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Protein

Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3

Gene

Plod3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

L-lysine-[procollagen] + 2-oxoglutarate + O2 = (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi670 – 6701IronPROSITE-ProRule annotation
Metal bindingi672 – 6721IronPROSITE-ProRule annotation
Metal bindingi722 – 7221IronPROSITE-ProRule annotation
Active sitei732 – 7321Sequence analysis

GO - Molecular functioni

  • iron ion binding Source: InterPro
  • L-ascorbic acid binding Source: UniProtKB-KW
  • procollagen glucosyltransferase activity Source: MGI
  • procollagen-lysine 5-dioxygenase activity Source: MGI

GO - Biological processi

  • basement membrane assembly Source: MGI
  • cellular response to hormone stimulus Source: Ensembl
  • collagen fibril organization Source: MGI
  • endothelial cell morphogenesis Source: MGI
  • epidermis morphogenesis Source: MGI
  • in utero embryonic development Source: MGI
  • lung morphogenesis Source: MGI
  • neural tube development Source: MGI
  • protein localization Source: MGI
  • vasodilation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (EC:1.14.11.4)
Alternative name(s):
Lysyl hydroxylase 3
Short name:
LH3
Gene namesi
Name:Plod3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1347008. Plod3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Chaini28 – 741714Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3PRO_0000024687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi66 – 661N-linked (GlcNAc...)1 Publication
Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence analysis
Glycosylationi551 – 5511N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ9R0E1.
MaxQBiQ9R0E1.
PaxDbiQ9R0E1.
PRIDEiQ9R0E1.

PTM databases

iPTMnetiQ9R0E1.
PhosphoSiteiQ9R0E1.

Expressioni

Tissue specificityi

Highly expressed in the heart, lung, liver and testis.1 Publication

Gene expression databases

BgeeiQ9R0E1.
ExpressionAtlasiQ9R0E1. baseline and differential.
GenevisibleiQ9R0E1. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi204985. 1 interaction.
IntActiQ9R0E1. 2 interactions.
MINTiMINT-4107969.
STRINGi10090.ENSMUSP00000004968.

Structurei

3D structure databases

ProteinModelPortaliQ9R0E1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini650 – 74192Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1971. Eukaryota.
ENOG410Y4QU. LUCA.
GeneTreeiENSGT00550000074427.
HOGENOMiHOG000231099.
HOVERGENiHBG053618.
InParanoidiQ9R0E1.
KOiK13646.
OMAiYPEVEGK.
OrthoDBiEOG79PJNP.
PhylomeDBiQ9R0E1.
TreeFamiTF313826.

Family and domain databases

InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR001006. Procol_lys_dOase.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
PS01325. LYS_HYDROXYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:iD1B79B386339D9F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81P → H in BAB28704 (PubMed:16141072).Curated

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.
UniGeneiMm.251003.

Genome annotation databases

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

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.
UniGeneiMm.251003.

3D structure databases

ProteinModelPortaliQ9R0E1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204985. 1 interaction.
IntActiQ9R0E1. 2 interactions.
MINTiMINT-4107969.
STRINGi10090.ENSMUSP00000004968.

PTM databases

iPTMnetiQ9R0E1.
PhosphoSiteiQ9R0E1.

Proteomic databases

EPDiQ9R0E1.
MaxQBiQ9R0E1.
PaxDbiQ9R0E1.
PRIDEiQ9R0E1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8985.
MGIiMGI:1347008. Plod3.

Phylogenomic databases

eggNOGiKOG1971. Eukaryota.
ENOG410Y4QU. LUCA.
GeneTreeiENSGT00550000074427.
HOGENOMiHOG000231099.
HOVERGENiHBG053618.
InParanoidiQ9R0E1.
KOiK13646.
OMAiYPEVEGK.
OrthoDBiEOG79PJNP.
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

ChiTaRSiPlod3. mouse.
PROiQ9R0E1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R0E1.
ExpressionAtlasiQ9R0E1. baseline and differential.
GenevisibleiQ9R0E1. MM.

Family and domain databases

InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR001006. Procol_lys_dOase.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
PS01325. LYS_HYDROXYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse."
    Ruotsalainen H., Sipila L., Kerkela E., Pospiech H., Myllylae R.
    Matrix Biol. 18:325-329(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase."
    Ruotsalainen H., Vanhatupa S., Tampio M., Sipila L., Valtavaara M., Myllylae R.
    Matrix Biol. 20:137-146(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryo, Lung and Thymus.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-66.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiPLOD3_MOUSE
AccessioniPrimary (citable) accession number: Q9R0E1
Secondary accession number(s): Q542E0, Q9CYY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.