Q63042 (ALR_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: FAD-linked sulfhydryl oxidase ALR EC=1.8.3.2 Alternative name(s): Augmenter of liver regeneration | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 198 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Within the mitochondrial intermembrane space, participates in a chain of disulfide exchange reactions with MIA40, that generate disulfide bonds in a number of resident proteins with twin Cx3C and Cx9C motifs. May have a function in liver regeneration and spermatogenesis. Ref.1 |
| Catalytic activity | 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2. |
| Cofactor | FAD. Ref.4 |
| Subunit structure | Homodimer; disulfide-linked. Ref.4 |
| Subcellular location | Cytoplasm. Mitochondrion intermembrane space By similarity. |
| Sequence similarities | Contains 1 ERV/ALR sulfhydryl oxidase domain. |
| Sequence caution | The sequence AAF12808.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA06399.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Mitochondrion |
| Ligand | FAD Flavoprotein |
| Molecular function | Growth factor Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | growth factor activity Inferred from electronic annotation. Source: UniProtKB-KW thiol oxidase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||
Molecule processing | ||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 198 | 198 | FAD-linked sulfhydryl oxidase ALR | PRO_0000208550 | ||||||||||||||||
Regions | ||||||||||||||||||||
| Domain | 88 – 188 | 101 | ERV/ALR sulfhydryl oxidase | |||||||||||||||||
| Region | 171 – 188 | 18 | FAD-binding | |||||||||||||||||
Sites | ||||||||||||||||||||
| Binding site | 92 | 1 | FAD By similarity | |||||||||||||||||
| Binding site | 93 | 1 | FAD By similarity | |||||||||||||||||
| Binding site | 97 | 1 | FAD By similarity | |||||||||||||||||
| Binding site | 164 | 1 | FAD By similarity | |||||||||||||||||
| Binding site | 167 | 1 | FAD By similarity | |||||||||||||||||
| Binding site | 173 | 1 | FAD By similarity | |||||||||||||||||
| Binding site | 187 | 1 | FAD By similarity | |||||||||||||||||
Amino acid modifications | ||||||||||||||||||||
| Disulfide bond | 88 | Interchain (with C-197) Ref.4 | ||||||||||||||||||
| Disulfide bond | 135 ↔ 138 | Redox-active Potential | ||||||||||||||||||
| Disulfide bond | 164 ↔ 181 | Ref.4 | ||||||||||||||||||
| Disulfide bond | 197 | Interchain (with C-88) Ref.4 | ||||||||||||||||||
Secondary structure | ||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||
| Helix | 92 – 108 | 17 | ||||||||||||||||||
| Helix | 116 – 132 | 17 | ||||||||||||||||||
| Helix | 136 – 148 | 13 | ||||||||||||||||||
| Helix | 156 – 173 | 18 | ||||||||||||||||||
| Helix | 181 – 183 | 3 | ||||||||||||||||||
| Helix | 184 – 188 | 5 | ||||||||||||||||||
Sequences
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References
| [1] | "Cloning and sequence analysis of the rat augmenter of liver regeneration (ALR) gene: expression of biologically active recombinant ALR and demonstration of tissue distribution." Hagiya M., Francavilla A., Polimeno L., Ihara I., Sakai H., Seki T., Shimonishi M., Porter K.A., Starzl T.E. Proc. Natl. Acad. Sci. U.S.A. 91:8142-8146(1994) [PubMed: 8058770] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN LIVER REGENERATION. Strain: Fischer 344. Tissue: Liver. |
| [2] | Erratum Hagiya M., Francavilla A., Polimeno L., Ihara I., Sakai H., Seki T., Shimonishi M., Porter K.A., Starzl T.E. Proc. Natl. Acad. Sci. U.S.A. 92:3076-3076(1995) [PubMed: 7708779] [Abstract] |
| [3] | "Cloning and analysis of the genomic DNA sequence of augmenter of liver regeneration from rat." Dong J., Cheng J., Wang Q., Shi S., Wang G., Si C. Chin. Med. Sci. J. 17:63-67(2002) [PubMed: 12906155] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Wistar. |
| [4] | "The crystal structure of augmenter of liver regeneration: a mammalian FAD-dependent sulfhydryl oxidase." Wu C.-K., Dailey T.A., Dailey H.A., Wang B.-C., Rose J.P. Protein Sci. 12:1109-1118(2003) [PubMed: 12717032] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, COFACTOR, DISULFIDE BONDS. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | D30735 mRNA. Translation: BAA06399.1. Different initiation. AF197192 Genomic DNA. Translation: AAF12808.1. Different initiation. | ||||||||||||
| IPI | IPI00326141. | ||||||||||||
| PIR | I80184. | ||||||||||||
| RefSeq | NP_037354.2. NM_013222.2. | ||||||||||||
| UniGene | Rn.11039. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | Q63042. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSRNOT00000017917; ENSRNOP00000017917; ENSRNOG00000013370. | ||||||||||||
| GeneID | 27100. | ||||||||||||
| KEGG | rno:27100. | ||||||||||||
| UCSC | NM_013222. rat. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 2671. | ||||||||||||
| RGD | 61845. Gfer. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | roNOG12723. | ||||||||||||
| GeneTree | ENSGT00390000001979. | ||||||||||||
| HOVERGEN | HBG000235. | ||||||||||||
| InParanoid | Q63042. | ||||||||||||
| OMA | CTDFKSW. | ||||||||||||
| OrthoDB | EOG4M91ST. | ||||||||||||
| PhylomeDB | Q63042. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 1.8.3.2. 5301. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q63042. | ||||||||||||
| Genevestigator | Q63042. | ||||||||||||
| GermOnline | ENSRNOG00000013370. Rattus norvegicus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR017905. ERV/ALR_sulphydryl_oxidase. IPR006863. Evr1_Alr. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.20.120.310. Evr1_Alr. 1 hit. | ||||||||||||
| Pfam | PF04777. Evr1_Alr. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF69000. Evr1_Alr. 1 hit. | ||||||||||||
| PROSITE | PS51324. ERV_ALR. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| NextBio | 608049. | ||||||||||||
Entry information
| Entry name | ALR_RAT | ||||||||
| Accession | Primary (citable) accession number: Q63042 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with