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Entry version 146 (18 Sep 2019)
Sequence version 1 (01 May 2000)
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Protein

Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3

Gene

Plod3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Multifunctional enzyme that catalyzes a series of post-translational modifications on Lys residues in procollagen (PubMed:16447251). Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (PubMed:16447251). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (By similarity). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:16447251, PubMed:16467571, PubMed:21220425). Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:25419660). Catalyzes hydroxylation and glycosylation of Lys residues in the ADIPOQ collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:23209641). Essential for normal biosynthesis and secretion of type IV collagens (PubMed:15377789, PubMed:16467571, PubMed:17873278). Essential for normal formation of basement membranes (PubMed:15377789, PubMed:16467571).By similarity7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi115ManganeseBy similarity1
Metal bindingi118ManganeseBy similarity1
Metal bindingi256ManganeseBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei6022-oxoglutarateBy similarity1
Binding sitei6592-oxoglutarateBy similarity1
Metal bindingi670IronPROSITE-ProRule annotation1
Metal bindingi672IronPROSITE-ProRule annotation1
Binding sitei6792-oxoglutarateBy similarity1
Metal bindingi722IronPROSITE-ProRule annotation1
Binding sitei7322-oxoglutarateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDioxygenase, Glycosyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
LigandIron, Manganese, Metal-binding, Vitamin C

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.14.11.4 3474
2.4.1.66 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1650814 Collagen biosynthesis and modifying enzymes

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
Including the following 2 domains:
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (EC:1.14.11.42 Publications)
Alternative name(s):
Lysyl hydroxylase 3
Short name:
LH3
Procollagen glycosyltransferase (EC:2.4.1.50By similarity, EC:2.4.1.663 Publications)
Alternative name(s):
Galactosylhydroxylysine-glucosyltransferase
Procollagen galactosyltransferase
Procollagen glucosyltransferase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Plod3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1347008 Plod3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Full embryonic lethality. Mutant embryos are much smaller than wild-type by 9.5 dpc, and the majority are dead by 10.5 dpc. At 9.5 dpc, mutant embryos display fragmentation of basement membranes (PubMed:15377789, PubMed:16467571). The majority of the mutant embryos display dilated blood vessels, particularly in the region of the sinus venosus (PubMed:16467571). Mutant embryos display no decrease in global lysyl hydroxylase activity, due to the expression of other lysyl hydroxylases (PubMed:15377789). Mutant embryos display a nearly complete loss of procollagen glucosyltransferase activity (PubMed:15377789, PubMed:16467571).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi672D → A: Loss of lysyl hydroxylase activity. No effect on glycosyltransferase activity. Mutant mice are born at the expected Mendelian rate and have no visible phenotype, excepting decreased hydroxylysine modifications in type IV collagens in the skin. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 27Sequence analysisAdd BLAST27
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002468728 – 741Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3Add BLAST714

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi66N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi282 ↔ 285By similarity
Glycosylationi286N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi382 ↔ 388By similarity
Glycosylationi551N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi566 ↔ 701By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9R0E1

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9R0E1

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9R0E1

PeptideAtlas

More...
PeptideAtlasi
Q9R0E1

PRoteomics IDEntifications database

More...
PRIDEi
Q9R0E1

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2609

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9R0E1

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9R0E1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in blood serum, heart, brain, liver, kidney, lung, spleen, muscle and testis (at protein level) (PubMed:16447251). Highly expressed in the heart, lung, liver and testis (PubMed:10429951). Detected in the walls of blood vessels in placenta and embryos. Detected in chondrocytes in embryos at 14.5 dpc and in adults, in adult kidney mesangium and vascular poles of kidney glomeruli (PubMed:15377789). Detected around nerves and in the adrenal gland (PubMed:15377789).3 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Detected in embryos (at protein level) (PubMed:16467571). Ubiquitous and strongly expressed in embryos at 8.5 to 9.5 dpc. Expression becomes more restricted during embryonic development. Highly expressed in head, eye lens and developing bones at 12.5 dpc. Expression in the eye is decreased by 14.5 dpc. Detected in capillaries and in the photoreceptor layer in the adult eye (PubMed:15377789).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000004846 Expressed in 249 organ(s), highest expression level in adipose tissue

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9R0E1 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9R0E1 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
204985, 2 interactors

Protein interaction database and analysis system

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IntActi
Q9R0E1, 2 interactors

Molecular INTeraction database

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MINTi
Q9R0E1

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000004968

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9R0E1

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini650 – 741Fe2OG dioxygenasePROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni28 – 293Required for glycosyltransferase activityBy similarityAdd BLAST266
Regioni47 – 49UDP-sugar bindingBy similarity3
Regioni115 – 117UDP-sugar bindingBy similarity3
Regioni259 – 262UDP-sugar bindingBy similarity4
Regioni298 – 523Accessory regionBy similarityAdd BLAST226
Regioni675 – 718Important for dimerizationBy similarityAdd BLAST44

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal domain mediates glycosyltransferase activity.By similarity
The C-terminal domain that mediates lysyl hydroxylase activity is also important for homodimerization.By similarity

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1971 Eukaryota
ENOG410Y4QU LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000182728

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231099

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9R0E1

KEGG Orthology (KO)

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KOi
K13646

Identification of Orthologs from Complete Genome Data

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OMAi
CIVSSPR

Database of Orthologous Groups

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OrthoDBi
194164at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9R0E1

TreeFam database of animal gene trees

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TreeFami
TF313826

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029044 Nucleotide-diphossugar_trans
IPR005123 Oxoglu/Fe-dep_dioxygenase
IPR006620 Pro_4_hyd_alph
IPR001006 Procol_lys_dOase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03171 2OG-FeII_Oxy, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00702 P4Hc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53448 SSF53448, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51471 FE2OG_OXY, 1 hit
PS01325 LYS_HYDROXYLASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9R0E1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAAGPEPRL LLLLLLLLPP LPPVTSASDR PRGANAVNPD KLLVITVATA
60 70 80 90 100
ETEGYRRFLQ SAEFFNYTVR TLGLGQEWRG GDVARTVGGG QKVRWLKKEM
110 120 130 140 150
EKYADQKDMI IMFVDSYDVI LASSPTELLK KFVQSGSHLL FSAESFCWPE
160 170 180 190 200
WGLAEQYPEV GMGKRFLNSG GFIGFAPTIH QIVRQWNYKD DDDDQLFYTQ
210 220 230 240 250
LYLDPGLREK LKLSLDHKSR IFQNLNGALD EVILKFDQNR VRIRNVAYDT
260 270 280 290 300
LPVVVHGNGP TKLQLNYLGN YVPNGWTPQG GCGFCNQTLR TLPGGQPPPR
310 320 330 340 350
VLLAVFVEQP TPFLPRFLQR LLLLDYPPDR ISLFLHNSEV YHEPHIADAW
360 370 380 390 400
PQLQDHFSAV KLVGPEEALS AGEARDMAMD SCRQNPECEF YFSLDADAVL
410 420 430 440 450
TNPETLRVLI EQNRKVIAPM LSRHGKLWSN FWGALSPNEY YARSEDYVEL
460 470 480 490 500
VQRKRVGVWN VPYISQAYVI RGETLRTELP QKEVFSSSDT DPDMAFCKSV
510 520 530 540 550
RDKGIFLHLS NQHEFGRLLA TSRYDTDHLH PDLWQIFDNP VDWREQYIHE
560 570 580 590 600
NYSRALDGEG LVEQPCPDVY WFPLLTEQMC DELVEEMEHY GQWSGGRHED
610 620 630 640 650
SRLAGGYENV PTVDIHMKQV GYEDQWLQLL RTYVGPMTEY LFPGYHTKTR
660 670 680 690 700
AVMNFVVRYR PDEQPSLRPH HDSSTFTLNV ALNHKGVDYE GGGCRFLRYD
710 720 730 740
CRISSPRKGW ALLHPGRLTH YHEGLPTTRG TRYIMVSFVD P
Length:741
Mass (Da):84,922
Last modified:May 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD1B79B386339D9F4
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F6W3Q8F6W3Q8_MOUSE
Multifunctional procollagen lysine ...
Plod3
200Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti8P → H in BAB28704 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF046783 mRNA Translation: AAD54618.1
AY014830 Genomic DNA Translation: AAK00576.1
AK013195 mRNA Translation: BAB28704.1
AK033360 mRNA Translation: BAC28246.1
AK088948 mRNA Translation: BAC40669.1
BC043047 mRNA Translation: AAH43047.1
BC054734 mRNA Translation: AAH54734.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS19759.1

NCBI Reference Sequences

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RefSeqi
NP_036092.1, NM_011962.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000004968; ENSMUSP00000004968; ENSMUSG00000004846

Database of genes from NCBI RefSeq genomes

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GeneIDi
26433

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:26433

UCSC genome browser

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UCSCi
uc009abj.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF046783 mRNA Translation: AAD54618.1
AY014830 Genomic DNA Translation: AAK00576.1
AK013195 mRNA Translation: BAB28704.1
AK033360 mRNA Translation: BAC28246.1
AK088948 mRNA Translation: BAC40669.1
BC043047 mRNA Translation: AAH43047.1
BC054734 mRNA Translation: AAH54734.1
CCDSiCCDS19759.1
RefSeqiNP_036092.1, NM_011962.3

3D structure databases

SMRiQ9R0E1
ModBaseiSearch...

Protein-protein interaction databases

BioGridi204985, 2 interactors
IntActiQ9R0E1, 2 interactors
MINTiQ9R0E1
STRINGi10090.ENSMUSP00000004968

PTM databases

GlyConnecti2609
iPTMnetiQ9R0E1
PhosphoSitePlusiQ9R0E1

Proteomic databases

EPDiQ9R0E1
MaxQBiQ9R0E1
PaxDbiQ9R0E1
PeptideAtlasiQ9R0E1
PRIDEiQ9R0E1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004968; ENSMUSP00000004968; ENSMUSG00000004846
GeneIDi26433
KEGGimmu:26433
UCSCiuc009abj.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
8985
MGIiMGI:1347008 Plod3

Phylogenomic databases

eggNOGiKOG1971 Eukaryota
ENOG410Y4QU LUCA
GeneTreeiENSGT00950000182728
HOGENOMiHOG000231099
InParanoidiQ9R0E1
KOiK13646
OMAiCIVSSPR
OrthoDBi194164at2759
PhylomeDBiQ9R0E1
TreeFamiTF313826

Enzyme and pathway databases

BRENDAi1.14.11.4 3474
2.4.1.66 3474
ReactomeiR-MMU-1650814 Collagen biosynthesis and modifying enzymes

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Plod3 mouse

Protein Ontology

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PROi
PR:Q9R0E1

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000004846 Expressed in 249 organ(s), highest expression level in adipose tissue
ExpressionAtlasiQ9R0E1 baseline and differential
GenevisibleiQ9R0E1 MM

Family and domain databases

InterProiView protein in InterPro
IPR029044 Nucleotide-diphossugar_trans
IPR005123 Oxoglu/Fe-dep_dioxygenase
IPR006620 Pro_4_hyd_alph
IPR001006 Procol_lys_dOase
PfamiView protein in Pfam
PF03171 2OG-FeII_Oxy, 1 hit
SMARTiView protein in SMART
SM00702 P4Hc, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit
PROSITEiView protein in PROSITE
PS51471 FE2OG_OXY, 1 hit
PS01325 LYS_HYDROXYLASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPLOD3_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9R0E1
Secondary accession number(s): Q542E0, Q9CYY9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: May 1, 2000
Last modified: September 18, 2019
This is version 146 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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