Q9C9L4 (HMOX3_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 68.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Heme oxygenase 3, chloroplastic EC=1.14.99.3 | ||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Reference proteome] | ||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis![]() |
Protein attributes
| Sequence length | 285 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Plays a minor role in phytochrome assembly and photomorphogenesis. Ref.5 Ref.6 |
| Catalytic activity | Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. |
| Subcellular location | |
| Tissue specificity | Widely expressed at low levels. Ref.5 |
| Disruption phenotype | No visible phenotype under normal growth conditions. Ref.5 |
| Sequence similarities | Belongs to the heme oxygenase family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 7.0. Ref.6 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Photosynthesis |
| Cellular component | Chloroplast Plastid |
| Coding sequence diversity | Alternative splicing |
| Domain | Transit peptide |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | heme oxidation Inferred from electronic annotation. Source: InterPro photosynthesisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | chloroplast Inferred from direct assay PubMed 10072395. Source: TAIR |
| Molecular_function | heme binding Inferred from direct assay Ref.6. Source: TAIR heme oxygenase (decyclizing) activityInferred from direct assay Ref.5Ref.6. Source: TAIR metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9C9L4-1) 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. | ||||||
| Isoform 2 (identifier: Q9C9L4-2) The sequence of this isoform differs from the canonical sequence as follows: 220-227: VSKKILDN → LCRYLRRY 228-285: Missing. | ||||||
| Note: Derived from EST data. No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 58 | 58 | Chloroplast Potential | ||||||
| Chain | 59 – 285 | 227 | Heme oxygenase 3, chloroplastic | PRO_0000412187 | |||||
Sites | |||||||||
| Metal binding | 89 | 1 | Iron (heme axial ligand) By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 220 – 227 | 8 | VSKKILDN → LCRYLRRY in isoform 2. | VSP_041653 | |||||
| Alternative sequence | 228 – 285 | 58 | Missing in isoform 2. | VSP_041654 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The heme-oxygenase family required for phytochrome chromophore biosynthesis is necessary for proper photomorphogenesis in higher plants." Davis S.J., Bhoo S.H., Durski A.M., Walker J.M., Vierstra R.D. Plant Physiol. 126:656-669(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. Davis R.W.Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [3] | The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia. |
| [4] | "Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). |
| [5] | "Multiple heme oxygenase family members contribute to the biosynthesis of the phytochrome chromophore in Arabidopsis." Emborg T.J., Walker J.M., Noh B., Vierstra R.D. Plant Physiol. 140:856-868(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE. |
| [6] | "Characterization of the haem oxygenase protein family in Arabidopsis thaliana reveals a diversity of functions." Gisk B., Yasui Y., Kohchi T., Frankenberg-Dinkel N. Biochem. J. 425:425-434(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF320022 Genomic DNA. Translation: AAK63006.1. AC013289 Genomic DNA. Translation: AAG52552.1. CP002684 Genomic DNA. Translation: AEE34966.1. CP002684 Genomic DNA. Translation: AEE34967.1. AY084250 mRNA. Translation: AAM60844.1. |
| IPI | IPI00548070. IPI00891017. |
| PIR | B96719. |
| RefSeq | NP_001117574.1. NM_001124102.1. NP_177130.1. NM_105640.3. |
| UniGene | At.35382. At.71252. |
3D structure databases | |
| ProteinModelPortal | Q9C9L4. |
| SMR | Q9C9L4. Positions 153-280. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 3702.AT1G69720.1-P. |
Proteomic databases | |
| PRIDE | Q9C9L4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 843308. |
| KEGG | ath:AT1G69720. |
Organism-specific databases | |
| TAIR | At1g69720. |
Phylogenomic databases | |
| eggNOG | NOG308332. |
| HOGENOM | HOG000265822. |
| InParanoid | Q9C9L4. |
| KO | K00510. |
| OMA | ISYARTL. |
| PhylomeDB | Q9C9L4. |
| ProtClustDB | CLSN2682571. |
Gene expression databases | |
| Genevestigator | Q9C9L4. |
Family and domain databases | |
| Gene3D | 1.20.910.10. 1 hit. |
| InterPro | IPR016053. Haem_Oase-like. IPR016084. Haem_Oase-like_multi-hlx. IPR016951. Haem_Oase_decyc_pln. [Graphical view] |
| Pfam | PF01126. Heme_oxygenase. 1 hit. [Graphical view] |
| PIRSF | PIRSF030219. Heme_Oase_decyc_pln. 1 hit. |
| SUPFAM | SSF48613. Heme_oxygenase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | HMOX3_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9C9L4 Secondary accession number(s): B3H531 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
