P92983 (PROD1_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 102.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Proline dehydrogenase 1, mitochondrial EC=1.5.99.8 Alternative name(s): Osmotic stress-induced proline dehydrogenase Proline oxidase Protein EARLY RESPONSIVE TO DEHYDRATION 5 | ||||||||
| 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 | 499 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 | Converts proline to delta-1-pyrroline-5-carboxylate. Ref.8 Ref.11 |
| Catalytic activity | L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor. |
| Cofactor | FAD. |
| Pathway | Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2. |
| Subcellular location | |
| Tissue specificity | Ubiquitous. Highest expression in pollen grains, in the stigma and in developing embryos. Ref.8 Ref.11 |
| Induction | Down-regulated by salt or drought stress. Up-regulated by proline, hypoosmolarity or rehydration. Ref.1 Ref.8 Ref.10 Ref.11 |
| Disruption phenotype | No visible phenotype when grown under normal conditions. Proline hypersensitivity. Ref.9 Ref.11 |
| Sequence similarities | Belongs to the proline oxidase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Proline metabolism Stress response |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | defense response to bacterium Inferred from mutant phenotype PubMed 21311034. Source: TAIR glutamate biosynthetic processInferred from electronic annotation. Source: InterPro proline catabolic processInferred from genetic interaction Ref.3. Source: TAIR proline catabolic process to glutamateInferred from electronic annotation. Source: UniProtKB-UniPathway response to oxidative stressInferred from expression pattern PubMed 9449849. Source: TAIR response to water deprivationInferred from genetic interaction PubMed 21791601. Source: TAIR |
| Cellular_component | mitochondrion Inferred from direct assay Ref.3. Source: TAIR |
| Molecular_function | proline dehydrogenase activity Inferred from mutant phenotype Ref.3. Source: TAIR |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| CPK4 | Q38869 | 1 | EBI-2299617,EBI-979475 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 16 | 16 | Mitochondrion Potential | ||||||
| Chain | 17 – 499 | 483 | Proline dehydrogenase 1, mitochondrial | PRO_0000025804 | |||||
Experimental info | |||||||||
| Sequence conflict | 30 | 1 | A → V in AAB40615. Ref.1 | ||||||
| Sequence conflict | 46 | 1 | P → T in AAB40615. Ref.1 | ||||||
| Sequence conflict | 51 | 1 | H → Q in AAB40615. Ref.1 | ||||||
| Sequence conflict | 91 | 1 | A → P in CAA65783. Ref.2 | ||||||
| Sequence conflict | 355 | 1 | A → R in BAA11682. Ref.3 | ||||||
| Sequence conflict | 361 | 1 | L → V in CAA65783. Ref.2 | ||||||
| Sequence conflict | 398 | 1 | V → A in AAL67111. Ref.7 | ||||||
| Sequence conflict | 425 | 1 | K → R in AAL16138. Ref.7 | ||||||
| Sequence conflict | 477 | 1 | A → P in AAB40615. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Reciprocal regulation of delta 1-pyrroline-5-carboxylate synthetase and proline dehydrogenase genes controls proline levels during and after osmotic stress in plants." Peng Z., Lu Q., Verma D.P.S. Mol. Gen. Genet. 253:334-341(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. Strain: cv. Columbia. |
| [2] | "Environmental and developmental signals modulate proline homeostasis: evidence for a negative transcriptional regulator." Verbruggen N., Hua X.J., May M., van Montagu M. Proc. Natl. Acad. Sci. U.S.A. 93:8787-8791(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Root. |
| [3] | "A nuclear gene encoding mitochondrial proline dehydrogenase, an enzyme involved in proline metabolism, is upregulated by proline but downregulated by dehydration in Arabidopsis." Kiyosue T., Yoshiba Y., Yamaguchi-Shinozaki K., Shinozaki K. Plant Cell 8:1323-1335(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. |
| [4] | "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S. DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [5] | "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S. DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [6] | The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia. |
| [7] | "Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R.Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [8] | "A gene encoding proline dehydrogenase is not only induced by proline and hypoosmolarity, but is also developmentally regulated in the reproductive organs of Arabidopsis." Nakashima K., Satoh R., Kiyosue T., Yamaguchi-Shinozaki K., Shinozaki K. Plant Physiol. 118:1233-1241(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION. |
| [9] | "Toxicity of free proline revealed in an arabidopsis T-DNA-tagged mutant deficient in proline dehydrogenase." Nanjo T., Fujita M., Seki M., Kato T., Tabata S., Shinozaki K. Plant Cell Physiol. 44:541-548(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE. |
| [10] | "Two tobacco proline dehydrogenases are differentially regulated and play a role in early plant development." Ribarits A., Abdullaev A., Tashpulatov A., Richter A., Heberle-Bors E., Touraev A. Planta 225:1313-1324(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION. |
| [11] | "Non-redundant functions of two proline dehydrogenase isoforms in Arabidopsis." Funck D., Eckard S., Mueller G. BMC Plant Biol. 10:70-70(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U59508 mRNA. Translation: AAB40615.1. X97075 mRNA. Translation: CAA65783.1. D83025 mRNA. Translation: BAA11682.1. AB028614, AP001296 Genomic DNA. Translation: BAB02917.1. CP002686 Genomic DNA. Translation: AEE77659.1. AF428306 mRNA. Translation: AAL16138.1. AY074571 mRNA. Translation: AAL67111.1. |
| IPI | IPI00526335. |
| RefSeq | NP_189701.3. NM_113981.5. |
| UniGene | At.24174. At.71996. At.74287. |
3D structure databases | |
| ProteinModelPortal | P92983. |
| SMR | P92983. Positions 264-488. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P92983. 1 interaction. |
| STRING | 3702.AT3G30775.1-P. |
Proteomic databases | |
| PaxDb | P92983. |
| PRIDE | P92983. |
Protocols and materials databases | |
| DNASU | 822833. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT3G30775.1; AT3G30775.1; AT3G30775. |
| GeneID | 822833. |
| KEGG | ath:AT3G30775. |
Organism-specific databases | |
| TAIR | At3g30775. |
Phylogenomic databases | |
| eggNOG | COG0506. |
| HOGENOM | HOG000243575. |
| InParanoid | P92983. |
| KO | K00318. |
| OMA | GQTGREL. |
| PhylomeDB | P92983. |
| ProtClustDB | PLN02681. |
Enzyme and pathway databases | |
| BioCyc | ARA:AT3G30775-MONOMER. MetaCyc:AT3G30775-MONOMER. |
| UniPathway | UPA00261; UER00373. |
Gene expression databases | |
| Genevestigator | P92983. |
| GermOnline | AT3G30775. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR002872. Proline_DH. IPR015659. Proline_oxidase. [Graphical view] |
| PANTHER | PTHR13914. PTHR13914. 1 hit. |
| Pfam | PF01619. Pro_dh. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PROD1_ARATH | ||||||||
| Accession | Primary (citable) accession number: P92983 Secondary accession number(s): P92945 Q96281 | ||||||||
| 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 |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
