Prolyl 3-hydroxylase 2 precursor - Rattus norvegicus (Rat)

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Q4KLM6 (P3H2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Prolyl 3-hydroxylase 2
EC=1.14.11.7

Alternative name(s):
Leprecan-like protein 1

Gene names

Name:	Leprel1
Synonyms:	P3h2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	703 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Golgi apparatus
Domain	Repeat Signal TPR repeat
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	collagen metabolic process Inferred from direct assay Ref.2. Source: UniProtKB negative regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-proline hydroxylation Inferred from direct assay Ref.2. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB basement membrane Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB
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-proline 3-dioxygenase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Potential

Chain

22 – 703

682

Prolyl 3-hydroxylase 2

PRO_0000240358

Regions

Repeat

42 – 75

TPR 1

Repeat

144 – 177

TPR 2

Repeat

205 – 238

TPR 3

Repeat

301 – 334

TPR 4

Domain

552 – 666

115

Fe2OG dioxygenase

Motif

700 – 703

Prevents secretion from ER Potential

Sites

Active site

657

By similarity

Metal binding

575

Iron

Metal binding

577

Iron

Metal binding

647

Iron

Amino acid modifications

Glycosylation

444

N-linked (GlcNAc...) Potential

Glycosylation

455

N-linked (GlcNAc...) Potential

Glycosylation

544

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q4KLM6 [UniParc].

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

703

79,833

        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' referencesShow '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.
IPI	IPI00561579.
RefSeq	NP_001020798.1. NM_001025627.1.
UniGene	Rn.213595.
3D structure databases
ProteinModelPortal	Q4KLM6.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000002639.
PTM databases
PhosphoSite	Q4KLM6.
Proteomic databases
PaxDb	Q4KLM6.
PRIDE	Q4KLM6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	288016.
KEGG	rno:288016.
UCSC	RGD:1304568. rat.
Organism-specific databases
CTD	55214.
RGD	1304568. Leprel1.
Phylogenomic databases
eggNOG	NOG269251.
HOGENOM	HOG000231087.
HOVERGEN	HBG053224.
InParanoid	Q4KLM6.
OrthoDB	EOG4WSW97.
Gene expression databases
ArrayExpress	Q4KLM6.
Genevestigator	Q4KLM6.
GermOnline	ENSRNOG00000001925. Rattus norvegicus.
Family and domain databases
Gene3D	1.25.40.10. 3 hits.
InterPro	IPR005123. Oxoglu/Fe-dep_dioxygenase. IPR006620. Pro_4_hyd_alph. IPR011990. TPR-like_helical. IPR013105. TPR_2. [Graphical view]
Pfam	PF13640. 2OG-FeII_Oxy_3. 1 hit. PF07719. TPR_2. 2 hits. [Graphical view]
SMART	SM00702. P4Hc. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. PS51471. FE2OG_OXY. 1 hit. PS50005. TPR. False negative. PS50293. TPR_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	627416.

Entry information

Entry name

P3H2_RAT

Accession

Primary (citable) accession number: Q4KLM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	August 2, 2005
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents