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Q6JHU7 (P3H2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length694 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types II, IV and V By similarity.

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 – 2323 Potential
Chain24 – 694671Prolyl 3-hydroxylase 2
PRO_0000240359

Regions

Repeat35 – 6834TPR 1
Repeat136 – 16934TPR 2
Repeat196 – 22934TPR 3
Repeat292 – 32534TPR 4
Domain543 – 657115Fe2OG dioxygenase
Coiled coil386 – 41833 Potential
Motif691 – 6944Prevents secretion from ER Potential

Sites

Active site6481 By similarity
Metal binding5661Iron
Metal binding5681Iron
Metal binding6381Iron

Amino acid modifications

Glycosylation4461N-linked (GlcNAc...) Potential
Glycosylation5351N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q6JHU7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6263153C4577AFBD

FASTA69478,430
        10         20         30         40         50         60 
MAPGSRSWGA VLLLAAMLPA ACGSCGADGG PLEPFDALYA SGVEAYYGGD FAGAARCLEQ 

        70         80         90        100        110        120 
ALRSRRELRA ERLRCRRRCR GQVRLAALGA GPAGELPFFG ALLRRAGCLR SCEEPRLGAA 

       130        140        150        160        170        180 
SRHRAAEEVR SDFQRRVPYS YLQRAYIQLN KLEEAANAAH TFFMANPEHM EIQQDIENYK 

       190        200        210        220        230        240 
TTAGKVSLID LEAKPHMEDY SAGVRHYDKE EYGLAITFLE RALEGYYAED EDCQIMCEGP 

       250        260        270        280        290        300 
QRFEEHEYLE YKAGLYEAIA DHYMQVLACK HDCIRELATR SGRISPIENF LPLHYDYLQF 

       310        320        330        340        350        360 
AYYRVGDYVK ALECARSYLL FHPDDEDVLE NAAYYEGLLE GTVDPATIKP RKEAKALLRR 

       370        380        390        400        410        420 
HKLESHLLRV AAVGLGFTYT EPNYWKRYGA RQDEHSVPSS ISSEPEDGPR LSLTKKPTPK 

       430        440        450        460        470        480 
PDRELKEGGP LLYSDVKFVY NSQQLNGTQR VLLDNVISEE QCRELHRVAS GIMLAGDGYR 

       490        500        510        520        530        540 
GKTSPHTPNE RFEGATVLKA LKYGYEGRVP LKSARLFYDI SEKARRIVES YFMLNSTLYF 

       550        560        570        580        590        600 
SYTHLVCRTA LSGQQERRND LSHPIHADNC LLDPEANECW KEPPAYTFRD YSALLYMNAD 

       610        620        630        640        650        660 
FEGGEFIFTE MDAKTVTASI KPKCGRMVSF SSGGENPHGV KAVTKGQRCA VALWFTLDPL 

       670        680        690 
YRELERIQAD EVIAMLDQEH VGRSEMNINP KDEL

« Hide

References

[1]"Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes."
Vranka J.A., Sakai L.Y., Bachinger H.P.
J. Biol. Chem. 279:23615-23621(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY463529 mRNA. Translation: AAS45238.1.
IPIIPI00602752.
RefSeqNP_001001530.1. NM_001001530.1.
UniGeneGga.16244.

3D structure databases

ProteinModelPortalQ6JHU7.
ModBaseSearch...

Proteomic databases

PaxDbQ6JHU7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID414143.
KEGGgga:414143.

Organism-specific databases

CTD55214.

Phylogenomic databases

eggNOGNOG269251.
HOGENOMHOG000231087.
HOVERGENHBG053224.
InParanoidQ6JHU7.
OrthoDBEOG4WSW97.

Family and domain databases

Gene3D1.25.40.10. 3 hits.
InterProIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF13640. 2OG-FeII_Oxy_3. 1 hit.
[Graphical view]
SMARTSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
PS51471. FE2OG_OXY. 1 hit.
PS50005. TPR. False negative.
PS50293. TPR_REGION. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio20818680.

Entry information

Entry nameP3H2_CHICK
AccessionPrimary (citable) accession number: Q6JHU7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: July 5, 2004
Last modified: April 3, 2013
This is version 67 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

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