ID A0A091JV59_COLST Unreviewed; 510 AA.
AC A0A091JV59;
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=N325_01752 {ECO:0000313|EMBL:KFP27863.1};
OS Colius striatus (Speckled mousebird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP27863.1, ECO:0000313|Proteomes:UP000053615};
RN [1] {ECO:0000313|EMBL:KFP27863.1, ECO:0000313|Proteomes:UP000053615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP27863.1};
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; KK530536; KFP27863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091JV59; -.
DR Proteomes; UP000053615; 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:UP000053615}.
FT DOMAIN 387..495
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP27863.1"
FT NON_TER 510
FT /evidence="ECO:0000313|EMBL:KFP27863.1"
SQ SEQUENCE 510 AA; 58503 MW; 9526E850569DA990 CRC64;
LGQMTDLIYA EKDLVQSLKE YIRAEENKLS QIKSWAEKMD VLTSKSTSDP EGYLAHPVNA
YKLVKRLNTD WLELENLVLQ DTTNGFIANL TIQRQFFPTE EDETGAAKAL MRLQDTYKLD
PETLSRGNLP GKSTLTVGDC FGMGKTAYND GDYYHTVLWM EQALKQHDEG EDTTVSKVEI
LDYLSYAVFQ FGDLHRAMEL TRRLISLDST HERAGSNLRY FEKLLEKERE EEKDKSVNET
MTTEPVVQSG AYERPLDYLP ERDIYEALCR GEGVKMTPRR QKRLFCRYHD GNRNPNLLIA
PFKEEDEWDS PHIVRYYDVM SDEEIEKIKQ LAKPKLARAT VRDPKTGVLT VASYRVSKSS
WLEEDDDPVV AKVNQRMQQI TGLTVKTAEL LQVANYGMGG QYEPHFDFSR KDEPDAFKRL
GTGNRVATFL NYMSDVEAGG ATVFPDFGAA IWPKKGTAVF WYNLFRSGEG DYRTRHAACP
VLVGCKWVSN KWFHERGNEF LRPCGRTEVD
//
