P35372 · OPRM_HUMAN
- ProteinMu-type opioid receptor
- GeneOPRM1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids400 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone (PubMed:10529478, PubMed:10836142, PubMed:12589820, PubMed:19300905, PubMed:7891175, PubMed:7905839, PubMed:7957926, PubMed:9689128).
Also activated by enkephalin peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher affinity for Met-enkephalin-Arg-Phe (By similarity).
Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors (PubMed:7905839).
The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extent to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15 (PubMed:12068084).
They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B (By similarity).
Also couples to adenylate cyclase stimulatory G alpha proteins (By similarity).
The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4 (By similarity).
Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization (By similarity).
Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction (By similarity).
The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins (By similarity).
The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist-specific receptor phosphorylation (By similarity).
Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling (By similarity).
Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling (By similarity).
Endogenous ligands induce rapid desensitization, endocytosis and recycling (By similarity).
Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties (By similarity).
Isoform 12
Isoform 16
Isoform 17
Miscellaneous
GO annotations
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMu-type opioid receptor
- Short namesM-OR-1; MOR-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP35372
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 12
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-68 | Extracellular | ||||
Sequence: MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNLSDPCGPNRTDLGGRDSLCPPTGSPSMI | ||||||
Transmembrane | 69-93 | Helical; Name=1 | ||||
Sequence: TAITIMALYSIVCVVGLFGNFLVMY | ||||||
Topological domain | 94-106 | Cytoplasmic | ||||
Sequence: VIVRYTKMKTATN | ||||||
Transmembrane | 107-131 | Helical; Name=2 | ||||
Sequence: IYIFNLALADALATSTLPFQSVNYL | ||||||
Topological domain | 132-142 | Extracellular | ||||
Sequence: MGTWPFGTILC | ||||||
Transmembrane | 143-165 | Helical; Name=3 | ||||
Sequence: KIVISIDYYNMFTSIFTLCTMSV | ||||||
Topological domain | 166-185 | Cytoplasmic | ||||
Sequence: DRYIAVCHPVKALDFRTPRN | ||||||
Transmembrane | 186-207 | Helical; Name=4 | ||||
Sequence: AKIINVCNWILSSAIGLPVMFM | ||||||
Topological domain | 208-230 | Extracellular | ||||
Sequence: ATTKYRQGSIDCTLTFSHPTWYW | ||||||
Transmembrane | 231-255 | Helical; Name=5 | ||||
Sequence: ENLLKICVFIFAFIMPVLIITVCYG | ||||||
Topological domain | 256-279 | Cytoplasmic | ||||
Sequence: LMILRLKSVRMLSGSKEKDRNLRR | ||||||
Transmembrane | 280-306 | Helical; Name=6 | ||||
Sequence: ITRMVLVVVAVFIVCWTPIHIYVIIKA | ||||||
Topological domain | 307-314 | Extracellular | ||||
Sequence: LVTIPETT | ||||||
Transmembrane | 315-338 | Helical; Name=7 | ||||
Sequence: FQTVSWHFCIALGYTNSCLNPVLY | ||||||
Topological domain | 339-400 | Cytoplasmic | ||||
Sequence: AFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_009525 | 6 | in dbSNP:rs1799972 | |||
Sequence: A → V | ||||||
Natural variant | VAR_009524 | 40 | in dbSNP:rs1799971 | |||
Sequence: N → D | ||||||
Natural variant | VAR_049426 | 63 | in dbSNP:rs9282817 | |||
Sequence: G → V | ||||||
Natural variant | VAR_049427 | 66 | in dbSNP:rs9282819 | |||
Sequence: S → F | ||||||
Mutagenesis | 142 | Abolishes ligand binding; when associated with A-219 or S-219. | ||||
Sequence: C → A or S | ||||||
Natural variant | VAR_009526 | 147 | in dbSNP:rs17174794 | |||
Sequence: S → C | ||||||
Natural variant | VAR_019252 | 152 | in dbSNP:rs17174801 | |||
Sequence: N → D | ||||||
Mutagenesis | 219 | Abolishes ligand binding; when associated with A-142 or S-142. | ||||
Sequence: C → A or S | ||||||
Natural variant | VAR_009527 | 260 | in dbSNP:rs1799974 | |||
Sequence: R → H | ||||||
Natural variant | VAR_019253 | 265 | in dbSNP:rs17174822 | |||
Sequence: R → C | ||||||
Mutagenesis | 273 | Impairs interaction with calmodulin. | ||||
Sequence: K → A | ||||||
Natural variant | VAR_019254 | 274 | in dbSNP:rs17174829 | |||
Sequence: D → N | ||||||
Mutagenesis | 275 | Impairs interaction with calmodulin. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_082952 | 388-400 | ||||
Sequence: Missing | ||||||
Natural variant | VAR_082953 | 411-420 | In isoform P35372-9; | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 659 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_0000069972 | 1-400 | Mu-type opioid receptor | |||
Sequence: MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNLSDPCGPNRTDLGGRDSLCPPTGSPSMITAITIMALYSIVCVVGLFGNFLVMYVIVRYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP | ||||||
Glycosylation | 9 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 12 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 33 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 40 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 48 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 142↔219 | |||||
Sequence: CKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDC | ||||||
Modified residue | 168 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Lipidation | 353 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 365 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 372 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 377 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 396 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with heterotrimeric G proteins; interaction with a heterotrimeric complex containing GNAI1, GNB1 and GNG2 stabilizes the active conformation of the receptor and increases its affinity for endomorphin-2, the synthetic opioid peptide DAMGO and for morphinan agonists (By similarity).
Interacts with PPL; the interaction disrupts agonist-mediated G-protein activation (PubMed:12810704).
Interacts (via C-terminus) with DNAJB4 (via C-terminus) (PubMed:16542645).
Interacts with calmodulin; the interaction inhibits the constitutive activity of OPRM1; it abolishes basal and attenuates agonist-stimulated G-protein coupling (PubMed:10419536, PubMed:10899953).
Interacts with FLNA, PLD2, RANBP9 and WLS and GPM6A (PubMed:12519790, PubMed:14573758, PubMed:19788913, PubMed:20214800).
Interacts with RTP4 (By similarity).
Interacts with SYP and GNAS (By similarity).
Interacts with RGS9, RGS17, RGS20, RGS4, PPP1R9B and HINT1 (By similarity).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 334-338 | NPxxY; plays a role in stabilizing the activated conformation of the receptor | ||||
Sequence: NPVLY |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 18 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
P35372-1
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
- Length400
- Mass (Da)44,779
- Last updated1998-07-15 v2
- Checksum1DABEBEC9AFF6F66
P35372-2
- Name2
- SynonymsMOR1A, MOR-1A
- Differences from canonical
- 389-400: LENLEAETAPLP → VRSL
P35372-3
- Name3
- SynonymsMOR-1R, MOR-1X
- Differences from canonical
- 389-400: LENLEAETAPLP → CLPIPSLSCWALEQGCLVVYPGPLQGPLVRYDLPAILHSSCLRGNTAPSPSGGAFLLS
P35372-4
- Name4
- SynonymsMOR-1B3
- Differences from canonical
- 389-400: LENLEAETAPLP → GPPAKFVADQLAGSS
P35372-5
- Name5
- SynonymsMOR-1C, MOR-1O
- Differences from canonical
- 389-400: LENLEAETAPLP → PPLAVSMAQIFTRYPPPTHREKTCNDYMKR
P35372-6
- Name6
- SynonymsMOR-1V, MOR-1Y, MOR-1Y2, MOR-1Y3
- 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
- 389-400: LENLEAETAPLP → IRDPISNLPRVSVF
P35372-7
- Name7
- SynonymsMOR-1B1
- Differences from canonical
- 389-400: LENLEAETAPLP → KIDLFQKSSLLNCEHTKG
P35372-8
- Name8
- SynonymsMOR-1B2
- Differences from canonical
- 389-400: LENLEAETAPLP → RERRQKSDW
P35372-9
- Name9
- SynonymsMOR-1B5
- Differences from canonical
- 389-400: LENLEAETAPLP → VELNLDCHCENAKPWPLSYNAGQSPFPFPGRV
P35372-10
- Name10
- SynonymsMOR-1i
- Differences from canonical
- 1-1: M → MCLHRRVPSEETYSLDRFAQNPPLFPPPSLPASESRMAHAPLLQRCGAARTGFCKKQQELWQRRKEAAEALGTRKVSVLLATSHSGARPAVSTM
P35372-11
- Name11
- SynonymsMOR-1B4
- Differences from canonical
- 389-400: LENLEAETAPLP → S
P35372-12
- Name12
- SynonymsMOR-1G1, MOR-1K
- Differences from canonical
- 1-100: Missing
P35372-13
- Name13
- SynonymsMOR-1G2
- Differences from canonical
- 1-96: MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNLSDPCGPNRTDLGGRDSLCPPTGSPSMITAITIMALYSIVCVVGLFGNFLVMYVIV → MMRAKSISTKAGKPS
P35372-14
- Name14
- SynonymsMu3
P35372-15
- Name15
- SynonymsMOR-1W
P35372-16
- Name16
- SynonymsSV1
- Differences from canonical
- 98-400: YTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP → YSWFVIGGPEGRRKQRRLGEDKRARGCGEKG
P35372-17
- Name17
- SynonymsSV2
- Differences from canonical
- 97-400: RYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP → SSSWF
P35372-18
- Name18
- SynonymshMOR-1Z
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_037693 | 1 | in isoform 10 | |||
Sequence: M → MCLHRRVPSEETYSLDRFAQNPPLFPPPSLPASESRMAHAPLLQRCGAARTGFCKKQQELWQRRKEAAEALGTRKVSVLLATSHSGARPAVSTM | ||||||
Alternative sequence | VSP_042328 | 1-96 | in isoform 13 | |||
Sequence: MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNLSDPCGPNRTDLGGRDSLCPPTGSPSMITAITIMALYSIVCVVGLFGNFLVMYVIV → MMRAKSISTKAGKPS | ||||||
Alternative sequence | VSP_042327 | 1-100 | in isoform 12, isoform 14 and isoform 15 | |||
Sequence: Missing | ||||||
Sequence conflict | 26 | in Ref. 11; BAG36624 | ||||
Sequence: P → L | ||||||
Sequence conflict | 51 | in Ref. 1; AAA20580 | ||||
Sequence: D → N | ||||||
Alternative sequence | VSP_042329 | 97-400 | in isoform 17 | |||
Sequence: RYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP → SSSWF | ||||||
Alternative sequence | VSP_047577 | 98-186 | in isoform 18 | |||
Sequence: YTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNA → FHRLYTNILSSNLVLGKPAEDLCFHLRLHYASAHHYRVLWTDDLAPQECPHALWLQRKGQESSKDHQDGAGGGGCVHRLLDSHSHLRHH | ||||||
Alternative sequence | VSP_042330 | 98-400 | in isoform 16 | |||
Sequence: YTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP → YSWFVIGGPEGRRKQRRLGEDKRARGCGEKG | ||||||
Sequence conflict | 109 | in Ref. 6; AAQ77391 | ||||
Sequence: I → V | ||||||
Alternative sequence | VSP_047578 | 187-400 | in isoform 18 | |||
Sequence: Missing | ||||||
Sequence conflict | 207 | in Ref. 2; AAB60354 | ||||
Sequence: M → I | ||||||
Sequence conflict | 234 | in Ref. 1; AAA20580 | ||||
Sequence: L → V | ||||||
Alternative sequence | VSP_037694 | 389-400 | in isoform 11 | |||
Sequence: LENLEAETAPLP → S | ||||||
Alternative sequence | VSP_042331 | 389-400 | in isoform 14 | |||
Sequence: LENLEAETAPLP → NYYIIHRCCCNTPLISQKPVLLWFCD | ||||||
Alternative sequence | VSP_001896 | 389-400 | in isoform 2 and isoform 15 | |||
Sequence: LENLEAETAPLP → VRSL | ||||||
Alternative sequence | VSP_037695 | 389-400 | in isoform 3 | |||
Sequence: LENLEAETAPLP → CLPIPSLSCWALEQGCLVVYPGPLQGPLVRYDLPAILHSSCLRGNTAPSPSGGAFLLS | ||||||
Alternative sequence | VSP_037696 | 389-400 | in isoform 4 | |||
Sequence: LENLEAETAPLP → GPPAKFVADQLAGSS | ||||||
Alternative sequence | VSP_037697 | 389-400 | in isoform 5 | |||
Sequence: LENLEAETAPLP → PPLAVSMAQIFTRYPPPTHREKTCNDYMKR | ||||||
Alternative sequence | VSP_037698 | 389-400 | in isoform 6 | |||
Sequence: LENLEAETAPLP → IRDPISNLPRVSVF | ||||||
Alternative sequence | VSP_037699 | 389-400 | in isoform 7 | |||
Sequence: LENLEAETAPLP → KIDLFQKSSLLNCEHTKG | ||||||
Alternative sequence | VSP_037700 | 389-400 | in isoform 8 | |||
Sequence: LENLEAETAPLP → RERRQKSDW | ||||||
Alternative sequence | VSP_037701 | 389-400 | in isoform 9 | |||
Sequence: LENLEAETAPLP → VELNLDCHCENAKPWPLSYNAGQSPFPFPGRV | ||||||
Sequence conflict | 402 | In isoform P35372-3; in Ref. 4; AAK74189 | ||||
Sequence: Q → H |
Polymorphism
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L25119 EMBL· GenBank· DDBJ | AAA20580.1 EMBL· GenBank· DDBJ | mRNA | ||
U12569 EMBL· GenBank· DDBJ | AAB60354.1 EMBL· GenBank· DDBJ | mRNA | ||
L29301 EMBL· GenBank· DDBJ | AAA73958.1 EMBL· GenBank· DDBJ | mRNA | ||
AY036622 EMBL· GenBank· DDBJ | AAK74189.1 EMBL· GenBank· DDBJ | mRNA | ||
AY036623 EMBL· GenBank· DDBJ | AAK74190.1 EMBL· GenBank· DDBJ | mRNA | ||
AY195733 EMBL· GenBank· DDBJ | AAO21305.1 EMBL· GenBank· DDBJ | mRNA | ||
AY225404 EMBL· GenBank· DDBJ | AAP44727.1 EMBL· GenBank· DDBJ | mRNA | ||
AY309001 EMBL· GenBank· DDBJ | AAQ77385.1 EMBL· GenBank· DDBJ | mRNA | ||
AY309005 EMBL· GenBank· DDBJ | AAQ77389.1 EMBL· GenBank· DDBJ | mRNA | ||
AY309006 EMBL· GenBank· DDBJ | AAQ77390.1 EMBL· GenBank· DDBJ | mRNA | ||
AY309007 EMBL· GenBank· DDBJ | AAQ77391.1 EMBL· GenBank· DDBJ | mRNA | ||
AY309008 EMBL· GenBank· DDBJ | AAQ77392.1 EMBL· GenBank· DDBJ | mRNA | ||
AY309009 EMBL· GenBank· DDBJ | AAQ77393.1 EMBL· GenBank· DDBJ | mRNA | ||
EU340241 EMBL· GenBank· DDBJ | ACA49726.1 EMBL· GenBank· DDBJ | mRNA | ||
EU340242 EMBL· GenBank· DDBJ | ACA49727.1 EMBL· GenBank· DDBJ | mRNA | ||
EU340243 EMBL· GenBank· DDBJ | ACA49728.1 EMBL· GenBank· DDBJ | mRNA | ||
AY364230 EMBL· GenBank· DDBJ | AAR12887.1 EMBL· GenBank· DDBJ | mRNA | ||
AY364890 EMBL· GenBank· DDBJ | AAR11568.1 EMBL· GenBank· DDBJ | mRNA | ||
HQ699462 EMBL· GenBank· DDBJ | AET97615.1 EMBL· GenBank· DDBJ | mRNA | ||
EU360599 EMBL· GenBank· DDBJ | ABY61366.1 EMBL· GenBank· DDBJ | mRNA | ||
EU362990 EMBL· GenBank· DDBJ | ABY66530.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313901 EMBL· GenBank· DDBJ | BAG36624.1 EMBL· GenBank· DDBJ | mRNA | ||
AY521028 EMBL· GenBank· DDBJ | AAS00462.1 EMBL· GenBank· DDBJ | mRNA | ||
AY587764 EMBL· GenBank· DDBJ | AAS83107.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ041292 EMBL· GenBank· DDBJ | ACM90350.1 EMBL· GenBank· DDBJ | mRNA | ||
FJ041293 EMBL· GenBank· DDBJ | ACM90351.1 EMBL· GenBank· DDBJ | mRNA | ||
FJ041294 EMBL· GenBank· DDBJ | ACM90352.1 EMBL· GenBank· DDBJ | mRNA | ||
AL132774 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL136444 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL445220 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471051 EMBL· GenBank· DDBJ | EAW47705.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
BC074927 EMBL· GenBank· DDBJ | AAH74927.1 EMBL· GenBank· DDBJ | mRNA | ||
AY292290 EMBL· GenBank· DDBJ | AAP44409.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY292291 EMBL· GenBank· DDBJ | AAP44410.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF153500 EMBL· GenBank· DDBJ | AAD44318.1 EMBL· GenBank· DDBJ | Genomic DNA |