ID A0A3L8SJ95_CHLGU Unreviewed; 563 AA.
AC A0A3L8SJ95;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
DE Flags: Fragment;
GN ORFNames=DV515_00006954 {ECO:0000313|EMBL:RLW02992.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW02992.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW02992.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW02992.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW02992.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other
CC proteins. {ECO:0000256|ARBA:ARBA00002035}.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the P4HA family.
CC {ECO:0000256|ARBA:ARBA00006511}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW02992.1}.
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DR EMBL; QUSF01000017; RLW02992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SJ95; -.
DR STRING; 44316.ENSEGOP00005016253; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:UniProtKB-EC.
DR Gene3D; 6.10.140.1460; -; 1.
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; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR013547; Pro_4_hyd_alph_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10869:SF240; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-2; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF08336; P4Ha_N; 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:UP000276834}.
FT DOMAIN 440..548
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RLW02992.1"
SQ SEQUENCE 563 AA; 64822 MW; 9C0364BA77AE04C1 CRC64;
VLCEGGVELK GCCDRLYQGI WKMKPWLQLM FFPCVFLIWH TEAEFFTSIG QMTDLIYAEK
DLVQSLQEYI RAEEKKLSQI KSWAEKMDIL TSKSASDPEG YLAHPVNAYK LVKRLNTDWL
ELENLVLQDT THGFIANLTI QRQFFPTEED ETGAAKALMR LQDTYKLDPE TLSRGNLPGT
KYRSSLTVGD CFGMGKTAYN DGDYYHTVLW MEQALKQHDE GEDTTVSKVE ILDYLSYAVF
QFGDLHRAME LTRRLISLDS THERAGSNLR YFEKLLEKER EEKEKENSIN KTVTTTEAVV
QSGAYERPLD YLPERDIYEA LCRGEGVKMT PRRQKRLFCR YHDGNRNPHL LIAPFKEEDE
WDSPHIVRYY DVMSDEEIEK IKQLAKPKLA RATVRDPKTG VLTVASYRVS KSSWLEEDDD
PVVAKVNQRM QQITGLTVET AELLQVANYG MGGQYEPHFD FSRKDEPDAF KRLGTGNRVA
TFLNYMSDVE AGGATVFPDF GAAIWPKKGT AVFWYNLFRS GEGDYRTRHA ACPVLVGCKW
VSNKWFHERG NEFLRPCGRT EVD
//
