ID   A0A3Q7S039_VULVU        Unreviewed;       678 AA.
AC   A0A3Q7S039;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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|RefSeq:XP_025851349.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025851349.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025851349.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025851349.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025851349.1};
RG   RefSeq;
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=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SIMILARITY: Belongs to the leprecan family.
CC       {ECO:0000256|ARBA:ARBA00006487}.
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DR   RefSeq; XP_025851349.1; XM_025995564.1.
DR   AlphaFoldDB; A0A3Q7S039; -.
DR   STRING; 9627.ENSVVUP00000015294; -.
DR   KEGG; vvp:112917513; -.
DR   OrthoDB; 5398065at2759; -.
DR   Proteomes; UP000286640; Unplaced.
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:0032963; P:collagen metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like 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   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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..678
FT                   /note="procollagen-proline 3-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018780732"
FT   DOMAIN          501..615
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          192..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..649
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..678
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   678 AA;  76121 MW;  92EFC20CB0ADAFF6 CRC64;
     MLRLLRLLLL LLLPPPGSPE PPGLAPLSPG APPQAPDLLY ADGLRAYAAG AWAPAPRAAL
     RRAECLTQCG ARRLGPGGAA RLRVGGALRD AFRRREPYNY LQRAYYQLKK LDLAAAAAHT
     FFVANPTHLQ MREDMAKYRR MSRVRPQSFR DLETPPHWAA YDEGLELLGR QEAELALPRL
     EEALQESLAQ MESCRAGCEG PEEQQSEEEE EGAGSQGGLY EIIAGHWIRV LQCRQRCVGD
     TATRPGRSFP VPDFLPSLLR QLHKAHAQVG NLSQAMENVL SVLLFYPEDE AAKKALNEYQ
     TQLGEPRPGL GPREDIQHFI LRSLGEKRQL YYAMEHLGAS FKDPDPWTPA AVIPEALREK
     LREDQEKRPW DHEPPQPKPL THWKDVLLLE GVTLTHDARQ LNGSERVVLD GLLTPAECGV
     LLQLAKDATE AGARSGYRGR RSPHSPHERF EGLTVLKAAQ LAHAGAVGSQ GAKLLLEVSE
     RVRTLTQAYF SPERPLHLSF TQLVCRSAIE GEQDQRMDLS HPVHADNCVL DPDTGECWRE
     PPAYTYRDYS GLLYLNDDFH GGDLFFTEPN ALTVTAQVRP RCGRLVAFSS GGENPHGVWA
     VTRGRRCALA LWHTWAPEHR EQEWTEAKEL LKEPEEEEEE EEEEEEMPSR DPSPEPPSRR
     LQRVQDKTGK LPRVREEL
//