P50542 · PEX5_HUMAN
- ProteinPeroxisomal targeting signal 1 receptor
- GenePEX5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids639 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) (PubMed:11101887, PubMed:11336669, PubMed:12456682, PubMed:16314507, PubMed:17157249, PubMed:17428317, PubMed:21976670, PubMed:26344566, PubMed:7706321, PubMed:7719337, PubMed:7790377).
Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins (PubMed:12456682, PubMed:17157249, PubMed:21976670, PubMed:26344566).
PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle (PubMed:11336669, PubMed:24662292).
Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins (PubMed:12456682, PubMed:17157249, PubMed:21976670, PubMed:26344566).
PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle (PubMed:11336669, PubMed:24662292).
Isoform 1
In addition to promoting peroxisomal translocation of proteins containing a PTS1 peroxisomal targeting signal, mediates peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal via its interaction with PEX7 (PubMed:11336669, PubMed:11546814, PubMed:25538232, PubMed:33389129, PubMed:9668159).
Interaction with PEX7 only takes place when PEX7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal (PubMed:25538232).
PEX7 along with PTS2-containing cargo proteins are then translocated through the PEX13-PEX14 docking complex together with PEX5 (PubMed:25538232).
Interaction with PEX7 only takes place when PEX7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal (PubMed:25538232).
PEX7 along with PTS2-containing cargo proteins are then translocated through the PEX13-PEX14 docking complex together with PEX5 (PubMed:25538232).
Isoform 2
Does not mediate translocation of peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal.
Activity regulation
Cys-11 acts as a sensor of redox state (PubMed:24118911).
In response to oxidative stress, monoubiquitination at Cys-11 is prevented (PubMed:24118911).
In response to oxidative stress, monoubiquitination at Cys-11 is prevented (PubMed:24118911).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 11 | Sensor of redox state | ||||
Sequence: C |
GO annotations
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeroxisomal targeting signal 1 receptor
- Short namesPTS1 receptor ; PTS1R
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP50542
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Cycles between the cytosol and the peroxisome matrix (PubMed:11336669, PubMed:16314507).
Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins (By similarity).
Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol (By similarity).
Cys-11 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (PubMed:16314507, PubMed:19208625, PubMed:24118911, PubMed:29884772).
Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix (By similarity).
The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzymes, resetting PEX5 for a subsequent import cycle (By similarity).
Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins (By similarity).
Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol (By similarity).
Cys-11 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (PubMed:16314507, PubMed:19208625, PubMed:24118911, PubMed:29884772).
Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix (By similarity).
The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzymes, resetting PEX5 for a subsequent import cycle (By similarity).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Peroxisome biogenesis disorder 2A (PBD2A)
- Note
- DescriptionA fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and characterized clinically by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life.
- See alsoMIM:214110
Peroxisome biogenesis disorder 2B (PBD2B)
- Note
- DescriptionA peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid.
- See alsoMIM:202370
Natural variants in PBD2B
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_087153 | 427-639 | missing | in PBD2B; impaired ability to mediate peroxisomal import of proteins containing both a C-terminal PTS1- and PTS2-type targeting signals | |
VAR_007543 | 526 | N>K | in PBD2B; neonatal adrenoleukodystrophy; strongly affects peroxisomal protein import containing a C-terminal PTS1-type targeting signal without affecting import of proteins with a PTS2 targeting signal; dbSNP:rs61752138 | |
VAR_031328 | 600 | S>W | in PBD2B; infantile Refsum disease; mildly affects peroxisomal protein import |
Rhizomelic chondrodysplasia punctata 5 (RCDP5)
- Note
- DescriptionA form of rhizomelic chondrodysplasia punctata, a disease characterized by severely disturbed endochondral bone formation, rhizomelic shortening of femur and humerus, vertebral disorders, dwarfism, cataract, cutaneous lesions, facial dysmorphism, and severe intellectual disability with spasticity.
- See alsoMIM:616716
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 11 | Promotes accumulation at the peroxisomal membrane because of impaired export into the cytosol. Does not affect monoubiquitination by TRIM37. | ||||
Sequence: C → A | ||||||
Mutagenesis | 11 | Does not affect ability to mediate peroxisomal import of proteins. | ||||
Sequence: C → K | ||||||
Mutagenesis | 11 | Promotes accumulation at the peroxisomal membrane because of impaired export into the cytosol. | ||||
Sequence: C → S or R | ||||||
Mutagenesis | 62-66 | Abolished interaction with PEX14. | ||||
Sequence: LVAEF → AAAAA | ||||||
Mutagenesis | 118 | Strongly reduced interaction with PEX14. | ||||
Sequence: W → A | ||||||
Mutagenesis | 122 | Strongly reduced interaction with PEX14. | ||||
Sequence: F → A | ||||||
Mutagenesis | 140 | Decreased interaction with PEX14. | ||||
Sequence: W → A | ||||||
Mutagenesis | 141 | Abolished phosphorylation by ATM, leading to impaired monoubiquitination at K-209. | ||||
Sequence: S → A | ||||||
Mutagenesis | 141 | Mimics phosphorylation, leading to increased pexophagy in response to reactive oxygen species (ROS). | ||||
Sequence: S → E | ||||||
Mutagenesis | 209 | Does not affect monoubiquitination by TRIM37. | ||||
Sequence: K → A | ||||||
Mutagenesis | 209 | Abolished interaction with SQSTM1, leading to decreased pexophagy in response to reactive oxygen species (ROS). | ||||
Sequence: K → R | ||||||
Natural variant | VAR_087152 | 218 | found in a family with congenital cataract; likely pathogenic; impaired interaction with PEX7; impaired ability to mediate peroxisomal import of proteins containing a C-terminal PTS2-type targeting signal without affecting import of proteins with a PTS1 targeting signal | |||
Sequence: F → S | ||||||
Natural variant | VAR_087153 | 427-639 | in PBD2B; impaired ability to mediate peroxisomal import of proteins containing both a C-terminal PTS1- and PTS2-type targeting signals | |||
Sequence: Missing | ||||||
Mutagenesis | 472 | Abolished monoubiquitination by TRIM37, leading to decreased stability. | ||||
Sequence: K → A | ||||||
Natural variant | VAR_007543 | 526 | in PBD2B; neonatal adrenoleukodystrophy; strongly affects peroxisomal protein import containing a C-terminal PTS1-type targeting signal without affecting import of proteins with a PTS2 targeting signal; dbSNP:rs61752138 | |||
Sequence: N → K | ||||||
Mutagenesis | 527 | Does not affect monoubiquitination by TRIM37. | ||||
Sequence: K → A | ||||||
Mutagenesis | 527 | Does not affect PEX5 recycling. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_031328 | 600 | in PBD2B; infantile Refsum disease; mildly affects peroxisomal protein import | |||
Sequence: S → W |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 854 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, cross-link, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000106305 | 1-639 | UniProt | Peroxisomal targeting signal 1 receptor | |||
Sequence: MAMRELVEAECGGANPLMKLAGHFTQDKALRQEGLRPGPWPPGAPASEAASKPLGVASEDELVAEFLQDQNAPLVSRAPQTFKMDDLLAEMQQIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVTQDYNETDWSQEFISEVTDPLSVSPARWAEEYLEQSEEKLWLGEPEGTATDRWYDEYHPEEDLQHTASDFVAKVDDPKLANSEFLKFVRQIGEGQVSLESGAGSGRAQAEQWAAEFIQQQGTSDAWVDQFTRPVNTSALDMEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLTSATYDKGYQFEEENPLRDHPQPFEEGLRRLQEGDLPNAVLLFEAAVQQDPKHMEAWQYLGTTQAENEQELLAISALRRCLELKPDNQTALMALAVSFTNESLQRQACETLRDWLRYTPAYAHLVTPAEEGAGGAGLGPSKRILGSLLSDSLFLEVKELFLAAVRLDPTSIDPDVQCGLGVLFNLSGEYDKAVDCFTAALSVRPNDYLLWNKLGATLANGNQSEEAVAAYRRALELQPGYIRSRYNLGISCINLGAHREAVEHFLEALNMQRKSRGPRGEGGAMSENIWSTLRLALSMLGQSDAYGAADARDLSTLLTMFGLPQ | |||||||
Cross-link | 11 | UniProt | Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: C | |||||||
Modified residue (large scale data) | 58 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 115 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 141 | UniProt | Phosphoserine; by ATM | ||||
Sequence: S | |||||||
Modified residue | 153 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 155 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 167 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 167 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 209 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 268 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 279 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 472 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 527 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Monoubiquitinated at Cys-11 by PEX2 during PEX5 passage through the retrotranslocation channel (By similarity).
Cys-11 monoubiquitination acts as a recognition signal for the PEX1-PEX6 complex and is required for PEX5 extraction and export from peroxisomes (PubMed:29884772).
Monoubiquitination at Cys-11 is removed by USP9X in the cytosol, resetting PEX5 for a subsequent import cycle (PubMed:22371489).
When PEX5 recycling is compromised, polyubiquitinated by PEX10 during its passage through the retrotranslocation channel, leading to its degradation (By similarity).
Monoubiquitination at Lys-472 by TRIM37 promotes its stability by preventing its polyubiquitination and degradation by the proteasome (PubMed:28724525).
Ubiquitination at Lys-527 is not mediated by the PEX2-PEX10-PEX12 ligase complex and is not related to PEX5 recycling (PubMed:24662292).
Monoubiquitinated at Lys-209 by PEX2 following phosphorylation by ATM in response to starvation or reactive oxygen species (ROS), leading to PEX5 recognition by p62/SQSTM1 and induction of pexophagy (PubMed:26344566, PubMed:27597759).
Cys-11 monoubiquitination acts as a recognition signal for the PEX1-PEX6 complex and is required for PEX5 extraction and export from peroxisomes (PubMed:29884772).
Monoubiquitination at Cys-11 is removed by USP9X in the cytosol, resetting PEX5 for a subsequent import cycle (PubMed:22371489).
When PEX5 recycling is compromised, polyubiquitinated by PEX10 during its passage through the retrotranslocation channel, leading to its degradation (By similarity).
Monoubiquitination at Lys-472 by TRIM37 promotes its stability by preventing its polyubiquitination and degradation by the proteasome (PubMed:28724525).
Ubiquitination at Lys-527 is not mediated by the PEX2-PEX10-PEX12 ligase complex and is not related to PEX5 recycling (PubMed:24662292).
Monoubiquitinated at Lys-209 by PEX2 following phosphorylation by ATM in response to starvation or reactive oxygen species (ROS), leading to PEX5 recognition by p62/SQSTM1 and induction of pexophagy (PubMed:26344566, PubMed:27597759).
Phosphorylated at Ser-141 by ATM in response to reactive oxygen species (ROS), promoting monoubiquitination at Lys-209 and induction of pexophagy.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts (via WxxxF/Y and LVxEF motifs) with PEX14; promoting translocation through the PEX13-PEX14 docking complex (PubMed:11438541, PubMed:19197237, PubMed:24235149, PubMed:24662292, PubMed:28765278).
Interacts with PEX12 (PubMed:10562279).
Interacts (Cys-linked ubiquitinated) with ZFAND6 (PubMed:21980954).
Interacts (when ubiquitinated at Lys-209) with p62/SQSTM1 (PubMed:26344566).
Interacts with DDO; the interaction is direct and required for localization of DDO to the peroxisome (PubMed:9820813).
Interacts with PEX12 (PubMed:10562279).
Interacts (Cys-linked ubiquitinated) with ZFAND6 (PubMed:21980954).
Interacts (when ubiquitinated at Lys-209) with p62/SQSTM1 (PubMed:26344566).
Interacts with DDO; the interaction is direct and required for localization of DDO to the peroxisome (PubMed:9820813).
Isoform 1
Interacts with PEX7, promoting peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 11-33 | Amphipathic helix 1 (AH1) | ||||
Sequence: CGGANPLMKLAGHFTQDKALRQE | ||||||
Region | 33-53 | Disordered | ||||
Sequence: EGLRPGPWPPGAPASEAASKP | ||||||
Motif | 62-66 | LVxEF motif | ||||
Sequence: LVAEF | ||||||
Region | 81-99 | Amphipathic helix 2 (AH2) | ||||
Sequence: TFKMDDLLAEMQQIEQSNF | ||||||
Motif | 118-122 | WxxxF/Y motif 1 | ||||
Sequence: WAQEF | ||||||
Motif | 140-144 | WxxxF/Y motif 2 | ||||
Sequence: WSQEF | ||||||
Motif | 159-163 | WxxxF/Y motif 3 | ||||
Sequence: WAEEY | ||||||
Motif | 184-188 | WxxxF/Y motif 4 | ||||
Sequence: WYDEY | ||||||
Region | 190-206 | Amphipathic helix 3 (AH3) | ||||
Sequence: PEEDLQHTASDFVAKVD | ||||||
Motif | 243-247 | WxxxF/Y motif 5 | ||||
Sequence: WAAEF | ||||||
Motif | 257-261 | WxxxF/Y motif 6 | ||||
Sequence: WVDQF | ||||||
Region | 284-300 | Amphipathic helix 4 (AH4) | ||||
Sequence: DVDFWDKLQAELEEMAK | ||||||
Motif | 308-312 | WxxxF/Y motif 7 | ||||
Sequence: WLSDY | ||||||
Repeat | 335-368 | TPR 1 | ||||
Sequence: HPQPFEEGLRRLQEGDLPNAVLLFEAAVQQDPKH | ||||||
Repeat | 369-402 | TPR 2 | ||||
Sequence: MEAWQYLGTTQAENEQELLAISALRRCLELKPDN | ||||||
Repeat | 403-436 | TPR 3 | ||||
Sequence: QTALMALAVSFTNESLQRQACETLRDWLRYTPAY | ||||||
Repeat | 452-485 | TPR 4 | ||||
Sequence: LGPSKRILGSLLSDSLFLEVKELFLAAVRLDPTS | ||||||
Repeat | 488-521 | TPR 5 | ||||
Sequence: PDVQCGLGVLFNLSGEYDKAVDCFTAALSVRPND | ||||||
Repeat | 522-555 | TPR 6 | ||||
Sequence: YLLWNKLGATLANGNQSEEAVAAYRRALELQPGY | ||||||
Repeat | 556-589 | TPR 7 | ||||
Sequence: IRSRYNLGISCINLGAHREAVEHFLEALNMQRKS |
Domain
The TPR repeats mediate interaction with proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type).
The WxxxF/Y motifs mediate interaction with PEX14, promoting association with the PEX13-PEX14 docking complex.
The amphipathic helix 1 and 2 (AH1 and AH2, respectively) are required for PEX5 retrotranslocation and recycling (By similarity).
AH2 mediates interaction with lumenal side of the PEX2-PEX10-PEX12 ligase complex, while AH1 is required for extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity).
AH2 mediates interaction with lumenal side of the PEX2-PEX10-PEX12 ligase complex, while AH1 is required for extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity).
Sequence similarities
Belongs to the peroxisomal targeting signal receptor family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
P50542-1
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
- SynonymsPEX5L
- Length639
- Mass (Da)70,865
- Last updated2006-12-12 v3
- Checksum9D6951F58AED31AC
P50542-2
- Name2
- SynonymsPEX5S
- Differences from canonical
- 215-251: Missing
P50542-3
- Name3
- Differences from canonical
- 283-290: Missing
P50542-4
- Name4
- Differences from canonical
- 45-45: P → PASEAVSVLEVESPGA
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3KPV0 | J3KPV0_HUMAN | PEX5 | 410 | ||
H0YGT8 | H0YGT8_HUMAN | PEX5 | 31 | ||
B4E0T2 | B4E0T2_HUMAN | PEX5 | 660 | ||
F5GZ41 | F5GZ41_HUMAN | PEX5 | 115 | ||
F5GXX3 | F5GXX3_HUMAN | PEX5 | 104 | ||
F5GYB4 | F5GYB4_HUMAN | PEX5 | 128 | ||
F5H5C0 | F5H5C0_HUMAN | PEX5 | 272 | ||
F5H637 | F5H637_HUMAN | PEX5 | 168 | ||
F5H3X7 | F5H3X7_HUMAN | PEX5 | 248 | ||
F5H432 | F5H432_HUMAN | PEX5 | 102 | ||
F5H0L9 | F5H0L9_HUMAN | PEX5 | 118 | ||
F5H205 | F5H205_HUMAN | PEX5 | 114 |
Features
Showing features for alternative sequence, sequence conflict.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U19721 EMBL· GenBank· DDBJ | AAC50103.1 EMBL· GenBank· DDBJ | mRNA | ||
Z48054 EMBL· GenBank· DDBJ | CAA88131.1 EMBL· GenBank· DDBJ | mRNA | ||
X84899 EMBL· GenBank· DDBJ | CAA59324.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292256 EMBL· GenBank· DDBJ | BAF84945.1 EMBL· GenBank· DDBJ | mRNA | ||
AK302742 EMBL· GenBank· DDBJ | BAG63957.1 EMBL· GenBank· DDBJ | mRNA | ||
AK316250 EMBL· GenBank· DDBJ | BAH14621.1 EMBL· GenBank· DDBJ | mRNA | ||
AC018653 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471116 EMBL· GenBank· DDBJ | EAW88671.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471116 EMBL· GenBank· DDBJ | EAW88674.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471116 EMBL· GenBank· DDBJ | EAW88672.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC010621 EMBL· GenBank· DDBJ | AAH10621.1 EMBL· GenBank· DDBJ | mRNA |