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   16-JUN-2009, entry version 76.
DE   RecName: Full=Prolyl 4-hydroxylase subunit alpha-1;
DE            EC=1.14.11.2;
DE   AltName: Full=4-PH alpha-1;
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; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=95014533; PubMed=7929409;
RA   Veijola J., Koivunen P., Annunen P., Pihlajaniemi T., Kivirikko K.I.;
RT   "Cloning, baculovirus expression, and characterization of the alpha
RT   subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis
RT   elegans. This alpha subunit forms an active alpha beta dimer with the
RT   human protein 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   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   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   [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).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158, AND MASS
RP   SPECTROMETRY.
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
RT   to identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158, AND MASS
RP   SPECTROMETRY.
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.
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-1(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; 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   EMBL; Z81134; CAB03452.1; -; Genomic_DNA.
DR   EMBL; AL031635; CAB03452.1; JOINED; Genomic_DNA.
DR   PIR; A55069; A55069.
DR   PIR; T25418; T25418.
DR   RefSeq; NP_499464.1; -.
DR   UniGene; Cel.19527; -.
DR   Ensembl; Y47D3B.10; Caenorhabditis elegans.
DR   GeneID; 176569; -.
DR   KEGG; cel:Y47D3B.10; -.
DR   WormBase; WBGene00001077; dpy-18.
DR   WormPep; Y47D3B.10; CE20261.
DR   OMA; Q10576; NTERTMY.
DR   BRENDA; 1.14.11.2; 672.
DR   NextBio; 893122; -.
DR   ArrayExpress; Q10576; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
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:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:EC.
DR   GO; GO:0010171; P:body morphogenesis; IMP:WormBase.
DR   GO; GO:0040011; P:locomotion; IMP:WormBase.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0040018; P:positive regulation of multicellular organi...; IMP:WormBase.
DR   InterPro; IPR005123; Oxoglutarate/Fe-dep_Oase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR013547; Pro_4_hyd_alph_N.
DR   InterPro; IPR011990; TPR-like_helical.
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   SMART; SM00702; P4Hc; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Dioxygenase; Direct protein sequencing;
KW   Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding;
KW   Oxidoreductase; Signal; Vitamin C.
FT   SIGNAL        1     16
FT   CHAIN        17    559       Prolyl 4-hydroxylase subunit alpha-1.
FT                                /FTId=PRO_0000022728.
FT   DOMAIN      328    511       PKHD.
FT   METAL       422    422       Iron (By similarity).
FT   METAL       424    424       Iron (By similarity).
FT   METAL       493    493       Iron (By similarity).
FT   BINDING     503    503       2-oxoglutarate (Potential).
FT   CARBOHYD    158    158       N-linked (GlcNAc...).
FT   CONFLICT    297    301       QKDIS -> RRHL (in Ref. 1; AAA62207).
FT   CONFLICT    308    312       KRDRP -> LAGPS (in Ref. 1; AAA62207).
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
//