ID   P4HA2_CAEEL             Reviewed;         539 AA.
AC   Q20065;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   04-NOV-2008, entry version 59.
DE   RecName: Full=Prolyl 4-hydroxylase subunit alpha-2;
DE            EC=1.14.11.2;
DE   AltName: Full=4-PH alpha-2;
DE   AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2;
DE   Flags: Precursor;
GN   Name=phy-2; ORFNames=F35G2.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION.
RX   MEDLINE=20266296; PubMed=10805750;
RX   DOI=10.1128/MCB.20.11.4084-4093.2000;
RA   Winter A.D., Page A.P.;
RT   "Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme
RT   required for exoskeleton formation and the maintenance of body shape
RT   in the nematode Caenorhabditis elegans.";
RL   Mol. Cell. Biol. 20:4084-4093(2000).
RN   [3]
RP   FUNCTION.
RX   MEDLINE=20243765; PubMed=10781079; DOI=10.1073/pnas.97.9.4736;
RA   Friedman L., Higgin J.J., Moulder G., Barstead R., Raines R.T.,
RA   Kimble J.;
RT   "Prolyl 4-hydroxylase is required for viability and morphogenesis in
RT   Caenorhabditis elegans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:4736-4741(2000).
RN   [4]
RP   SUBUNIT.
RX   MEDLINE=22151124; PubMed=12036960; DOI=10.1074/jbc.M203824200;
RA   Myllyharju J., Kukkola L., Winter A.D., Page A.P.;
RT   "The exoskeleton collagens in Caenorhabditis elegans are modified by
RT   prolyl 4-hydroxylases with unique combinations of subunits.";
RL   J. Biol. Chem. 277:29187-29196(2002).
CC   -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC       hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other
CC       proteins.
CC   -!- CATALYTIC ACTIVITY: Procollagen L-proline + 2-oxoglutarate + O(2)
CC       = procollagen trans-4-hydroxy-L-proline + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit.
CC   -!- COFACTOR: Ascorbate.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC       Exist either as a phy-2(2)/pdi-2(2) tetramer or as a phy-1/phy-
CC       2/pdi-2(2) tetramer.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- SIMILARITY: Belongs to the P4HA family.
CC   -!- SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.
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DR   EMBL; Z69637; CAA93469.1; -; Genomic_DNA.
DR   PIR; T21816; T21816.
DR   RefSeq; NP_502317.1; -.
DR   UniGene; Cel.12536; -.
DR   Ensembl; F35G2.4; Caenorhabditis elegans.
DR   GeneID; 178170; -.
DR   KEGG; cel:F35G2.4; -.
DR   WormBase; WBGene00004025; phy-2.
DR   WormPep; F35G2.4; CE05811.
DR   NextBio; 900006; -.
DR   ArrayExpress; Q20065; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR005123; 2OG-FeII_Oase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR013547; Pro_4_hyd_alph_N.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR013105; TPR_2.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF08336; P4Ha_N; 1.
DR   Pfam; PF07719; TPR_2; 1.
DR   SMART; SM00702; P4Hc; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein;
KW   Iron; Metal-binding; Oxidoreductase; Signal; Vitamin C.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17    539       Prolyl 4-hydroxylase subunit alpha-2.
FT                                /FTId=PRO_0000022729.
FT   DOMAIN      325    508       PKHD.
FT   METAL       419    419       Iron (By similarity).
FT   METAL       421    421       Iron (By similarity).
FT   METAL       490    490       Iron (By similarity).
FT   BINDING     500    500       2-oxoglutarate (Potential).
FT   CARBOHYD    110    110       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   539 AA;  61527 MW;  718F76F84193B02B CRC64;
     MRAVLLVCLL AGLAHADLFT AIADLQHMLG AEKDVTTIID QYIEAERARL DDLRRYAHEY
     VHRNAHAESV GPEFVTNPIN AYLLIKRLTT EWKKVENIML NNKASTFLKN ITDNRVRSEV
     KFPGEEDLSG AATALLRLQD TYSLDTLDLS NGIIGGEKVS NKLSGHDTFE VGRSAYNQKD
     YYHCLMWMQV ALVKIENENP PTIEEWEILE YLAYSLYQQG NVRRALSLTK RLAKIAPNHP
     RAKGNVKWYE DMLQGKDMVG DLPPIVNKRV EYDGIVERDA YEALCRGEIP PVEPKWKNKL
     RCYLKRDKPF LKLAPIKVEI LRFDPLAVLF KNVIHDSEIE VIKELASPKL KRATVQNSKT
     GELEHATYRI SKSAWLKGDL DPVIDRVNRR IEDFTNLNQA TSEELQVANY GLGGHYDPHF
     DFARKEEKNA FKTLNTGNRI ATVLFYMSQP ERGGATVFNH LGTAVFPSKN DALFWYNLRR
     DGEGDLRTRH AACPVLLGVK WVSNKWIHEK GQEFTRPCGL EEEVQENFIG DLSPYANDP
//