ID A0A2K6VM80_ONCVO Unreviewed; 589 AA.
AC A0A2K6VM80;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, 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};
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282 {ECO:0000313|EnsemblMetazoa:OVOC12409.1, ECO:0000313|Proteomes:UP000024404};
RN [1] {ECO:0000313|Proteomes:UP000024404}
RP NUCLEOTIDE SEQUENCE.
RA Cotton J., Tsai J., Stanley E., Tracey A., Holroyd N., Lustigman S.,
RA Berriman M.;
RT "Genome sequencing of Onchocerca volvulus.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:OVOC12409.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2018) to UniProtKB.
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; CMVM020000454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2K6VM80; -.
DR STRING; 6282.A0A2K6VM80; -.
DR EnsemblMetazoa; OVOC12409.1; OVOC12409.1; WBGene00249218.
DR OMA; NWEMKDI; -.
DR Proteomes; UP000024404; 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:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 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:UP000024404}.
SQ SEQUENCE 589 AA; 67756 MW; 05850041404C14AB CRC64;
MILWRVLHVF LLVAAVSAEV YSSLFSLKAI TGAKQDILVM INAYVEKEIG RLDYLKKFAQ
KVKEHIDKAI RDTEGAIRYP INAFLVIKEM TADWNKVVKI MQSNSADNVI RNVTRQRIIK
HIIYPTEEDL LGAATGLLRL QDTYQMDTKD IADGKILNSQ MCTVALTAGD CFEIGRVAYH
KYDYYHTIMW MQEALERAEK ETISTANIED ILEYLAISLY KQGNLKRALL FTDELCRMNP
DHPRAKDNMG EYENLLENNG IQRIDMRQGI PPIINVRHGN GLDKGVMLLY EALCRQEVPV
VTASSPCDTK AQFQLYCYYK MDHPYLRLAP FKVEIIRQNS LAVLFYDIML DDEVRVIQLL
AKPKACLVLL ALYYNTTKRS KIFNFLTGKS EPTSFRVAKS ARLRSTEHEI IKRIDRRLEL
ATNLEIETAE DLGVHNYGIG GQYEPHLDCA LISEGEECFE KLGTGNRIAT ILIYMTEPEI
GGRTVFMTNS KISLPCIKNA ALFWYNLMRD GKVDMRSRHA GCPVLTGVKW VANKWFHERG
QEWRRPCGLN QFDQERYVGD LGVPNPKHHL NMRSEAKKLK KMNRKHWEV
//
