Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 precursor

Preferred order of sections

Names and origin

Protein names

Recommended name:
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
EC=1.14.11.4

Alternative name(s):
Lysyl hydroxylase 1
Short name=LH1

Gene names

Name:	PLOD1
Synonyms:	PLOD

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	726 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.
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
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 binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW procollagen-lysine 5-dioxygenase activity Inferred 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 – 18

18

By similarity

Chain

19 – 726

708

Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1

PRO_0000024677

Regions

Domain

635 – 726

92

Fe2OG dioxygenase

Sites

Active site

717

1

Potential

Metal binding

655

1

Iron By similarity

Metal binding

657

1

Iron By similarity

Metal binding

707

1

Iron By similarity

Amino acid modifications

Glycosylation

196

1

N-linked (GlcNAc...) Potential

Glycosylation

537

1

N-linked (GlcNAc...) Potential

Glycosylation

685

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

140

1

K → N in AAC25107. Ref.1

Sequence conflict

164

1

S → I in AAC25107. Ref.1

Sequence conflict

209 – 210

2

LD → FH in AAC25107. Ref.1

Sequence conflict

309

1

R → L in AAC25107. Ref.1

Sequence conflict

317

1

L → F in AAC25107. Ref.1

Sequence conflict

404

1

A → T in AAC25107. Ref.1

Sequence conflict

607

1

F → Y in AAC25107. Ref.1

Sequence conflict

666

1

A → G in AAC25107. Ref.1

Sequence conflict

710

1

L → V in AAC25107. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O77588 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: D215F7E093CCADE9
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FASTA

726

83,487

        10         20         30         40         50         60 
MRLLLLLAPL GWLLLAETKG DAKPEDNLLV LTVATKETEG FRRFKRSAQF FNYKIQALGL 

        70         80         90        100        110        120 
GEDWPGEAML AGGGLKVRLL KKALEKHADK ENLVILFTDS YDVVFASGPR ELLKKFRQAR 

       130        140        150        160        170        180 
SQVVFSAEEL IYPDRRLEAK YPVVSDGKRF LGSGGFIGYA PNLSKLVAEW EGQDSDSDQL 

       190        200        210        220        230        240 
FYTKIFLDPE KREQINITLD HRCRIFQNLD GALDEVVLKF EMGQVRARNL AYDTLPVLIH 

       250        260        270        280        290        300 
GNGPTKLQLN YLGNYIPRFW TFETGCAVCD EGLRSLKGIG DEALPAVLVG VFIEQPTPFL 

       310        320        330        340        350        360 
SLFFQRLLRL HYPQKRLRLF IHNHEQHHKA QVEQFLAEHG DEYQSVKLVG PEVRVANADA 

       370        380        390        400        410        420 
RNMGADLCRQ DRGCTYYFSV DADVALTEPK TLRLLIEQNK NVIAPLMTRH GRLWSNFWGA 

       430        440        450        460        470        480 
LSADGYYARS EDYVDIVQGR RVGVWNVPYI SNIYLIKGSA LRAELQETDL FHHSKLDPDM 

       490        500        510        520        530        540 
AFCANIRQQD VFMFLTNRHS FGHLLSLDSY QTTHLHNDLW EVFSNPEDWK EKYIHENYTK 

       550        560        570        580        590        600 
ALAGKMVEMP CPDVYWFPIF TETACDELVE EMEHYGQWSL GDNKDNRIQG GYENVPTIDI 

       610        620        630        640        650        660 
HMNQINFERE WHKFLVEYIA PMTEKLYPGY YTRAQFDLAF VVRYKPDEQP SLVPHHDAST 

       670        680        690        700        710        720 
FTINIALNRV GVDYEGGGCR FLRYNCSIRA PRKGWTLMHP GRLTHYHEGL PTTKGTRYIA 


VSFVDP

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Knight M.A., Drinkwater R.D. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF054274 mRNA. Translation: AAC25107.1. BT025353 mRNA. Translation: ABF57309.1.
IPI	IPI00718774.
RefSeq	NP_776573.1. NM_174148.1.
UniGene	Bt.4998.
3D structure databases
ProteinModelPortal	O77588.
ModBase	Search...
Protein-protein interaction databases
STRING	O77588.
Proteomic databases
PRIDE	O77588.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	281409.
KEGG	bta:281409.
Organism-specific databases
CTD	5351.
Phylogenomic databases
eggNOG	maNOG06338.
GeneTree	ENSGT00550000074427.
HOVERGEN	HBG053618.
InParanoid	O77588.
OMA	KFEMGHV.
OrthoDB	EOG4K0QMV.
Family and domain databases
InterPro	IPR005123. Oxoglutarate/Fe-dep_oxygenase. IPR006620. Pro_4_hyd_alph. IPR001006. Procol_lys_dOase. [Graphical view]
KO	K00473.
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...

Entry information

Entry name

PLOD1_BOVIN

Accession

Primary (citable) accession number: O77588
Secondary accession number(s): Q1JPK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	July 25, 2006
Last modified:	November 16, 2011
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents