Q9R0B9 (PLOD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 84.
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: Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 EC=1.14.11.4 Alternative name(s): Lysyl hydroxylase 2 Short name=LH2 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 737 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. |
| Catalytic activity | L-lysine-[procollagen] + 2-oxoglutarate + O2 = (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2. |
| Cofactor | Iron By similarity. Ascorbate By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. |
| Tissue specificity | Is highly expressed in the heart, lung, kidney, eye, ovary and placenta. Ref.1 |
| Sequence similarities | Contains 1 Fe2OG dioxygenase domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Signal |
| Ligand | Iron Metal-binding Vitamin C |
| Molecular function | Dioxygenase Oxidoreductase |
| PTM | Glycoprotein Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | rough endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion bindingInferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygenInferred from electronic annotation. Source: UniProtKB-KW procollagen-lysine 5-dioxygenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 25 | 25 | Potential | ||||||
| Chain | 26 – 737 | 712 | Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 | PRO_0000024684 | |||||
Regions | |||||||||
| Domain | 644 – 737 | 94 | Fe2OG dioxygenase | ||||||
Sites | |||||||||
| Active site | 728 | 1 | Potential | ||||||
| Metal binding | 666 | 1 | Iron By similarity | ||||||
| Metal binding | 668 | 1 | Iron By similarity | ||||||
| Metal binding | 718 | 1 | Iron By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 320 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 323 | 1 | Phosphotyrosine By similarity | ||||||
| Glycosylation | 63 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 209 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 365 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 522 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 696 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 725 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 2 | 1 | G → E in AAD53987. Ref.1 | ||||||
| Sequence conflict | 405 | 1 | F → I in AAH21352. Ref.3 | ||||||
| Sequence conflict | 611 | 1 | I → T in AAD53987. Ref.1 | ||||||
| Sequence conflict | 611 | 1 | I → T in AAH21352. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse." Ruotsalainen H., Sipila L., Kerkela E., Pospiech H., Myllylae R. Matrix Biol. 18:325-329(1999) [PubMed: 10429951] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. |
| [2] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF080572 mRNA. Translation: AAD53987.1. AC165156 Genomic DNA. No translation available. BC021352 mRNA. Translation: AAH21352.1. |
| IPI | IPI00918500. |
| RefSeq | NP_001136388.1. NM_001142916.1. NP_036091.2. NM_011961.3. |
| UniGene | Mm.79983. |
3D structure databases | |
| ProteinModelPortal | Q9R0B9. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9R0B9. |
PTM databases | |
| PhosphoSite | Q9R0B9. |
Proteomic databases | |
| PRIDE | Q9R0B9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000070522; ENSMUSP00000068611; ENSMUSG00000032374. |
| GeneID | 26432. |
| KEGG | mmu:26432. |
| UCSC | uc009rau.2. mouse. |
Organism-specific databases | |
| CTD | 5352. |
| MGI | MGI:1347007. Plod2. |
Phylogenomic databases | |
| eggNOG | roNOG07750. |
| GeneTree | ENSGT00550000074427. |
| HOVERGEN | HBG053618. |
| InParanoid | Q9R0B9. |
| OrthoDB | EOG4KKZ2D. |
Gene expression databases | |
| ArrayExpress | Q9R0B9. |
| Bgee | Q9R0B9. |
| Genevestigator | Q9R0B9. |
| GermOnline | ENSMUSG00000032374. Mus musculus. |
Family and domain databases | |
| InterPro | IPR005123. Oxoglutarate/Fe-dep_oxygenase. IPR006620. Pro_4_hyd_alph. IPR001006. Procol_lys_dOase. [Graphical view] |
| KO | K13645. |
| Pfam | PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view] |
| SMART | SM00702. P4Hc. 1 hit. [Graphical view] |
| PROSITE | PS51471. FE2OG_OXY. 1 hit. PS01325. LYS_HYDROXYLASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 304489. |
| SOURCE | Search... |
Entry information
| Entry name | PLOD2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9R0B9 Secondary accession number(s): E9QM54, Q8VDT4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with