ID A0A3P8QKN1_ASTCA Unreviewed; 681 AA.
AC A0A3P8QKN1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:ENSACLP00000029622.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000029622.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000029622.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000029622.1}
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; A0A3P8QKN1; -.
DR STRING; 8154.ENSACLP00000029622; -.
DR Ensembl; ENSACLT00000030321.1; ENSACLP00000029622.1; ENSACLG00000020074.1.
DR GeneTree; ENSGT00940000159593; -.
DR OMA; LECARSY; -.
DR OrthoDB; 5398065at2759; -.
DR Proteomes; UP000265100; Chromosome 23.
DR Bgee; ENSACLG00000020074; Expressed in spleen and 7 other cell types or tissues.
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 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 Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..681
FT /note="procollagen-proline 3-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018035475"
FT DOMAIN 530..644
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 681 AA; 77772 MW; AD9C54A62849E63C CRC64;
MDGNLFPTLI FLPVLLSAVL PSSAGVLEPY DLLYDNAVEA FYSADYESVV RYMEGALSSH
RQVRATRVRC RLRCQDQHPL DESFSDLRFF DSVLRRAACM NKCIEEKVGT QSLHKVSEDV
VQDFNRRIPY NYLQQAYQKL QRPDKAAEAA HTYFQANPEH VEMGRDLEQY KNLQGVEETH
FVDREARPHQ RSFTAAVQLY DKGDYEGATA LFEEALVEYY KADVDCRALC QGPQKFEGQD
HLRYRYSLHE VVSDHFTQVL HCEHECVRDL ATRPGRLSPM ENYLPLHYDY LQFAYFKAGR
LEEALQCALT YLLFHEGEEF MKENADYYRE ELGHDAEPRE KAAWYLRRHK QELKLLLIGS
KIMGAEFTEG NYWRSTGGRD DSNSVPSGTD GWMEYVPISH KKNVTVTSPQ SLKEGGPLLY
EGVQLVQNSA ALNGTQRVLL DHVLSEEECA ELRQLAHTVT MAGDGYKGRM SPHTPNEKFE
GASVLKTLQH GFEGRVPMRS ARLFYETSER ARRIIESYFV LNSTLHFSYT HLVCRTAIKG
QQDHRNDLSH PIHADNCLLD PDANECWKEP PAYTNRDYSA LLYLNADFEG GEFVFTEMDA
KTVTASVKPK CGRMVGFSSG GENPHGVKAV TSGQRCAVAL WFTLNPLYRE LERLQADEVV
QALDTQHVFG QGLNINPKDE L
//