P4HA2_CAEEL
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 03-AUG-2022, entry version 142.
DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-2;
DE Short=4-PH alpha-2;
DE EC=1.14.11.2;
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; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX 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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=10805750; 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 required
RT for exoskeleton formation and the maintenance of body shape in the nematode
RT Caenorhabditis elegans.";
RL Mol. Cell. Biol. 20:4084-4093(2000).
RN [3]
RP FUNCTION.
RX PubMed=10781079; DOI=10.1073/pnas.97.9.4736;
RA Friedman L., Higgin J.J., Moulder G., Barstead R., Raines R.T., 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 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 prolyl
RT 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. {ECO:0000269|PubMed:10781079, ECO:0000269|PubMed:10805750}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC trans-4-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:18945, Rhea:RHEA-
CC COMP:11676, Rhea:RHEA-COMP:11680, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.2;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Note=Binds 1 Fe(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains. Exist
CC either as a phy-2(2)/pdi-2(2) tetramer or as a phy-1/phy-2/pdi-2(2)
CC tetramer. {ECO:0000269|PubMed:12036960}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR EMBL; Z69637; CAA93469.1; -; Genomic_DNA.
DR PIR; T21816; T21816.
DR RefSeq; NP_502317.1; NM_069916.3.
DR AlphaFoldDB; Q20065; -.
DR SMR; Q20065; -.
DR BioGRID; 43263; 10.
DR STRING; 6239.F35G2.4; -.
DR EPD; Q20065; -.
DR PaxDb; Q20065; -.
DR PeptideAtlas; Q20065; -.
DR EnsemblMetazoa; F35G2.4.1; F35G2.4.1; WBGene00004025.
DR GeneID; 178170; -.
DR KEGG; cel:CELE_F35G2.4; -.
DR UCSC; F35G2.4.1; c. elegans.
DR CTD; 178170; -.
DR WormBase; F35G2.4; CE05811; WBGene00004025; phy-2.
DR eggNOG; KOG1591; Eukaryota.
DR GeneTree; ENSGT00940000163795; -.
DR HOGENOM; CLU_024155_1_1_1; -.
DR InParanoid; Q20065; -.
DR OMA; NLTQYRN; -.
DR OrthoDB; 391515at2759; -.
DR PhylomeDB; Q20065; -.
DR BRENDA; 1.14.11.2; 1045.
DR PRO; PR:Q20065; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004025; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0031545; F:peptidyl-proline 4-dioxygenase activity; IDA:WormBase.
DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IBA:GO_Central.
DR GO; GO:0043412; P:macromolecule modification; IDA:WormBase.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR013547; Pro_4_hyd_alph_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10869; PTHR10869; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF08336; P4Ha_N; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome; Signal; Vitamin C.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..539
FT /note="Prolyl 4-hydroxylase subunit alpha-2"
FT /id="PRO_0000022729"
FT DOMAIN 401..509
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 419
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 421
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 490
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 500
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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
