ID A0A093EQ44_TYTAL Unreviewed; 515 AA.
AC A0A093EQ44;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=N341_02894 {ECO:0000313|EMBL:KFV46170.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV46170.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV46170.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV46170.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KK376343; KFV46170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093EQ44; -.
DR Proteomes; UP000054190; 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:UP000054190}.
FT DOMAIN 392..500
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV46170.1"
FT NON_TER 515
FT /evidence="ECO:0000313|EMBL:KFV46170.1"
SQ SEQUENCE 515 AA; 59171 MW; 163F267331A1333C CRC64;
LGQMTDLIYA EKDLVQSLKE YIRAEESKLS QIKSWAEKMD VLTSKSTSDP EGYLAHPVNA
YKLVKRLNTD WLELENLVLQ DTTNGFIANL TIQRQFFPTE EDETGAAKAL MRLQDTYKLD
PETLSRGNLP GTKYRSSLTV GDCFGMGKTA YNDGDYYHTV LWMEQALKQH DEGEDTIVSK
VEILDYLSYA VFQFGDLHRA MELTRRLISL DSAHERAGSN LRYFEKLLEK EREEKEKEKS
INKTMTTTEP VVQSGAYERP LDYLPERDIY EALCRGEGVK MTPRRQKRLF CRYHNGNRNP
HLLIAPFKEE DEWDSPHIVR YYDVMSDEEI EKIKQLAKPR LARATVRDPK TGVLTVASYR
VSKSSWLEED DDPVVAKVNQ RMQQITGLTV KTAELLQVAN YGMGGQYEPH FDFSRKDEPD
AFKRLGTGNR VATFLNYMSD VEAGGATVFP DFGAAIWPKK GTAVFWYNLF RSGEGDYRTR
HAACPVLVGC KWVSNKWFHE RGNEFLRPCG RTEVD
//
