ID B0XDL7_CULQU Unreviewed; 520 AA.
AC B0XDL7;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN Name=6051274 {ECO:0000313|EnsemblMetazoa:CPIJ017129-PA};
GN ORFNames=CpipJ_CPIJ017129 {ECO:0000313|EMBL:EDS45527.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS45527.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS45527.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ017129-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ017129-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; DS232767; EDS45527.1; -; Genomic_DNA.
DR RefSeq; XP_001867741.1; XM_001867706.1.
DR AlphaFoldDB; B0XDL7; -.
DR STRING; 7176.B0XDL7; -.
DR EnsemblMetazoa; CPIJ017129-RA; CPIJ017129-PA; CPIJ017129.
DR KEGG; cqu:CpipJ_CPIJ017129; -.
DR VEuPathDB; VectorBase:CPIJ017129; -.
DR VEuPathDB; VectorBase:CQUJHB010108; -.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_024155_1_1_1; -.
DR InParanoid; B0XDL7; -.
DR OMA; RMEYPAK; -.
DR Proteomes; UP000002320; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000002320};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..520
FT /note="procollagen-proline 4-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011409329"
FT DOMAIN 398..505
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT COILED 50..84
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 520 AA; 59274 MW; E4E8B81003AEE1AB CRC64;
MVAAADFLLL KLVILTLGSY TVSAETQNRT EFYTSTVGME RLLQSELAIL DRLDTIIAKS
EAEITLLKRE RDRLRAEVAG AKQNPIAYVS NPIRAFLMTK RLLVEYRDID ARVRRGVGVE
LIDAWTALPR VDDLQGVAEG LSRLQEVYKM KAAELAKGNL NGERVVRELS VEECYWIGRA
MAQGACFRNA NQWFREALDR LEVEEACKVS RFEILDYYSH SLSEVGRYEE ALELTNELLE
INSTFVGGIA KKKVIEGWLD HIERNGRKRK LPKPAIIKLY EKLCRGDYER PGEVTSQLFC
RYETSATPFL RLAPLKLEVV NLEPLIVVYH EAVSDREIAK LIELARPLIK RSAVGDTRSE
QISKIRISQN AWFENEHDPI VETLNQRARD MAGGLNEPSY ELLQVNNYGL GGFYSIHYDW
STSANPFPNK GMGNRIATLM FYLSDVQEGG STVFPRLNLA VRPRKGTAIF WYNLHRNGKG
NKKTLHAACP VLIGSKWVAN KWIHERHQEF VRPCELDPKK
//
