P4HA1_CAEEL
ID P4HA1_CAEEL Reviewed; 559 AA.
AC Q10576; O18153;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-1;
DE Short=4-PH alpha-1;
DE EC=1.14.11.2;
DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1;
DE AltName: Full=Protein dumpy-18;
DE Flags: Precursor;
GN Name=dpy-18; Synonyms=phy-1; ORFNames=Y47D3B.10;
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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7929409; DOI=10.1016/s0021-9258(18)47082-2;
RA Veijola J., Koivunen P., Annunen P., Pihlajaniemi T., Kivirikko K.I.;
RT "Cloning, baculovirus expression, and characterization of the alpha subunit
RT of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans. This
RT alpha subunit forms an active alpha beta dimer with the human protein
RT disulfide isomerase/beta subunit.";
RL J. Biol. Chem. 269:26746-26753(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Bristol N2;
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 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 [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).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
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: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. Exists
CC either as a phy-1(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; U12762; AAA62207.1; -; mRNA.
DR EMBL; AJ270999; CAB71298.1; -; mRNA.
DR EMBL; AL031635; CAA21045.1; -; Genomic_DNA.
DR EMBL; Z81134; CAA21045.1; JOINED; Genomic_DNA.
DR PIR; A55069; A55069.
DR PIR; T25418; T25418.
DR RefSeq; NP_499464.1; NM_067063.3.
DR AlphaFoldDB; Q10576; -.
DR SMR; Q10576; -.
DR BioGRID; 41751; 11.
DR STRING; 6239.Y47D3B.10; -.
DR iPTMnet; Q10576; -.
DR World-2DPAGE; 0020:Q10576; -.
DR EPD; Q10576; -.
DR PaxDb; Q10576; -.
DR PeptideAtlas; Q10576; -.
DR EnsemblMetazoa; Y47D3B.10.1; Y47D3B.10.1; WBGene00001077.
DR GeneID; 176569; -.
DR KEGG; cel:CELE_Y47D3B.10; -.
DR UCSC; Y47D3B.10.2; c. elegans.
DR CTD; 176569; -.
DR WormBase; Y47D3B.10; CE20261; WBGene00001077; dpy-18.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_024155_1_1_1; -.
DR InParanoid; Q10576; -.
DR OMA; MLLMAWF; -.
DR OrthoDB; 391515at2759; -.
DR PhylomeDB; Q10576; -.
DR PRO; PR:Q10576; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001077; Expressed in embryo and 4 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; IDA:WormBase.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
DR GO; GO:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0010172; P:embryonic body morphogenesis; IGI:WormBase.
DR GO; GO:0043412; P:macromolecule modification; IDA:WormBase.
DR GO; GO:0019511; P:peptidyl-proline hydroxylation; IDA:WormBase.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IBA:GO_Central.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IGI:WormBase.
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; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Signal; Vitamin C.
FT SIGNAL 1..16
FT CHAIN 17..559
FT /note="Prolyl 4-hydroxylase subunit alpha-1"
FT /id="PRO_0000022728"
FT DOMAIN 404..512
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 422
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 424
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 493
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 503
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CONFLICT 297..301
FT /note="QKDIS -> RRHL (in Ref. 1; AAA62207)"
FT /evidence="ECO:0000305"
FT CONFLICT 308..312
FT /note="KRDRP -> LAGPS (in Ref. 1; AAA62207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 63927 MW; F3681F4560A2B83D CRC64;
MRLALLVLAT IGYAVADLFT SIADMQNLLE TERNIPKILD KYIHDEEERL VQLKKLSEEY
SKKNEISIEN GLKDITNPIN AFLLIKRKIF DWKEIESKMN ANKAGNVVSS ITDDSYGVRY
PTADDLSGAA IGLLRLQDTY RLDTKDLADG KIYADQGNYT FSAKDCFEIA RAAYNEHDFY
HTVMWMEEAQ RRLGDEVEPT VEVEDILEYL AFALYKQNNL KHALKLTEEL YKMNPTHPRA
KGNVKWYEDL LEQEGVRRSD MRKNLPPIQN RRPDSVLGNT ERTMYEALCR NEVPVSQKDI
SRLYCYYKRD RPFLVYAPIK VEIKRFNPLA VLFKDVISDD EVAAIQELAK PKLARATVHD
SVTGKLVTAT YRISKSAWLK EWEGDVVETV NKRIGYMTNL EMETAEELQI ANYGIGGHYD
PHFDHAKKEE SKSFESLGTG NRIATVLFYM SQPSHGGGTV FTEAKSTILP TKNDALFWYN
LYKQGDGNPD TRHAACPVLV GIKWVSNKWI HEKGNEFRRP CGLKSSDYER FVGDLGYGPE
PRNAPNVSPN LAKDVWETL
