Q60766 · IRGM1_MOUSE
- ProteinImmunity-related GTPase family M protein 1
- GeneIrgm1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids409 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Immunity-related GTPase that plays important roles in innate immunity and inflammatory response (PubMed:11457893, PubMed:14576437, PubMed:14707092, PubMed:15908352, PubMed:16339555, PubMed:17911638, PubMed:17982087, PubMed:19620982, PubMed:19920210).
Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes (PubMed:19620982, PubMed:27098192).
Required for clearance of acute protozoan and bacterial infections by interacting with autophagy and lysosome regulatory proteins, thereby promoting the fusion of phagosomes with lysosomes for efficient degradation of cargo including microbes (PubMed:11457893, PubMed:14576437, PubMed:14707092, PubMed:15607973, PubMed:15908352, PubMed:16339555, PubMed:17982087, PubMed:19620982, PubMed:19920210, PubMed:21757726, PubMed:22874556, PubMed:24751652, PubMed:32453761).
Regulates selective autophagy, including xenophagy and mitophagy, both directly and indirectly (PubMed:15607973, PubMed:21757726).
Directly regulates autophagy by acting as a molecular adapter that promotes the coassembly of the core autophagy machinery to mediate antimicrobial defense: Irgm1 1 activates AMPK, which in turn phosphorylates ULK1 and BECN1 to induce autophagy, 2 promotes the coassembly of ULK1 and BECN1, enhancing BECN1-interacting partners and 3 influences the composition of the BECN1 complex, by competing with the negative regulators BCL2 and RUBCN, to trigger autophagy (By similarity).
Also activates autophagy by promoting recruitment of STX17 to autophagosomes (By similarity).
In collaboration with ATG8 proteins, regulate lysosomal biogenesis, a fundamental process for any autophagic pathway, by promoting TFEB dephosphorylation (By similarity).
Also modulates autophagy by assisting with autophagosome formation and preventing lysosomal deacidification (PubMed:21757726).
Regulates autophagy by affecting mitochondrial fusion and fission (PubMed:24751652).
Also involved in M1 macrophage activation for the production of proinflammatory cytokines (PubMed:15908352, PubMed:27439214, PubMed:27443879).
While activating autophagy, acts as a key negative regulator of the inflammatory and interferon responses both by 1 promoting mitophagy and 2 mediating autophagy-dependent degradation of effectors of the inflammatory response (PubMed:30612879, PubMed:33510463, PubMed:34467632).
Promotes degradation of damaged and IFNG/IFN-gamma-stressed mitochondria via mitophagy, preventing cytosolic release of ligands that activate inflammation (PubMed:32715615, PubMed:33510463).
Negatively regulates interferon-signaling in hematopoietic stem cells, preserving hematopoietic stem cell number and function (PubMed:18371424, PubMed:21633090).
Promotes expansion of activated CD4+ T-cells by inhibiting IFNG/IFN-gamma signaling, thereby preventing Ifng-mediated cell death of CD4+ T-cells (PubMed:18806793).
Acts as a suppressor of inflammation by promoting recruitment of inflammation effectors, such as CGAS, RIGI/RIG-I and NLRP3, to autophagosome membranes, leading to their SQSTM1/p62-dependent autophagic degradation (By similarity).
Also directly inhibits assembly of the NLRP3 inflammasome by preventing the association between NLRP3 and PYCARD (By similarity).
Acts as a negative regulator of antiviral innate immune response by suppressing the RIPK2-dependent pro-inflammatory response: mediates recruitment of RIPosomes, composed of RIPK2 and NOD1 or NOD2, to autophagosome membranes, promoting their SQSTM1/p62-dependent autophagic degradation (By similarity).
Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes (PubMed:19620982, PubMed:27098192).
Required for clearance of acute protozoan and bacterial infections by interacting with autophagy and lysosome regulatory proteins, thereby promoting the fusion of phagosomes with lysosomes for efficient degradation of cargo including microbes (PubMed:11457893, PubMed:14576437, PubMed:14707092, PubMed:15607973, PubMed:15908352, PubMed:16339555, PubMed:17982087, PubMed:19620982, PubMed:19920210, PubMed:21757726, PubMed:22874556, PubMed:24751652, PubMed:32453761).
Regulates selective autophagy, including xenophagy and mitophagy, both directly and indirectly (PubMed:15607973, PubMed:21757726).
Directly regulates autophagy by acting as a molecular adapter that promotes the coassembly of the core autophagy machinery to mediate antimicrobial defense: Irgm1 1 activates AMPK, which in turn phosphorylates ULK1 and BECN1 to induce autophagy, 2 promotes the coassembly of ULK1 and BECN1, enhancing BECN1-interacting partners and 3 influences the composition of the BECN1 complex, by competing with the negative regulators BCL2 and RUBCN, to trigger autophagy (By similarity).
Also activates autophagy by promoting recruitment of STX17 to autophagosomes (By similarity).
In collaboration with ATG8 proteins, regulate lysosomal biogenesis, a fundamental process for any autophagic pathway, by promoting TFEB dephosphorylation (By similarity).
Also modulates autophagy by assisting with autophagosome formation and preventing lysosomal deacidification (PubMed:21757726).
Regulates autophagy by affecting mitochondrial fusion and fission (PubMed:24751652).
Also involved in M1 macrophage activation for the production of proinflammatory cytokines (PubMed:15908352, PubMed:27439214, PubMed:27443879).
While activating autophagy, acts as a key negative regulator of the inflammatory and interferon responses both by 1 promoting mitophagy and 2 mediating autophagy-dependent degradation of effectors of the inflammatory response (PubMed:30612879, PubMed:33510463, PubMed:34467632).
Promotes degradation of damaged and IFNG/IFN-gamma-stressed mitochondria via mitophagy, preventing cytosolic release of ligands that activate inflammation (PubMed:32715615, PubMed:33510463).
Negatively regulates interferon-signaling in hematopoietic stem cells, preserving hematopoietic stem cell number and function (PubMed:18371424, PubMed:21633090).
Promotes expansion of activated CD4+ T-cells by inhibiting IFNG/IFN-gamma signaling, thereby preventing Ifng-mediated cell death of CD4+ T-cells (PubMed:18806793).
Acts as a suppressor of inflammation by promoting recruitment of inflammation effectors, such as CGAS, RIGI/RIG-I and NLRP3, to autophagosome membranes, leading to their SQSTM1/p62-dependent autophagic degradation (By similarity).
Also directly inhibits assembly of the NLRP3 inflammasome by preventing the association between NLRP3 and PYCARD (By similarity).
Acts as a negative regulator of antiviral innate immune response by suppressing the RIPK2-dependent pro-inflammatory response: mediates recruitment of RIPosomes, composed of RIPK2 and NOD1 or NOD2, to autophagosome membranes, promoting their SQSTM1/p62-dependent autophagic degradation (By similarity).
Catalytic activity
- GTP + H2O = GDP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameImmunity-related GTPase family M protein 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ60766
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Behaves like an integral membrane protein (PubMed:15294976).
Recruited to the plasma membrane around forming phagocytic cups, it remains associated with maturing phagosomes (PubMed:15294976).
Association with phagosomes is dependent on nucleotide-binding but is IFNG-independent (PubMed:15294976).
Also detected in late endosomes and lysosomes: lysosomal localization is IFN-gamma-induced during bacterial infections such as S.typhimurium infection (PubMed:17982087, PubMed:20072621).
Associates with lipid droplets and 'self' cytoplasmic vacuoles, while it does not coat 'non-self' pathogen-containing vacuoles (PubMed:23785284).
Recruited to the plasma membrane around forming phagocytic cups, it remains associated with maturing phagosomes (PubMed:15294976).
Association with phagosomes is dependent on nucleotide-binding but is IFNG-independent (PubMed:15294976).
Also detected in late endosomes and lysosomes: lysosomal localization is IFN-gamma-induced during bacterial infections such as S.typhimurium infection (PubMed:17982087, PubMed:20072621).
Associates with lipid droplets and 'self' cytoplasmic vacuoles, while it does not coat 'non-self' pathogen-containing vacuoles (PubMed:23785284).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice do not show obvious abnormalities, but are more susceptible to infection by S.typhimurium, T.cruzi, T.gondii, L.monocytogenes, C.rodentium and M.tuberculosis (PubMed:11457893, PubMed:14576437, PubMed:32453761).
Upon infection, alterations of blood elements occur including lymphopenia, anemia, and thrombocytopenia (PubMed:11457893, PubMed:14576437, PubMed:18371424).
Mice become anemic and neutropenic as a result of chronic infection, and their hematopoietic stem cells are defective in the ability to reconstitute the blood of a Bone marrow-depleted host (PubMed:18371424).
Mice display impaired expansion of activated CD4+ T-cell population: defects are caused by Infg-mediated cell death of CD4+ T-cells (PubMed:18806793).
Mice also show increased inflammation with autoimmune features (PubMed:28154172, PubMed:28814662, PubMed:30612879, PubMed:32715615, PubMed:33510463).
Macrophages show an increased production of proinflammatory cytokines associated with marked metabolic changes, characterized by increased glycolysis and an accumulation of long chain acylcarnitines (PubMed:28154172).
Mice display autoimmune disorder reminiscent of Sjogren's syndrome, characterized by up-regulation of type I interferons (PubMed:28814662).
Type I interferonopathy, characterized by up-regulation of type I interferons, is caused by activation of inflammation effectors, such as CGAS and NLRP3 (PubMed:30612879, PubMed:32715615, PubMed:33510463).
Mice show an increased antiviral innate immune response and are highly resistant to chikungunya virus (CHIKV) infection (PubMed:34467632).
Mice lacking both Irgm1 and Igtp/Irgm3 display resistance to Mycobacterium tuberculosis infection compared to Irgm1 mice that are highly susceptible to infection (PubMed:36629440).
Mice lacking Irgm1, Irgm2 and Igtp/Irgm3 (panIrgm mice) show resistance against M.tuberculosis one month post-infection; then, panIrgm mice display higher bacterial burden and altered cytokine during late stage of infection, leading to increased mortality (PubMed:36629440).
Upon infection, alterations of blood elements occur including lymphopenia, anemia, and thrombocytopenia (PubMed:11457893, PubMed:14576437, PubMed:18371424).
Mice become anemic and neutropenic as a result of chronic infection, and their hematopoietic stem cells are defective in the ability to reconstitute the blood of a Bone marrow-depleted host (PubMed:18371424).
Mice display impaired expansion of activated CD4+ T-cell population: defects are caused by Infg-mediated cell death of CD4+ T-cells (PubMed:18806793).
Mice also show increased inflammation with autoimmune features (PubMed:28154172, PubMed:28814662, PubMed:30612879, PubMed:32715615, PubMed:33510463).
Macrophages show an increased production of proinflammatory cytokines associated with marked metabolic changes, characterized by increased glycolysis and an accumulation of long chain acylcarnitines (PubMed:28154172).
Mice display autoimmune disorder reminiscent of Sjogren's syndrome, characterized by up-regulation of type I interferons (PubMed:28814662).
Type I interferonopathy, characterized by up-regulation of type I interferons, is caused by activation of inflammation effectors, such as CGAS and NLRP3 (PubMed:30612879, PubMed:32715615, PubMed:33510463).
Mice show an increased antiviral innate immune response and are highly resistant to chikungunya virus (CHIKV) infection (PubMed:34467632).
Mice lacking both Irgm1 and Igtp/Irgm3 display resistance to Mycobacterium tuberculosis infection compared to Irgm1 mice that are highly susceptible to infection (PubMed:36629440).
Mice lacking Irgm1, Irgm2 and Igtp/Irgm3 (panIrgm mice) show resistance against M.tuberculosis one month post-infection; then, panIrgm mice display higher bacterial burden and altered cytokine during late stage of infection, leading to increased mortality (PubMed:36629440).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 8 | Does not affect palmitoylation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 90 | Loss of targeting to plasma membrane and phagosomes. | ||||
Sequence: S → N | ||||||
Mutagenesis | 257-258 | Does not affect palmitoylation. | ||||
Sequence: CC → AA | ||||||
Mutagenesis | 270 | Abolished ubiquitination by the DCX(WDR77) complex. | ||||
Sequence: K → A | ||||||
Mutagenesis | 275 | Does not affect ubiquitination by the DCX(WDR77) complex. | ||||
Sequence: K → A | ||||||
Mutagenesis | 350-356 | Abolished lipid-binding and subsequent recruitment to phagosome membranes, leading to impaired innate immunity. | ||||
Sequence: KLRLMTC → ALALATA | ||||||
Mutagenesis | 356 | No effect on subcellular location. | ||||
Sequence: C → A | ||||||
Mutagenesis | 358 | No effect on subcellular location. | ||||
Sequence: I → A | ||||||
Mutagenesis | 359 | No effect on subcellular location. | ||||
Sequence: V → A | ||||||
Mutagenesis | 360 | No effect on subcellular location. Abolishes Golgi and lysosomal localization; when associated with A-364. | ||||
Sequence: N → A | ||||||
Mutagenesis | 362 | No effect on subcellular location. | ||||
Sequence: F → A | ||||||
Mutagenesis | 362 | Decreased lipid-binding. | ||||
Sequence: F → E | ||||||
Mutagenesis | 362 | Disrupts amphipathicity and abolishes Golgi localization; when associated with Glu-367. | ||||
Sequence: F → EF | ||||||
Mutagenesis | 362-367 | Abolished lipid-binding and subsequent recruitment to phagosome membranes, leading to impaired innate immunity. | ||||
Sequence: FFRLLR → EFRLLE | ||||||
Mutagenesis | 363 | No effect on subcellular location. | ||||
Sequence: F → A | ||||||
Mutagenesis | 364 | No effect on subcellular location. Abolishes Golgi and lysosomal localization; when associated with A-360 or A-367. | ||||
Sequence: R → A | ||||||
Mutagenesis | 365 | No effect on subcellular location. | ||||
Sequence: L → A | ||||||
Mutagenesis | 366 | No effect on subcellular location. | ||||
Sequence: L → A | ||||||
Mutagenesis | 367 | No effect on subcellular location. Abolishes Golgi and lysosomal localization; when associated with A-364. | ||||
Sequence: R → A | ||||||
Mutagenesis | 367 | Disrupts amphipathicity and abolishes Golgi localization; when associated with Glu-362. | ||||
Sequence: R → ER | ||||||
Mutagenesis | 371-375 | Abolished palmitoylation and localization to membranes. | ||||
Sequence: CVCCC → AVAAA | ||||||
Mutagenesis | 398 | Does not affect ubiquitination by the DCX(WDR77) complex. | ||||
Sequence: K → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 29 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000325750 | 1-409 | Immunity-related GTPase family M protein 1 | |||
Sequence: MKPSHSSCEAAPLLPNMAETHYAPLSSAFPFVTSYQTGSSRLPEVSRSTERALREGKLLELVYGIKETVATLSQIPVSIFVTGDSGNGMSSFINALRVIGHDEDASAPTGVVRTTKTRTEYSSSHFPNVVLWDLPGLGATAQTVEDYVEEMKFSTCDLFIIIASEQFSSNHVKLSKIIQSMGKRFYIVWTKLDRDLSTSVLSEVRLLQNIQENIRENLQKEKVKYPPVFLVSSLDPLLYDFPKLRDTLHKDLSNIRCCEPLKTLYGTYEKIVGDKVAVWKQRIANESLKNSLGVRDDDNMGECLKVYRLIFGVDDESVQQVAQSMGTVVMEYKDNMKSQNFYTLRREDWKLRLMTCAIVNAFFRLLRFLPCVCCCLRRLRHKRMLFLVAQDTKNILEKILRDSIFPPQI | ||||||
Modified residue | 202 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 270 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Palmitoylated on C-terminal Cys residues (PubMed:24751652).
Palmitoylation, together with the alpha-K amphipathic helix, which binds phosphatidylinositol, mediate binding to membranes (PubMed:24751652).
Palmitoylation, together with the alpha-K amphipathic helix, which binds phosphatidylinositol, mediate binding to membranes (PubMed:24751652).
Ubiquitinated via 'Lys-63'-linked polyubiquitination in a NOD2-dependent process. 'Lys-63'-linked polyubiquitination is required for interactions with the core autophagy factors (By similarity).
Ubiquitination at Lys-270 by the DCX(WDR77) complex, also named CLR4(WDR77) complex, in intestinal cells, leading to its degradation by the proteasome (PubMed:35197566).
Ubiquitination at Lys-270 by the DCX(WDR77) complex, also named CLR4(WDR77) complex, in intestinal cells, leading to its degradation by the proteasome (PubMed:35197566).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in lung and primary macrophages.
Induction
Up-regulated by LPS and IFNG (at protein level) (PubMed:11457893, PubMed:14576437, PubMed:15294976, PubMed:17911638, PubMed:7561525).
Up-regulated upon infection by various pathogens including T.cruzi, T.gondii, L.monocytogenes, M.tuberculosis and murine cytomegalovirus (PubMed:14707092, PubMed:16339555).
Up-regulated upon infection by various pathogens including T.cruzi, T.gondii, L.monocytogenes, M.tuberculosis and murine cytomegalovirus (PubMed:14707092, PubMed:16339555).
Gene expression databases
Interaction
Subunit
Interacts with ULK1; promoting the coassembly of ULK1 and BECN1. Interacts with BECN1; enhancing BECN1-interacting partners and influencing the composition of the BECN1 complex. Interacts with ATG16L1. Interacts with NOD2; promoting Irgm1 'Lys-63'-linked polyubiquitination, which is required for interactions with the core autophagy factors (By similarity).
Interacts with STX17; promoting STX17 recruitment to autophagosomes (By similarity).
Interacts with ATG8 proteins (GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C); promoting STX17 recruitment to autophagosomes (By similarity).
Interacts with TFEB; promoting association between TFEB and PPP3CB and TFEB dephosphorylation (By similarity).
Interacts with PPP3CB; promoting association between TFEB and PPP3CB and TFEB dephosphorylation (By similarity).
Interacts with NLRP3; preventing NLRP3 inflammasome assembly and promoting SQSTM1/p62-dependent autophagic degradation of NLRP3 (By similarity).
Interacts with CGAS; promoting SQSTM1/p62-dependent autophagic degradation of CGAS (By similarity).
Interacts with RIGI/RIG-I; promoting SQSTM1/p62-dependent autophagic degradation of RIGI/RIG-I (By similarity).
Interacts with NOD1; promoting SQSTM1/p62-dependent autophagic degradation of RIGI/RIG-I (By similarity).
Interacts with NOD2; promoting SQSTM1/p62-dependent autophagic degradation of RIGI/RIG-I (By similarity).
Interacts with RIPK2; promoting SQSTM1/p62-dependent autophagic degradation of RIGI/RIG-I (By similarity).
Interacts with PIK3CA (PubMed:19620982).
Interacts with STX17; promoting STX17 recruitment to autophagosomes (By similarity).
Interacts with ATG8 proteins (GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C); promoting STX17 recruitment to autophagosomes (By similarity).
Interacts with TFEB; promoting association between TFEB and PPP3CB and TFEB dephosphorylation (By similarity).
Interacts with PPP3CB; promoting association between TFEB and PPP3CB and TFEB dephosphorylation (By similarity).
Interacts with NLRP3; preventing NLRP3 inflammasome assembly and promoting SQSTM1/p62-dependent autophagic degradation of NLRP3 (By similarity).
Interacts with CGAS; promoting SQSTM1/p62-dependent autophagic degradation of CGAS (By similarity).
Interacts with RIGI/RIG-I; promoting SQSTM1/p62-dependent autophagic degradation of RIGI/RIG-I (By similarity).
Interacts with NOD1; promoting SQSTM1/p62-dependent autophagic degradation of RIGI/RIG-I (By similarity).
Interacts with NOD2; promoting SQSTM1/p62-dependent autophagic degradation of RIGI/RIG-I (By similarity).
Interacts with RIPK2; promoting SQSTM1/p62-dependent autophagic degradation of RIGI/RIG-I (By similarity).
Interacts with PIK3CA (PubMed:19620982).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 75-251 | IRG-type G | ||||
Sequence: IPVSIFVTGDSGNGMSSFINALRVIGHDEDASAPTGVVRTTKTRTEYSSSHFPNVVLWDLPGLGATAQTVEDYVEEMKFSTCDLFIIIASEQFSSNHVKLSKIIQSMGKRFYIVWTKLDRDLSTSVLSEVRLLQNIQENIRENLQKEKVKYPPVFLVSSLDPLLYDFPKLRDTLHKD | ||||||
Region | 350-374 | Alpha-K amphipathic helix | ||||
Sequence: KLRLMTCAIVNAFFRLLRFLPCVCC |
Domain
The alpha-K amphipathic helix mediates targeting to the phagosome membrane via binding to phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4)P2) and phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3).
Sequence similarities
Belongs to the TRAFAC class dynamin-like GTPase superfamily. IRG family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q60766-1
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
- Length409
- Mass (Da)46,552
- Last updated1996-11-01 v1
- ChecksumE4913367193059B6
Q60766-2
- Name2
- Differences from canonical
- 1-16: Missing
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_032384 | 1-16 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 151 | in Ref. 2; BAE39622 | ||||
Sequence: M → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U19119 EMBL· GenBank· DDBJ | AAB48942.1 EMBL· GenBank· DDBJ | mRNA | ||
AK002545 EMBL· GenBank· DDBJ | BAB22176.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167558 EMBL· GenBank· DDBJ | BAE39622.1 EMBL· GenBank· DDBJ | mRNA | ||
AK171743 EMBL· GenBank· DDBJ | BAE42645.1 EMBL· GenBank· DDBJ | mRNA | ||
AL645849 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC145957 EMBL· GenBank· DDBJ | AAI45958.1 EMBL· GenBank· DDBJ | mRNA |