ID H0WLY9_OTOGA Unreviewed; 739 AA.
AC H0WLY9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=procollagen-proline 3-dioxygenase {ECO:0000256|ARBA:ARBA00012262};
DE EC=1.14.11.7 {ECO:0000256|ARBA:ARBA00012262};
GN Name=P3H3 {ECO:0000313|Ensembl:ENSOGAP00000002707.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000002707.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000002707.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC trans-3-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:22872, Rhea:RHEA-
CC COMP:11676, Rhea:RHEA-COMP:11678, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:85428; EC=1.14.11.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024148};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the leprecan family.
CC {ECO:0000256|ARBA:ARBA00006487}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAQR03127833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03127834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003796441.1; XM_003796393.2.
DR AlphaFoldDB; H0WLY9; -.
DR STRING; 30611.ENSOGAP00000002707; -.
DR Ensembl; ENSOGAT00000003026.2; ENSOGAP00000002707.2; ENSOGAG00000003025.2.
DR GeneID; 100951275; -.
DR KEGG; oga:100951275; -.
DR CTD; 10536; -.
DR eggNOG; KOG4459; Eukaryota.
DR GeneTree; ENSGT00940000159164; -.
DR HOGENOM; CLU_017820_0_0_1; -.
DR InParanoid; H0WLY9; -.
DR OMA; KQCWREP; -.
DR OrthoDB; 5398065at2759; -.
DR TreeFam; TF320837; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:1902494; C:catalytic complex; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0032964; P:collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR039575; P3H.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR14049; LEPRECAN 1; 1.
DR PANTHER; PTHR14049:SF14; PROLYL 3-HYDROXYLASE 3; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..739
FT /note="procollagen-proline 3-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003543698"
FT DOMAIN 561..675
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 254..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..710
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 82217 MW; 0D5AF06BCEA0FE36 CRC64;
MLWLLRLLLL LLLLPPPGSP EPPGLAPVFP GAPPQAPDLL YADGLRAYSA GAWAPAVALL
REALRSWAEL GRARRDCGAS CAAEPGAALP FVLLGATSPD LGPGPAQGSW ERLLLRAALR
RAECLTQCAA RRLGPGGAAR LRVGSALRDA FRRREPYNYL QGAYYKLKKL DLAAAAAHTF
FVANPTHLQM REDMAKYRRM SGVQPQSFRD LETPPHWAAY DTGLELLRRQ EAGLALPRLE
EALQGSLAQM ESCRAGCEGP EEQQGAGEEE EGAGSQGGLY EAIAGHWIRV LQCRQRCVGE
TATRPGRSFP VPDFLPSQLR WLHETYAQVG NLSQAVENVL SVLLFYPEDE AAKSALNKYQ
AQIGEPRPGL GPREDIQHFF LRSLGEKRQL YYAMEHLGIN FTDPDPWTPA ALIPETLREK
LREDQEKRPW DHEPPQPKPL TYWKDVLLLE GVTLTQDARQ LNGSERAVLD GLLTPAECGV
LLQLAKDAAG AGARSGYRGR RSPHTPHERF EGLTVLKAVQ LARAGTIGSQ GAKLLLEVSE
RVRTVTQAYF SPERPLHLSF THLVCRSAIE GEQEQRMDLS HPVHADNCVL DPDTGECWRE
PPAYTYRDYS GLLYLNDDFQ GGDLFFTEPN ALTVTAQVRP RCGRLVAFSS GGENPHGVWA
VTRGRRCALA LWHTWAPEHR EQEWTEAKEL LRESEEEEES EEEEEEEMPS RDPSPEPPSH
RLHRVQDKTG KPARIREEL
//
