ID   A0A2Y9EGK3_PHYMC        Unreviewed;       707 AA.
AC   A0A2Y9EGK3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=procollagen-proline 3-dioxygenase {ECO:0000256|ARBA:ARBA00012262};
DE            EC=1.14.11.7 {ECO:0000256|ARBA:ARBA00012262};
GN   Name=P3H2 {ECO:0000313|RefSeq:XP_007102333.2};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007102333.2};
RN   [1] {ECO:0000313|RefSeq:XP_007102333.2}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007102333.2};
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=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}.
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DR   RefSeq; XP_007102333.2; XM_007102271.3.
DR   AlphaFoldDB; A0A2Y9EGK3; -.
DR   Ensembl; ENSPCTT00005019961; ENSPCTP00005018109; ENSPCTG00005012805.
DR   KEGG; pcad:102993003; -.
DR   InParanoid; A0A2Y9EGK3; -.
DR   OrthoDB; 5398065at2759; -.
DR   Proteomes; UP000248484; Chromosome 1.
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:0032963; P:collagen metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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:SF1; PROLYL 3-HYDROXYLASE 2; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF48452; TPR-like; 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:UP000248484};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..707
FT                   /note="procollagen-proline 3-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016040876"
FT   DOMAIN          556..670
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   707 AA;  80759 MW;  BFD0963C33A4FD42 CRC64;
     MRERIWAQLP LLLPWLLLPP PPLWGGPPDG RCPESEPEPG PLQPFDLLYA SGVAAYYSGD
     YEVAVRDLEA ALRSHRRLRE ICARCARHCA ARRPLVPPGA GPGAELPFFR ALLERARCYR
     SCQSQRLGGP ASRHRASEDV RSDFQRRVPY NYLQRAYIKL NQLEKAVEAA HTFFMANPEH
     MEMQQNIKNY RTMVGVEDLQ LVDRDAKPHL ESYSEGVKHY EADDFELAIK YFEQALREYF
     NEDTECRALC EGPQRFEEYE YLGYKAGLYE AIADHYVQVL VCQHECVREL ATRPGRLSPI
     ENFLPLHYDY LQFAYYRVGE YVKALECAKA YLLLHPDDED VRDNVDYYES LLDDSTDPAS
     IQAREDLAMF VKHHKLESEL IKSAAEGLGF SYTEPNYWIQ YGGRQDENQV PSGVNVEGAE
     VHGLSTRKKS SPKIDRDLRE GGPLLYENIT FVYNSEQLNG TQRVLLDNVL SEEQCQELHS
     VASGIMLVGD GYRGKTSPHT PNEKFEGATV LKALKFGYEG RVPLKSARLF YDISEKARKI
     VESYFMLNST LYFSYTHMVC RTALSGQQDR RNDLSHPIHA DNCLLDPEAN ECWKEPPAYT
     FRDYSALLYM NDDFEGGEFI FTEMDAKTVT ASIKPKCGRM ISFSSGGENP HGVKAVTKGQ
     RCAVALWFTL DPLYRELERI QADEVIAILD QEQPGKHKPN INPKDEL
//