ID A0A3P8S742_AMPPE Unreviewed; 645 AA.
AC A0A3P8S742;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
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|Ensembl:ENSAPEP00000008603.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000008603.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000008603.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000008603.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3P8S742; -.
DR Ensembl; ENSAPET00000008847.1; ENSAPEP00000008603.1; ENSAPEG00000006169.1.
DR GeneTree; ENSGT00940000159593; -.
DR Proteomes; UP000265080; Chromosome 2.
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; 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:SF1; PROLYL 3-HYDROXYLASE 2; 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:UP000265080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..645
FT /note="procollagen-proline 3-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017943932"
FT DOMAIN 494..608
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 645 AA; 73582 MW; BC452C12E1C45F52 CRC64;
MDGNSPPAAV WCVVLLCAAL SSSAAFLEPY DLLYDTAVRA FYSSDYGGVV RSMEAALSSH
REVRRTKVRC RLRCQDQHPF EETFSDLRFF DAVLRRAACM DKCIEEKLGA QSVHKVSEDV
VQDFNRRIPY NYLQLAYQKL NQPDKAAAAA HTYFQANPEH VEMGQDLEQY KDLQGVQEDH
FVDREARPHQ RSFTAAVRLY DKGDYEAALG LFEEALVEYY KADVDCRALC QGPQRFEGHD
HLRYRYSLHE LVSDHFTQVL HCEHECVRDL ATRPGRLSPM ENYLPLHYDY LQFAYFKGTC
ALQCALTYLL FHDGEEFMTD NVDYFREVLG HDGKPREVRI SNQELHKSDI FKSLFPASFS
IFSVNALSKY SKYPGICAGG PLLYDNVQLV QNSVALNGTQ RVLLDHVISE DECADLRYLA
HAVTMAGDGY RGRMSPHTPN EKFEGATVLK TLQYGFEGRV PMRNARLFYD TSERARRIIE
SYFMLNSTLH FSYTHLVCRT AITGQQDHRN DLSHPIHADN CLLDPDANEC WKEPPAYTYR
DYSALLYLNG DFEGGEFIFT EMDAKTVTAS VKPRCGRMVG FSSGGENPHG VKAVTRGQRC
AVALWFTLDP LFRELERLQA DEVIQALDTQ SVWGQGLNIN PKDEL
//