[1]	NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. DOI=10.1016/S0945-053X(99)00016-5; PubMed=10429951 [NCBI, ExPASy, EBI, Israel, Japan] Ruotsalainen H., Sipila L., Kerkela E., Pospiech H., Myllylae R.; "Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse."; Matrix Biol. 18:325-329(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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: Procollagen L-lysine + 2-oxoglutarate + O₂ = procollagen 5-hydroxy-L-lysine + succinate + CO₂.
COFACTOR: Iron (By similarity).
COFACTOR: Ascorbate (By similarity).
SUBUNIT: 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.
SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF080572; AAD53987.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021352; AAH21352.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_036091.1; -.

UniGene

Mm.79983

3D structure databases

ModBase

Q9R0B9.

PTM databases

PhosphoSite

Q9R0B9; -.

Organism-specific databases

MGI

MGI:1347007; Plod2.

Gene expression databases

ArrayExpress

Q9R0B9; -.

GermOnline

ENSMUSG00000032374; Mus musculus.

Ontologies

GO:0030867;	Cellular component: rough endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031418;	Molecular function: L-ascorbic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016702;	Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005123; 2OG-FeII_Oase.
IPR006620; Pro_4_hyd_alph.
IPR001006; Procol_lys_dOase.
Graphical view of domain structure.

Pfam

PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.

ProDom

PD011578; ProcolLys_dioxy; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00702; P4Hc; 1.
SMART graphical view of domain structure.

PROSITE

PS01325; LYS_HYDROXYLASE; 1.

Genome annotation databases

Ensembl

ENSMUSG00000032374; Mus musculus. [Contig view]

GeneID

26432; -.

KEGG

mmu:26432; -.

Phylogenomic databases

HOVERGEN

Q9R0B9; -.

Other

NextBio

304489; -.

SOURCE

Plod2; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase; Phosphoprotein; Signal; Vitamin C.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 25`	`25`	`Potential.`
`CHAIN`	`26 737`	`712`	`Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2.`	`PRO_0000024684`
`DOMAIN`	`563 737`	`175`	`PKHD.`
`ACT_SITE`	`728 728`		`Potential.`
`METAL`	`666 666`		`Iron (By similarity).`
`METAL`	`668 668`		`Iron (By similarity).`
`METAL`	`718 718`		`Iron (By similarity).`
`MOD_RES`	`320 320`		`Phosphothreonine (By similarity).`
`MOD_RES`	`323 323`		`Phosphotyrosine (By similarity).`
`CARBOHYD`	`63 63`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`209 209`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`365 365`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`522 522`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`696 696`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`725 725`		`N-linked (GlcNAc...) (Potential).`
`CONFLICT`	`2 2`		`E -> G (in Ref. 2; AAH21352).`
`CONFLICT`	`611 611`		`I -> T (in Ref. 2; AAH21352).`

Sequence information

Length: 737 AA [This is the length of the unprocessed precursor]

Molecular weight: 84526 Da [This is the MW of the unprocessed precursor]

CRC64: 712A61B3A78F9526 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEDRGARPGR LMPMLALLSW AAGLGVAEET PGRIPADKLL VITVATKEND GFHRFMNSAK 

        70         80         90        100        110        120 
YFNYTVKVLG QGQEWRGGDG MNSIGGGQKV RLLKEAMEHY ASQEDLVILF TECFDVVFAG 

       130        140        150        160        170        180 
GPEEVLKKFQ KTNHKIVFAA DGLLWPDKRL ADKYPVVHIG KRYLNSGGFI GYAPYISRLV 

       190        200        210        220        230        240 
QQWNLQDNDD DQLFYTKVYI DPLKREAFNI TLDHKCKIFQ ALNGATDEVV LKFENGKSRV 

       250        260        270        280        290        300 
KNTFYETLPV AINGNGPTKI LLNYFGNYVP NSWTQENGCA LCDVDTIDLS TVDVPPKVTL 

       310        320        330        340        350        360 
GVFIEQPTPF LPRFLNLLLT LDYPKEALQL FIHNKEVYHE KDIKVFVDKA KHDISSIKIV 

       370        380        390        400        410        420 
GPEENLSQAE ARNMGMDFCR QDEKCDYYFS VDADVVLTNP RTLKILIEQN RKIIAPLVTR 

       430        440        450        460        470        480 
HGKLWSNFWG ALSPDGYYAR SEDYVDIVQG NRVGIWNVPY MANVYLIQGK TLRSEMNERN 

       490        500        510        520        530        540 
YFVRDKLDPD MALCRNARDM GVFMYISNRH EFGRLISTAN YNTSHLNNDF WQIFENPVDW 

       550        560        570        580        590        600 
KEKYINRDYS KIFTENIVEQ PCPDVFWFPI FSERACDELV EEMEHYGKWS GGKHHDSRIS 

       610        620        630        640        650        660 
GGYENVPTDD IHMKQIGLEN VWLHFIREFI APVTLKVFAG YYTKGFALLN FVVKYSPERQ 

       670        680        690        700        710        720 
RSLRPHHDAS TFTINIALNN VGEDFQGGGC KFLRYNCSIE SPRKGWSFMH PGRLTHLHEG 

       730 
LPVKNGTRYI AVSFIDP

Q9R0B9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools