A0A452R393 · A0A452R393_URSAM

Function

function

Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils. 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

Cofactor

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

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

GO annotations

AspectTerm
Cellular Componentrough endoplasmic reticulum membrane
Molecular Functioniron ion binding
Molecular FunctionL-ascorbic acid binding
Molecular Functionprocollagen-lysine 5-dioxygenase activity
Biological Processepidermis development
Biological Processpeptidyl-lysine hydroxylation
Biological Processresponse to hypoxia

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
  • EC number
  • Alternative names
    • Lysyl hydroxylase 1

Gene names

    • Name
      PLOD1

Organism names

Accessions

  • Primary accession
    A0A452R393

Proteomes

Subcellular Location

Rough endoplasmic reticulum membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-18
ChainPRO_501942861419-727Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1

Interaction

Subunit

Homodimer. Identified in a complex with P3H3 and P3H4.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain636-727Fe2OG dioxygenase

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    727
  • Mass (Da)
    83,534
  • Last updated
    2019-05-08 v1
  • Checksum
    80849D4182AD7C27
MRPLLLLAPLGWLLLAEAKGDAKPEDNLLVLTVATRETEGFRRFKRSGQFFNYKIQALGLGEDWSGEKGSSAGGGLKVRLLKKALEKHADKENLVILFIDSYDVLFASGPRELLKKFRQAKSQVVFSAEELIYPDRRLEAKYPAVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQLFYTKIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLIHGNGPTKLQLNYLGNYIPRFWTFETGCAVCDEGLRSLRGIGDEALPTVLVGVFIEQPTPFLSLFFQRLLRLRYPRKQMRLFIHNHEQHHKAQVEQFLAEHGGEYQSVKLVGPEVRVASADARNMGADLCRQDRSCTYYFSVDADVALTEPKTLRLLIEQNKNVIAPLMTRHGRLWSNFWGALSADGYYARSEDYVDIVQGRRVGVWNVPYISNVYLIKGSALRAELQQTDLFHHSKLDPDMAFCANIRQQDVFMFLTNRHTFGHLLSLDNYQTSHLHNDLWEVFSNPEDWKEKYIHENYTKALAGKLVEMPCPDVYWFPIFTEVACDELVEEMEHYGRWSLGDNKDSRIQGGYENVPTIDIHMNQISFEREWHKFLVEYIAPMTEKLYPGYYTRAQFDLAFVVRYKPDEQPSLMPHHDASTFTINIALNRVGVDYEGGGCRFLRYNCSIRAPRKGWTLMHPGRLTHYHEGLPTTRGTRYIAVSFVDP

Keywords

Genome annotation databases

Similar Proteins

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