Skip Header

Contribute Send feedback
Read comments (?) or add your own

P16924 (P4HA1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 93. 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 4-hydroxylase subunit alpha-1

Short name=4-PH alpha-1
EC=1.14.11.2
Alternative name(s):
Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
Gene names
Name:P4HA1
Synonyms:P4HA
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length516 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins By similarity.

Catalytic activity

L-proline-[procollagen] + 2-oxoglutarate + O2 = trans-4-hydroxy-L-proline-[procollagen] + succinate + CO2.

Cofactor

Binds 1 Fe2+ ion per subunit By similarity.

Ascorbate By similarity.

Subunit structure

Heterotetramer of two alpha chains and two beta chains (the beta chain is the multi-functional PDI) By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity.

Sequence similarities

Belongs to the P4HA family.

Contains 1 Fe2OG dioxygenase domain.

Contains 1 TPR repeat.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 516516Prolyl 4-hydroxylase subunit alpha-1
PRO_0000206659

Regions

Repeat189 – 22234TPR
Domain393 – 501109Fe2OG dioxygenase

Sites

Metal binding4111Iron By similarity
Metal binding4131Iron By similarity
Metal binding4821Iron By similarity
Binding site49212-oxoglutarate Potential

Amino acid modifications

Glycosylation971N-linked (GlcNAc...) Probable
Glycosylation2431N-linked (GlcNAc...) Probable

Sequences

Sequence LengthMass (Da)Tools
P16924 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 49EB14163CDE347B

FASTA51659,440
        10         20         30         40         50         60 
HTDFFTSIGH MTDLINTEKD LVISKLKDYI KAEESKLEQI KKWAEKLDKL TDTATKDPEG 

        70         80         90        100        110        120 
FLGHPANAFK LMKRLNTEWG ELESLVLKDM SDGFISNMTI QRQFFPNDED QTGARKALLR 

       130        140        150        160        170        180 
LQDTYNLDTD TLSRGNLPGV KHKSFLTAED CFELGKIRYT EADYYHTELW MEQALKQLDE 

       190        200        210        220        230        240 
GEVSSADKVY ILDYLSYAVY QQGDLSKAMM LTKRLLELDP EHQRANGNMK YFEYIMAKEK 

       250        260        270        280        290        300 
EANKSSTDAE DQTDKETEVK KKDYLPERRK YEMLCRGEGL KMTPRRQKRL FCRYYDGNRN 

       310        320        330        340        350        360 
PRYILGPVKQ EDEWDKPRIV RFLDIISDEE IETVKELAKP RLSRATVHDP ETGKLTTAHY 

       370        380        390        400        410        420 
RVSKSAWLSG YESPVVSRIN TRIQDLTGLD VSTAEELQVA NYGVGGQYEP HFDFGRKDEP 

       430        440        450        460        470        480 
DAFKELGTGN RIATWLFYMS DVSAGGATVF PEVGASVWPK KGTAVFWYNL FPSGEGDYST 

       490        500        510 
RHAACPVLVG NKWVSNKWLH ERGQEFRRPC TLSELE 

« Hide

References

[1]"Prolyl 4-hydroxylase: molecular cloning and the primary structure of the alpha subunit from chicken embryo."
Bassuk J.A., Kao W.W.-Y., Herzer P., Kedersha N., Seyer J., Demartino J.A., Daugherty B.L., Mark G.E. III, Berg R.A.
Proc. Natl. Acad. Sci. U.S.A. 86:7382-7386(1989) [PubMed: 2552442] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-516, PROTEIN SEQUENCE OF 1-42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26217 mRNA. Translation: AAA49002.1.
IPIIPI00598417.
PIRDACHA. A33832.
UniGeneGga.17975.

3D structure databases

ProteinModelPortalP16924.
SMRP16924. Positions 145-238.
ModBaseSearch...

Protein-protein interaction databases

STRINGP16924.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGveNOG13696.
GeneTreeENSGT00390000018885.
HOVERGENHBG006834.

Family and domain databases

InterProIPR005123. Oxoglutarate/Fe-dep_oxygenase.
IPR006620. Pro_4_hyd_alph.
IPR013547. Pro_4_hyd_alph_N.
IPR013026. TPR-contain.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
Gene3DG3DSA:1.25.40.10. TPR-like_helical. 1 hit.
PfamPF03171. 2OG-FeII_Oxy. 1 hit.
PF08336. P4Ha_N. 1 hit.
[Graphical view]
SMARTSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEPS51471. FE2OG_OXY. 1 hit.
PS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameP4HA1_CHICK
AccessionPrimary (citable) accession number: P16924
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: September 21, 2011
This is version 93 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