P02760 · AMBP_HUMAN
- ProteinProtein AMBP
- GeneAMBP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids352 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Alpha-1-microglobulin
Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments (PubMed:11877257, PubMed:15683711, PubMed:22096585, PubMed:23157686, PubMed:23642167, PubMed:25698971, PubMed:32092412, PubMed:32823731).
Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis (PubMed:11877257, PubMed:32092412).
Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential (PubMed:15683711).
Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage (PubMed:25698971).
Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures (PubMed:22096585, PubMed:23642167).
Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation (PubMed:21356557).
Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria (PubMed:23157686, PubMed:32823731).
Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (PubMed:15683711).
Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity).
Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis (PubMed:11877257, PubMed:32092412).
Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential (PubMed:15683711).
Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage (PubMed:25698971).
Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures (PubMed:22096585, PubMed:23642167).
Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation (PubMed:21356557).
Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria (PubMed:23157686, PubMed:32823731).
Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (PubMed:15683711).
Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity).
Inter-alpha-trypsin inhibitor light chain
Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion (PubMed:20463016, PubMed:25301953).
Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule-stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases (PubMed:10480954, PubMed:15917224, PubMed:16873769).
As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (PubMed:16873769).
Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity).
Also inhibits calcium oxalate crystallization (PubMed:7676539).
Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule-stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases (PubMed:10480954, PubMed:15917224, PubMed:16873769).
As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (PubMed:16873769).
Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity).
Also inhibits calcium oxalate crystallization (PubMed:7676539).
Trypstatin
Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases.
Miscellaneous
In vitro, the first twelve residues of the amino end of the inhibitor appear to have a reactive site capable of inhibiting the activity of a number of enzymes. Its in vivo function is not known.
Activity regulation
Inter-alpha-trypsin inhibitor light chain
Up-regulated by TNFAIP6. In a transesterification reaction, TNFAIP6 cleaves the ester bond between the heavy chain and the chondroitin sulfate chain in I-alpha-I complex and potentiates the antiprotease function of I-alpha-I complex through release of free bikunin.
pH Dependence
The reductase activity toward cytochrome c increases at alkaline pH 8-9 when compared to pH 6-7.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 53 | 3-hydroxy-L-kynurenine (UniProtKB | ChEBI); multimeric 3-hydroxykynurenine chromophore; covalent | ||||
Sequence: C | ||||||
Binding site | 111 | 3-hydroxy-L-kynurenine (UniProtKB | ChEBI); multimeric 3-hydroxykynurenine chromophore; covalent | ||||
Sequence: K | ||||||
Binding site | 137 | 3-hydroxy-L-kynurenine (UniProtKB | ChEBI); multimeric 3-hydroxykynurenine chromophore; covalent | ||||
Sequence: K | ||||||
Binding site | 149 | 3-hydroxy-L-kynurenine (UniProtKB | ChEBI); multimeric 3-hydroxykynurenine chromophore; covalent | ||||
Sequence: K | ||||||
Site | 199 | Cleavage; in the presence of oxyhemoglobin or MPO | ||||
Sequence: L | ||||||
Site | 241-242 | Inhibitory (P1) (chymotrypsin, elastase) | ||||
Sequence: MG | ||||||
Site | 297-298 | Inhibitory (P1) (trypsin) | ||||
Sequence: RA |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | blood microparticle | |
Cellular Component | cell surface | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | mitochondrial inner membrane | |
Cellular Component | nuclear membrane | |
Cellular Component | plasma membrane | |
Molecular Function | calcium channel inhibitor activity | |
Molecular Function | calcium oxalate binding | |
Molecular Function | carbohydrate binding | |
Molecular Function | heme binding | |
Molecular Function | IgA binding | |
Molecular Function | oxidoreductase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | serine-type endopeptidase inhibitor activity | |
Biological Process | cell adhesion | |
Biological Process | female pregnancy | |
Biological Process | heme catabolic process | |
Biological Process | negative regulation of immune response | |
Biological Process | negative regulation of JNK cascade |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtein AMBP
- Alternative names
- Cleaved into 3 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP02760
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Alpha-1-microglobulin
Cell membrane ; Peripheral membrane protein
Nucleus membrane ; Peripheral membrane protein
Mitochondrion inner membrane ; Peripheral membrane protein
Note: The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I.
Inter-alpha-trypsin inhibitor light chain
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 53 | Impairs the reductase activity toward cytochrome c independently of the electron donnor. Decreases the reductase activity toward methemoglobin. Decreases the reductase activity toward oxidized collagen. | ||||
Sequence: C → S | ||||||
Mutagenesis | 111 | Impairs the reductase activity toward cytochrome c in the presence of NADPH; when associated with T-137 and T-149. Impairs the reductase activity toward oxidized collagen; when associated with T-137 and T-149. | ||||
Sequence: K → T | ||||||
Mutagenesis | 137 | Impairs the reductase activity toward cytochrome c in the presence of NADPH; when associated with T-111 and T-149. Impairs the reductase activity toward oxidized collagen; when associated with T-111 and T-149. | ||||
Sequence: K → T | ||||||
Mutagenesis | 149 | Impairs the reductase activity toward cytochrome c in the presence of NADPH; when associated with T-111 and T-137. Impairs the reductase activity toward oxidized collagen; when associated with T-111 and T-137. | ||||
Sequence: K → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 443 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MRSLGALLLLLSACLAVSA | ||||||
Chain | PRO_0000017886 | 20-203 | Alpha-1-microglobulin | |||
Sequence: GPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRV | ||||||
Glycosylation | CAR_000172 | 24 | O-linked (GalNAc...) threonine | |||
Sequence: T | ||||||
Glycosylation | 36 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 91↔188 | |||||
Sequence: CEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGEC | ||||||
Glycosylation | 115 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000017887 | 206-352 | Inter-alpha-trypsin inhibitor light chain | |||
Sequence: AVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN | ||||||
Glycosylation | 215 | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | ||||||
Disulfide bond | 231↔281 | |||||
Sequence: CQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTC | ||||||
Disulfide bond | 240↔264 | |||||
Sequence: CMGMTSRYFYNGTSMACETFQYGGC | ||||||
Glycosylation | 250 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 256↔277 | |||||
Sequence: CETFQYGGCMGNGNNFVTEKEC | ||||||
Chain | PRO_0000318926 | 284-344 | Trypstatin | |||
Sequence: VAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGD | ||||||
Disulfide bond | 287↔337 | |||||
Sequence: CNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYC | ||||||
Disulfide bond | 296↔320 | |||||
Sequence: CRAFIQLWAFDAVKGKCVLFPYGGC | ||||||
Disulfide bond | 312↔333 | |||||
Sequence: CVLFPYGGCQGNGNKFYSEKEC |
Post-translational modification
The precursor is proteolytically processed into separately functioning proteins.
Alpha-1-microglobulin
Proteolytically cleaved in the presence of oxyhemoglobin or MPO (PubMed:11877257, PubMed:25698971).
The cleaved form t-alpha-1-microglobulin lacks the C-terminal tetrapeptide LIPR and is released from IgA-alpha-1-microglobulin complex as well as from free alpha-1-microglobulin when exposed to oxyhemoglobin or erythrocyte membranes. The cleavage of IgA-alpha-1-microglobulin complex is associated with the reduction of the covalent bond between IgA and alpha-1-microglobulin, yielding an intact IgA molecule (PubMed:11877257).
The cleavage by MPO is associated with the transfer of heme group from MPO to t-alpha-1-microglobulin (PubMed:25698971).
t-alpha-1-microglobulin has higher reductase activity when compared with full length protein (PubMed:15683711).
The cleaved form t-alpha-1-microglobulin lacks the C-terminal tetrapeptide LIPR and is released from IgA-alpha-1-microglobulin complex as well as from free alpha-1-microglobulin when exposed to oxyhemoglobin or erythrocyte membranes. The cleavage of IgA-alpha-1-microglobulin complex is associated with the reduction of the covalent bond between IgA and alpha-1-microglobulin, yielding an intact IgA molecule (PubMed:11877257).
The cleavage by MPO is associated with the transfer of heme group from MPO to t-alpha-1-microglobulin (PubMed:25698971).
t-alpha-1-microglobulin has higher reductase activity when compared with full length protein (PubMed:15683711).
Alpha-1-microglobulin
3-hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with Cys-53, Lys-111, Lys-137, and Lys-149 to form heterogeneous polycyclic chromophores including hydroxanthommatin. The reaction by alpha-1-microglobulin is autocatalytic; the human protein forms chromophore even when expressed in insect and bacterial cells. The chromophore can react with accessible cysteines forming non-reducible thioether cross-links with other molecules of alpha-1-microglobulin or with other proteins such as Ig alpha-1 chain C region 'Cys-352'.
Inter-alpha-trypsin inhibitor light chain
Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the C-terminal aspartate.
Inter-alpha-trypsin inhibitor light chain
Proteolytically cleaved by PRSS3 at Kunitz domain 2.
N-glycosylated. N-glycan heterogeneity at Asn-115: Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5 (minor). N-glycan at Asn-250: Hex5HexNAc4.
O-glycosylated. O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Alpha-1-microglobulin
Expressed by the liver and secreted in plasma. Occurs in many physiological fluids including plasma, urine, and cerebrospinal fluid (PubMed:11877257).
Expressed in epidermal keratinocytes, in dermis and epidermal-dermal junction (at protein level) (PubMed:22096585).
Expressed in red blood cells (at protein level) (PubMed:32092412).
Expressed in placenta (PubMed:21356557).
Expressed in epidermal keratinocytes, in dermis and epidermal-dermal junction (at protein level) (PubMed:22096585).
Expressed in red blood cells (at protein level) (PubMed:32092412).
Expressed in placenta (PubMed:21356557).
Inter-alpha-trypsin inhibitor light chain
Detected in placenta (at protein level) (PubMed:32337544).
Detected in cerebrospinal fluid, plasma and urine (at protein level) (PubMed:25326458, PubMed:36213313, PubMed:37453717).
Expressed in airway epithelium and submucosal gland (at protein level). Colocalizes with TNFAIP6 at the ciliary border. Present in bronchoalveolar lavage fluid (at protein level)
Detected in cerebrospinal fluid, plasma and urine (at protein level) (PubMed:25326458, PubMed:36213313, PubMed:37453717).
Expressed in airway epithelium and submucosal gland (at protein level). Colocalizes with TNFAIP6 at the ciliary border. Present in bronchoalveolar lavage fluid (at protein level)
Induction
Alpha-1-microglobulin
Up-regulated upon oxidative stress (PubMed:21356557, PubMed:22096585, PubMed:23642167).
Up-regulated in keratinocytes upon exposure to heme and reactive oxygen species (PubMed:22096585).
Up-regulated in hemoglobin-perfused placenta (PubMed:21356557).
Up-regulated in keratinocytes upon exposure to heme and reactive oxygen species (PubMed:22096585).
Up-regulated in hemoglobin-perfused placenta (PubMed:21356557).
Inter-alpha-trypsin inhibitor light chain
Up-regulated in airway epithelium and submucosal gland in response to inflammatory cytokine TNF.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Alpha-1-microglobulin
Monomer (PubMed:22512701, PubMed:9183005).
Homodimer (PubMed:9183005).
In plasma, it occurs as a monomer or dimer and in covalently-linked complexes with immunoglobulin A (IgA), ALB/albumin and F2/prothrombin (PubMed:9183005).
Chromophore-bound alpha-1-microglobulin interacts with the constant region of immunoglobulin A (PubMed:9183005).
Chromophore-bound alpha-1-microglobulin interacts with ALB with molar ratio 2:1 and 1:1; this interaction does not prevent fatty acid binding to ALB (PubMed:9183005).
Interacts with F2/prothrombin (via N-terminus) with molar ratio 2:1 and 1:1; this interaction does not prevent the activation of prothrombin to thrombin (PubMed:9183005).
Interacts with NDUFAB1, a subunit of mitochondrial complex I (PubMed:23157686).
Interacts with FN1 (By similarity).
Homodimer (PubMed:9183005).
In plasma, it occurs as a monomer or dimer and in covalently-linked complexes with immunoglobulin A (IgA), ALB/albumin and F2/prothrombin (PubMed:9183005).
Chromophore-bound alpha-1-microglobulin interacts with the constant region of immunoglobulin A (PubMed:9183005).
Chromophore-bound alpha-1-microglobulin interacts with ALB with molar ratio 2:1 and 1:1; this interaction does not prevent fatty acid binding to ALB (PubMed:9183005).
Interacts with F2/prothrombin (via N-terminus) with molar ratio 2:1 and 1:1; this interaction does not prevent the activation of prothrombin to thrombin (PubMed:9183005).
Interacts with NDUFAB1, a subunit of mitochondrial complex I (PubMed:23157686).
Interacts with FN1 (By similarity).
Inter-alpha-trypsin inhibitor light chain
I-alpha-I plasma protease inhibitors are assembled from one or two heavy chains (HC) and one light chain, bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of ITIH1/HC1, ITIH2/HC2 and bikunin, and pre-alpha-inhibitor (P-alpha-I) of ITIH3/HC3 and bikunin (PubMed:16873769, PubMed:2476436).
Interacts with TNFAIP6 (via Link domain) (PubMed:15917224).
Interacts with TNFAIP6 (via Link domain) (PubMed:15917224).
Trypstatin
Monomer. Also occurs as a complex with tryptase in mast cells.
Alpha-1-microglobulin
(Microbial infection) Interacts with hepatitis E virus/HEV protein ORF3.
Inter-alpha-trypsin inhibitor light chain
(Microbial infection) Interacts with hepatitis E virus/HEV protein ORF3.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P02760 | CTSB P07858 | 4 | EBI-2115136, EBI-715062 | |
BINARY | P02760 | FHL3 Q13643 | 3 | EBI-2115136, EBI-741101 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 206-226 | Glycopeptide (secretory piece) | ||||
Sequence: AVLPQEEEGSGGGQLVTEVTK | ||||||
Domain | 231-281 | BPTI/Kunitz inhibitor 1 | ||||
Sequence: CQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTC | ||||||
Domain | 287-337 | BPTI/Kunitz inhibitor 2 | ||||
Sequence: CNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYC |
Domain
Inter-alpha-trypsin inhibitor light chain
The Kunitz domains 1 and 2 serve as protease inhibitor domains.
Sequence similarities
In the N-terminal section; belongs to the calycin superfamily. Lipocalin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length352
- Mass (Da)38,999
- Last updated1987-08-13 v1
- ChecksumBC001780094CBD06
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 48-57 | in Ref. 11; AA sequence | ||||
Sequence: Missing | ||||||
Sequence conflict | 57 | in Ref. 10; AA sequence and 12; AA sequence | ||||
Sequence: Missing | ||||||
Sequence conflict | 137 | in Ref. 11; AA sequence | ||||
Sequence: Missing | ||||||
Sequence conflict | 142 | in Ref. 11; AA sequence | ||||
Sequence: H → T | ||||||
Sequence conflict | 145 | in Ref. 11; AA sequence | ||||
Sequence: Missing | ||||||
Sequence conflict | 194 | in Ref. 11; AA sequence | ||||
Sequence: E → Q | ||||||
Sequence conflict | 215 | in Ref. 18; AA sequence | ||||
Sequence: S → T | ||||||
Sequence conflict | 218 | in Ref. 18; AA sequence | ||||
Sequence: G → T | ||||||
Sequence conflict | 291-292 | in Ref. 14; AA sequence and 15; AA sequence | ||||
Sequence: IV → VI | ||||||
Sequence conflict | 295 | in Ref. 15; AA sequence | ||||
Sequence: Missing | ||||||
Sequence conflict | 343 | in Ref. 14; AA sequence | ||||
Sequence: G → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X04225 EMBL· GenBank· DDBJ | CAA27803.1 EMBL· GenBank· DDBJ | mRNA | ||
X04494 EMBL· GenBank· DDBJ | CAA28182.1 EMBL· GenBank· DDBJ | mRNA | ||
X54816 EMBL· GenBank· DDBJ | CAA38585.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X54817 EMBL· GenBank· DDBJ | CAA38585.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X54818 EMBL· GenBank· DDBJ | CAA38585.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X54817 EMBL· GenBank· DDBJ | CAA38586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X54818 EMBL· GenBank· DDBJ | CAA38587.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M88249 EMBL· GenBank· DDBJ | AAA59196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M88165 EMBL· GenBank· DDBJ | AAA59196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M88243 EMBL· GenBank· DDBJ | AAA59196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M88244 EMBL· GenBank· DDBJ | AAA59196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M88246 EMBL· GenBank· DDBJ | AAA59196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M88247 EMBL· GenBank· DDBJ | AAA59196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY544123 EMBL· GenBank· DDBJ | AAT11154.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290837 EMBL· GenBank· DDBJ | BAF83526.1 EMBL· GenBank· DDBJ | mRNA | ||
AL137850 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471090 EMBL· GenBank· DDBJ | EAW87404.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC041593 EMBL· GenBank· DDBJ | AAH41593.1 EMBL· GenBank· DDBJ | mRNA |