importance. | ||||
Sequence: M → V | ||||||
Natural variant | VAR_007006 | 386 | in Sao Tome; dbSNP:rs569384943 | |||
Sequence: P → H | ||||||
Natural variant | VAR_007007 | 386 | in L-Offenbach; dbSNP:rs12233 | |||
Sequence: P → T | ||||||
Natural variant | VAR_007008 | 387 | in Christchurch; dbSNP:rs121912712 | |||
Sequence: E → K | ||||||
Natural variant | VAR_007009 | 393 | in M-Heerlen; dbSNP:rs199422209 | |||
Sequence: P → L | ||||||
Natural variant | VAR_007010 | 400 | in M2 and M3; associated with H-125 in M2; dbSNP:rs1303 | |||
Sequence: E → D | ||||||
Natural variant | VAR_007011 | 415 | in Y-Barcelona; associated with V-280 | |||
Sequence: P → H |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 686 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 signal, chain, modified residue, modified residue (large scale data), glycosylation, peptide.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-24 | UniProt | |||||
Sequence: MPSSVSWGILLLAGLCCLVPVSLA | |||||||
Chain | PRO_0000032377 | 25-418 | UniProt | Alpha-1-antitrypsin | |||
Sequence: EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK | |||||||
Modified residue | 38 | UniProt | Phosphoserine; by FAM20C | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 38 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 70 | UniProt | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 107 | UniProt | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | |||||||
Modified residue | 256 | UniProt | S-cysteinyl cysteine | ||||
Sequence: C | |||||||
Glycosylation | 271 | UniProt | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | |||||||
Peptide | PRO_0000364030 | 375-418 | UniProt | Short peptide from AAT | |||
Sequence: MFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK | |||||||
Modified residue | 383 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
N-glycosylated. Differential glycosylation produces a number of isoforms. N-linked glycan at Asn-107 is alternatively di-antennary, tri-antennary or tetra-antennary. The glycan at Asn-70 is di-antennary with trace amounts of tri-antennary. Glycan at Asn-271 is exclusively di-antennary. Structure of glycans at Asn-70 and Asn-271 is Hex5HexNAc4. The structure of the antennae is Neu5Ac(alpha1-6)Gal(beta1-4)GlcNAc attached to the core structure Man(alpha1-6)[Man(alpha1-3)]Man(beta1-4)GlcNAc(beta1-4)GlcNAc. Some antennae are fucosylated, which forms a Lewis-X determinant.
Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.
(Microbial infection) Proteolytically processed by Staphylococcus aureus seryl, cysteinyl, and metallo-proteases.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Ubiquitous. Expressed in leukocytes and plasma.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with CELA2A (PubMed:31358993).
Interacts with ERGIC3 and LMAN1/ERGIC53 (PubMed:31142615).
Interacts with PRSS1/trypsin (PubMed:11057674).
Interacts with PRSS1/Trypsin (PubMed:11057674).
The variants S and Z interact with CANX and PDIA3 (PubMed:23826168).
Interacts with ERGIC3 and LMAN1/ERGIC53 (PubMed:31142615).
Interacts with PRSS1/trypsin (PubMed:11057674).
Interacts with PRSS1/Trypsin (PubMed:11057674).
The variants S and Z interact with CANX and PDIA3 (PubMed:23826168).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P01009 | CELA1 P00772 | 2 | EBI-986224, EBI-986248 | |
BINARY | P01009 | ERGIC3 Q9Y282 | 2 | EBI-986224, EBI-781551 | |
XENO | P01009 | espB P71213 | 3 | EBI-986224, EBI-2615322 | |
BINARY | P01009 | MAGEB6 Q8N7X4 | 3 | EBI-986224, EBI-6447163 | |
XENO | P01009 | PRSS1 P00760 | 5 | EBI-986224, EBI-986385 | |
BINARY | P01009 | SERPINA1 P01009 | 7 | EBI-986224, EBI-986224 | |
BINARY | P01009 | SSR1 P43307 | 4 | EBI-986224, EBI-714168 | |
BINARY | P01009 | TMPRSS2 O15393 | 2 | EBI-986224, EBI-12549863 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 368-392 | RCL | ||||
Sequence: GTEAAGAMFLEAIPMSIPPEVKFNK |
Domain
The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
Sequence similarities
Belongs to the serpin family.
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 3 isoforms produced by Alternative splicing.
P01009-1
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
- Length418
- Mass (Da)46,737
- Last updated1996-10-01 v3
- Checksum7016555F273B7F16
P01009-2
- Name2
- Differences from canonical
- 356-418: AVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK → VRSP
P01009-3
- Name3
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
- Differences from canonical
- 307-418: Missing
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
G3V544 | G3V544_HUMAN | SERPINA1 | 156 | ||
G3V5R8 | G3V5R8_HUMAN | SERPINA1 | 92 | ||
G3V4I7 | G3V4I7_HUMAN | SERPINA1 | 22 | ||
G3V387 | G3V387_HUMAN | SERPINA1 | 117 | ||
G3V2B9 | G3V2B9_HUMAN | SERPINA1 | 105 | ||
A0A0G2JRN3 | A0A0G2JRN3_HUMAN | SERPINA1 | 359 | ||
A0A024R6N5 | A0A024R6N5_HUMAN | SERPINA1 | 418 | ||
A0A0B4J278 | A0A0B4J278_HUMAN | SERPINA1 | 144 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 4; AAA51546 | ||||
Sequence: Missing | ||||||
Sequence conflict | 23 | in Ref. 11; BAG38005 | ||||
Sequence: L → P | ||||||
Sequence conflict | 26 | in Ref. 18; AA sequence | ||||
Sequence: D → H | ||||||
Sequence conflict | 39 | in Ref. 18; AA sequence | ||||
Sequence: H → L | ||||||
Sequence conflict | 61 | in Ref. 9; AAF29581 | ||||
Sequence: L → P | ||||||
Sequence conflict | 96 | in Ref. 7; ABG73380 | ||||
Sequence: T → A | ||||||
Sequence conflict | 139-140 | in Ref. 1; AAB59375 | ||||
Sequence: GN → DG | ||||||
Sequence conflict | 174 | in Ref. 4; AAA51546 | ||||
Sequence: T → H | ||||||
Sequence conflict | 229 | in Ref. 4; AAA51546 | ||||
Sequence: E → D | ||||||
Sequence conflict | 273 | in Ref. 1; AAB59375 | ||||
Sequence: T → N | ||||||
Sequence conflict | 280 | in Ref. 7; ABG73380 | ||||
Sequence: D → G | ||||||
Alternative sequence | VSP_028890 | 307-418 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 326 | in Ref. 3; CAA25838 | ||||
Sequence: V → I | ||||||
Alternative sequence | VSP_028889 | 356-418 | in isoform 2 | |||
Sequence: AVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK → VRSP | ||||||
Sequence conflict | 410 | in Ref. 24; AA sequence | ||||
Sequence: G → L | ||||||
Sequence conflict | 414 | in Ref. 24; AA sequence | ||||
Sequence: N → S |
Polymorphism
The sequence shown is that of the M1V allele which is the most common form of PI (44 to 49%). Other frequent alleles are: M1A 20 to 23%; M2 10 to 11%; M3 14 to 19%.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
K01396 EMBL· GenBank· DDBJ | AAB59375.1 EMBL· GenBank· DDBJ | mRNA | ||
K02212 EMBL· GenBank· DDBJ | AAB59495.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X01683 EMBL· GenBank· DDBJ | CAA25838.1 EMBL· GenBank· DDBJ | mRNA | ||
M11465 EMBL· GenBank· DDBJ | AAA51546.1 EMBL· GenBank· DDBJ | mRNA | ||
J02619 EMBL· GenBank· DDBJ | AAA51547.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ682455 EMBL· GenBank· DDBJ | ABG73380.1 EMBL· GenBank· DDBJ | mRNA | ||
AM048838 EMBL· GenBank· DDBJ | CAJ15161.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF113676 EMBL· GenBank· DDBJ | AAF29581.1 EMBL· GenBank· DDBJ | mRNA | ||
AF130068 EMBL· GenBank· DDBJ | AAG35496.1 EMBL· GenBank· DDBJ | mRNA | ||
BX161449 EMBL· GenBank· DDBJ | CAD61914.1 EMBL· GenBank· DDBJ | mRNA | ||
BX247968 EMBL· GenBank· DDBJ | CAD62306.1 EMBL· GenBank· DDBJ | mRNA | ||
BX248002 EMBL· GenBank· DDBJ | CAD62334.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BX248257 EMBL· GenBank· DDBJ | CAD62585.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK315637 EMBL· GenBank· DDBJ | BAG38005.1 EMBL· GenBank· DDBJ | mRNA | ||
BT019455 EMBL· GenBank· DDBJ | AAV38262.1 EMBL· GenBank· DDBJ | mRNA | ||
BC011991 EMBL· GenBank· DDBJ | AAH11991.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015642 EMBL· GenBank· DDBJ | AAH15642.1 EMBL· GenBank· DDBJ | mRNA | ||
J00064 EMBL· GenBank· DDBJ | AAB59369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
J00066 EMBL· GenBank· DDBJ | AAB59370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
J00065 EMBL· GenBank· DDBJ | AAB59370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
J00067 EMBL· GenBank· DDBJ | AAB59371.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X02920 EMBL· GenBank· DDBJ | CAA26677.1 EMBL· GenBank· DDBJ | mRNA | ||
V00496 EMBL· GenBank· DDBJ | CAA23755.1 EMBL· GenBank· DDBJ | mRNA | ||
M26123 EMBL· GenBank· DDBJ | AAA51545.1 EMBL· GenBank· DDBJ | mRNA |