ID A0A182REC0_ANOFN Unreviewed; 393 AA.
AC A0A182REC0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN004542-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN004542-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN004542-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A182REC0; -.
DR STRING; 62324.A0A182REC0; -.
DR EnsemblMetazoa; AFUN004542-RA; AFUN004542-PA; AFUN004542.
DR VEuPathDB; VectorBase:AFUN004542; -.
DR VEuPathDB; VectorBase:AFUN2_009787; -.
DR OrthoDB; 2899308at2759; -.
DR Proteomes; UP000075900; 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; 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 InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10869:SF207; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-2; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF08336; P4Ha_N; 1.
DR Pfam; PF07719; TPR_2; 1.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 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 TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 84..117
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 269..378
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 393 AA; 44298 MW; 1AE1F6A5775FB808 CRC64;
MPTVDDLVGI AEGLARLQDM YQLDTKAMAS GKLFDRKVGR QLKTAECYEI GNKLTSATNY
RYAVSWLRES LRLWTTESPG VSKVEVMNAL AYALSNQGEY EEALELTNKV LKLQPDNQRA
LNSKEPLEKW IEYKKEHGLP PPVPDANYKN YPSLCRGDYQ RSTKEVAKLR CRYEHNRTPF
LRIAPLKLEE LNHDPFIVVY HEVLYAKEIA TLLDIAKPLL HRSMVGDDLQ NKVSKTRTSN
NGCLNAVIHP VVRTISRRTE DMTDLAMSAA EQLQVGNYGV GGHYLPHHDY AVPEEGKEAY
PAVGKGNRIA TVMYYLSDVA IGGATVFPEL GVGVFPRKGS AIFWYNLHAN GSIDARTLHG
ACPVFVGSKW VANKWIHEYG QEFRRPCQID QKV
//