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Q4KLM6 (P3H2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prolyl 3-hydroxylase 2

EC=1.14.11.7
Alternative name(s):
Leprecan-like protein 1
Gene names
Name:Leprel1
Synonyms:P3h2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length703 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Shows prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types IV and V By similarity. Catalyzes the 3-hydroxyproline modification in -Xaa-Pro-Gly-sequences in collagens, especially alpha-1 type II and alpha-2 type V. Ref.2

Catalytic activity

L-proline-[procollagen] + 2-oxoglutarate + O2 = trans-3-hydroxy-L-proline-[procollagen] + succinate + CO2.

Cofactor

Iron By similarity.

Ascorbate By similarity.

Subcellular location

Endoplasmic reticulum. Golgi apparatus By similarity.

Sequence similarities

Belongs to the leprecan family.

Contains 1 Fe2OG dioxygenase domain.

Contains 4 TPR repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 703682Prolyl 3-hydroxylase 2
PRO_0000240358

Regions

Repeat42 – 7534TPR 1
Repeat144 – 17734TPR 2
Repeat205 – 23834TPR 3
Repeat301 – 33434TPR 4
Domain552 – 666115Fe2OG dioxygenase
Motif700 – 7034Prevents secretion from ER Potential

Sites

Active site6571 By similarity
Metal binding5751Iron
Metal binding5771Iron
Metal binding6471Iron

Amino acid modifications

Glycosylation4441N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) Potential
Glycosylation5441N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4KLM6 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: EFE57CEF5F209B63

FASTA70379,833
        10         20         30         40         50         60 
MRESTWVSLL LLLLLPAPQR GGPQDGRGSP EPEPERGPLQ PFDLLYASGV AAYYSGDYEG 

        70         80         90        100        110        120 
AVRDLEAALR SHRRLRDIRT RCARHCAARR PLAPPGAGPG AELPFFRAVL ERARCSRSCQ 

       130        140        150        160        170        180 
SQRLGGPASR HRVSEDVRSD FQRRVPYNYL QRAYIKLNQL DKAMEAAHTF FMANPEHMEM 

       190        200        210        220        230        240 
QQNIEDYKAT ARVEAPLVDR EAKPHLESYN AGVKHYEADD FEAAIKYFEQ ALREYFNEDM 

       250        260        270        280        290        300 
VCRALCEGPQ RFEEYEYLGS KGSLYEAIAD HYMQVLVCQH ECVRELATRP GRLSPIENFL 

       310        320        330        340        350        360 
PLHYDYLQFA YYRVGEYVKA LECAKAYLMF HPDDQDVLDN VDFYESLLDD STDPASIEAR 

       370        380        390        400        410        420 
EDLTAFVKRH KLEAELIKSA AEGLGFSYSE PNYWISYGGR QDENRVPSGV NMDGAEVHGL 

       430        440        450        460        470        480 
SMGKKSPPKI GRDLREGGPL LYENITFVYN SEQLNGTQRV LLDNVLSEEQ CRELHSVASG 

       490        500        510        520        530        540 
IMLVGDGYRG KTSPHTPNEK FEGATVLKAL KFGYEGRVPL KSARLFYDIS EKARKIVESY 

       550        560        570        580        590        600 
FMLNSTLYFS YTHMVCRTAL SGQQDRRNDL SHPIHADNCL LDPEANECWK EPPAYTFRDY 

       610        620        630        640        650        660 
SALLYMNDDF EGGEFIFTEM DAKTVTASIK PKCGRMISFS SGGENPHGVK AVTRGQRCAV 

       670        680        690        700 
ALWFTLDPLY RELERIQADE VIAILDQEQH GKHGLNINPK DEL 

« Hide

References

« Hide 'large scale' references
[1]"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].
Tissue: Placenta.
[2]"A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens."
Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.
J. Biol. Chem. 286:30662-30669(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PROLYL-3-HYDROXYLASE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC099107 mRNA. Translation: AAH99107.1.
RefSeqNP_001020798.1. NM_001025627.1.
UniGeneRn.213595.

3D structure databases

ProteinModelPortalQ4KLM6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000002639.

PTM databases

PhosphoSiteQ4KLM6.

Proteomic databases

PaxDbQ4KLM6.
PRIDEQ4KLM6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID288016.
KEGGrno:288016.
UCSCRGD:1304568. rat.

Organism-specific databases

CTD55214.
RGD1304568. Leprel1.

Phylogenomic databases

eggNOGNOG269251.
HOGENOMHOG000231087.
HOVERGENHBG053224.
InParanoidQ4KLM6.
PhylomeDBQ4KLM6.

Gene expression databases

GenevestigatorQ4KLM6.

Family and domain databases

Gene3D1.25.40.10. 3 hits.
InterProIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR011990. TPR-like_helical.
IPR013105. TPR_2.
[Graphical view]
PfamPF13640. 2OG-FeII_Oxy_3. 1 hit.
PF07719. TPR_2. 2 hits.
[Graphical view]
SMARTSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
PS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio627416.
PROQ4KLM6.

Entry information

Entry nameP3H2_RAT
AccessionPrimary (citable) accession number: Q4KLM6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: August 2, 2005
Last modified: April 16, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families