LOCUS NP_000908 534 aa linear PRI 22-OCT-2008
DEFINITION prolyl 4-hydroxylase, alpha I subunit isoform 1 precursor [Homo
sapiens].
ACCESSION NP_000908
VERSION NP_000908.2 GI:63252886
DBSOURCE REFSEQ: accession NM_000917.2
KEYWORDS .
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 534)
AUTHORS Barbe,L., Lundberg,E., Oksvold,P., Stenius,A., Lewin,E.,
Bjorling,E., Asplund,A., Ponten,F., Brismar,H., Uhlen,M. and
Andersson-Svahn,H.
TITLE Toward a confocal subcellular atlas of the human proteome
JOURNAL Mol. Cell Proteomics 7 (3), 499-508 (2008)
PUBMED 18029348
REFERENCE 2 (residues 1 to 534)
AUTHORS Koivunen,P., Hirsila,M., Kivirikko,K.I. and Myllyharju,J.
TITLE The length of peptide substrates has a marked effect on
hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases
JOURNAL J. Biol. Chem. 281 (39), 28712-28720 (2006)
PUBMED 16885164
REMARK GeneRIF: HIF-P4H, HIF-1alpha and HIF-2alpha are effective oxygen
sensors
REFERENCE 3 (residues 1 to 534)
AUTHORS Fahling,M., Mrowka,R., Steege,A., Nebrich,G., Perlewitz,A.,
Persson,P.B. and Thiele,B.J.
TITLE Translational control of collagen prolyl 4-hydroxylase-alpha(I)
gene expression under hypoxia
JOURNAL J. Biol. Chem. 281 (36), 26089-26101 (2006)
PUBMED 16837461
REMARK GeneRIF: Results suggest that the alteration of translational
efficiency by nucleolin, which occurs through a hypoxia inducible
factor independent pathway, is an important step in collagen prolyl
4-hydroxylase-alpha(I) regulation under hypoxia.
REFERENCE 4 (residues 1 to 534)
AUTHORS Grimmer,C., Balbus,N., Lang,U., Aigner,T., Cramer,T., Muller,L.,
Swoboda,B. and Pfander,D.
TITLE Regulation of type II collagen synthesis during osteoarthritis by
prolyl-4-hydroxylases: possible influence of low oxygen levels
JOURNAL Am. J. Pathol. 169 (2), 491-502 (2006)
PUBMED 16877351
REMARK GeneRIF: In comparison with healthy cartilage, Osteoarthritis
articular chondrocytes exhibit increased in vivo synthesis of
collagen prolyl-4-hydroxylase type II, a pivotal enzyme in collagen
triple helix formation.
REFERENCE 5 (residues 1 to 534)
AUTHORS Chen,L., Shen,Y.H., Wang,X., Wang,J., Gan,Y., Chen,N., Wang,J.,
LeMaire,S.A., Coselli,J.S. and Wang,X.L.
TITLE Human prolyl-4-hydroxylase alpha(I) transcription is mediated by
upstream stimulatory factors
JOURNAL J. Biol. Chem. 281 (16), 10849-10855 (2006)
PUBMED 16488890
REMARK GeneRIF: positive (transforming growth factor beta1) and negative
(cigarette smoking extract) regulators appear to influence the
USF-E-box interaction and affect P4Halpha(I) expression
REFERENCE 6 (residues 1 to 534)
AUTHORS Horelli-Kuitunen,N., Kvist,A.P., Helaakoski,T., Kivirikko,K.,
Pihlajaniemi,T. and Palotie,A.
TITLE The order and transcriptional orientation of the human COL13A1 and
P4HA genes on chromosome 10 long arm determined by high-resolution
FISH
JOURNAL Genomics 46 (2), 299-302 (1997)
PUBMED 9417920
REFERENCE 7 (residues 1 to 534)
AUTHORS Annunen,P., Helaakoski,T., Myllyharju,J., Veijola,J.,
Pihlajaniemi,T. and Kivirikko,K.I.
TITLE Cloning of the human prolyl 4-hydroxylase alpha subunit isoform
alpha(II) and characterization of the type II enzyme tetramer. The
alpha(I) and alpha(II) subunits do not form a mixed
alpha(I)alpha(II)beta2 tetramer
JOURNAL J. Biol. Chem. 272 (28), 17342-17348 (1997)
PUBMED 9211872
REFERENCE 8 (residues 1 to 534)
AUTHORS Helaakoski,T., Veijola,J., Vuori,K., Rehn,M., Chow,L.T.,
Taillon-Miller,P., Kivirikko,K.I. and Pihlajaniemi,T.
TITLE Structure and expression of the human gene for the alpha subunit of
prolyl 4-hydroxylase. The two alternatively spliced types of mRNA
correspond to two homologous exons the sequences of which are
expressed in a variety of tissues
JOURNAL J. Biol. Chem. 269 (45), 27847-27854 (1994)
PUBMED 7961714
REFERENCE 9 (residues 1 to 534)
AUTHORS Pajunen,L., Jones,T.A., Helaakoski,T., Pihlajaniemi,T., Solomon,E.,
Sheer,D. and Kivirikko,K.I.
TITLE Assignment of the gene coding for the alpha-subunit of prolyl
4-hydroxylase to human chromosome region 10q21.3-23.1
JOURNAL Am. J. Hum. Genet. 45 (6), 829-834 (1989)
PUBMED 2556027
REFERENCE 10 (residues 1 to 534)
AUTHORS Helaakoski,T., Vuori,K., Myllyla,R., Kivirikko,K.I. and
Pihlajaniemi,T.
TITLE Molecular cloning of the alpha-subunit of human prolyl
4-hydroxylase: the complete cDNA-derived amino acid sequence and
evidence for alternative splicing of RNA transcripts
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 86 (12), 4392-4396 (1989)
PUBMED 2543975
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AL702003.1, M24486.1,
BC034998.1 and AA780802.1.
On May 11, 2005 this sequence version replaced gi:4505565.
Summary: This gene encodes a component of prolyl 4-hydroxylase, a
key enzyme in collagen synthesis composed of two identical alpha
subunits and two beta subunits. The encoded protein is one of
several different types of alpha subunits and provides the major
part of the catalytic site of the active enzyme. In collagen and
related proteins, prolyl 4-hydroxylase catalyzes the formation of
4-hydroxyproline that is essential to the proper three-dimensional
folding of newly synthesized procollagen chains. Alternatively
spliced transcript variants encoding different isoforms have been
described. [provided by RefSeq].
Transcript Variant: This variant (1) encodes isoform 1.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the
Entrez Gene record to access additional publications.
FEATURES Location/Qualifiers
source 1..534
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="10"
/map="10q21.3-q23.1"
Protein 1..534
/product="prolyl 4-hydroxylase, alpha I subunit isoform 1
precursor"
/EC_number="1.14.11.2"
/calculated_mol_wt=59028
sig_peptide 1..17
/calculated_mol_wt=1958
sig_peptide 18..534
/product="prolyl 4-hydroxylase, alpha I subunit isoform 1"
/calculated_mol_wt=59028
CDS 1..534
/gene="P4HA1"
/gene_synonym="P4HA"
/coded_by="NM_000917.2:134..1738"
/note="isoform 1 precursor is encoded by transcript
variant 1"
/db_xref="CCDS:CCDS7320.1"
/db_xref="GeneID:5033"
/db_xref="HGNC:8546"
/db_xref="HPRD:08901"
/db_xref="MIM:176710"
ORIGIN
1 miwyiliigi llpqslahpg fftsigqmtd lihtekdlvt slkdyikaee dkleqikkwa
61 ekldrltsta tkdpegfvgh pvnafklmkr lntewselen lvlkdmsdgf isnltiqrqy
121 fpndedqvga akallrlqdt ynldtdtisk gnlpgvkhks fltaedcfel gkvayteady
181 yhtelwmeqa lrqldegeis tidkvsvldy lsyavyqqgd ldkallltkk lleldpehqr
241 angnlkyfey imakekdvnk sasddqsdqk ttpkkkgvav dylperqkye mlcrgegikm
301 tprrqkklfc ryhdgnrnpk filapakqed ewdkpriirf hdiisdaeie ivkdlakprl
361 sratvhdpet gklttaqyrv sksawlsgye npvvsrinmr iqdltgldvs taeelqvany
421 gvggqyephf dfarkdepda fkelgtgnri atwlfymsdv saggatvfpe vgasvwpkkg
481 tavfwynlfa sgegdystrh aacpvlvgnk wvsnkwlher gqefrrpctl sele
//