A0A452S521 · A0A452S521_URSAM

Function

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

L-ascorbate (UniProtKB | Rhea| CHEBI:38290 )

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentendoplasmic reticulum membrane
Molecular Functioniron ion binding
Molecular FunctionL-ascorbic acid binding
Molecular Functionprocollagen-lysine 5-dioxygenase activity
Biological Processpeptidyl-lysine hydroxylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    procollagen-lysine 5-dioxygenase
  • EC number

Gene names

    • Name
      PLOD2

Organism names

Accessions

  • Primary accession
    A0A452S521

Proteomes

Subcellular Location

Endoplasmic reticulum membrane
; Peripheral membrane protein
Rough endoplasmic reticulum

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-25
ChainPRO_501926584726-667procollagen-lysine 5-dioxygenase

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain574-667Fe2OG dioxygenase

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    667
  • Mass (Da)
    77,391
  • Last updated
    2019-05-08 v1
  • Checksum
    985028A6FE0E6706
KLMSGTLGAFNLLVNHLMLVPSVFADKLLVITVATKESDGFHRFMQSAKYFNYTVKVLGQGEEWRGGDGINSIGGGQKVRLMKEVMEHYANQEDLVILFTECFNVIFAGGPEEVLKKFQKSNHKVVFAADGILWPDKRLADKYPIVHIGKRYLNSGGFIGYAPNINQIVQQWNLQDNDDDQLFYTKIYIDPLKRVWNSSHFQYNLLRTSTLIIICFYVCHKTKVRPNVTIGVFIEQPTPFLPRFLDILLTLDYPKEALKLFIHNKEVYHEKDIKVFFDKAKREISTIKIVGPEENLSQAEARNMGMDFCRQDENCDYYFSMDADVVLTNPRTLKILIEQNRKIIAPLVTRHGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGIWNVPYMANVYLIKGKTLRSEMNERNYFVRDKLDPDMALCRNAREMGVFMYISNRHEFGRLLSTANYNTSHYNNDLWQIFENPVDWKEKYINRDYSKIFTENIVEQPCPDVFWFPIFSEKACDELVEEMEHYGQWSGGKHHDSRISGGYENVPTDDIHMKQIDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQRSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEGLPVKNGTRYIAVSFIDP

Computationally mapped potential isoform sequences

There are 9 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A452S4S4A0A452S4S4_URSAMPLOD2728
A0A452S4T6A0A452S4T6_URSAMPLOD2688
A0A452S4W1A0A452S4W1_URSAMPLOD2667
A0A452S4R0A0A452S4R0_URSAMPLOD2683
A0A452S526A0A452S526_URSAMPLOD2691
A0A452S501A0A452S501_URSAMPLOD2712
A0A452S506A0A452S506_URSAMPLOD2646
A0A452S4M2A0A452S4M2_URSAMPLOD2725
A0A452S4Q0A0A452S4Q0_URSAMPLOD2707

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

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