PLOD_DROME
ID PLOD_DROME Reviewed; 721 AA.
AC Q9VTH0; Q86NR6; Q8MSV4;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase {ECO:0000303|PubMed:23369713};
DE AltName: Full=Procollagen lysyl hydroxylase {ECO:0000312|FlyBase:FBgn0036147};
DE EC=1.14.11.4 {ECO:0000250|UniProtKB:Q02809};
DE Flags: Precursor;
GN Name=Plod {ECO:0000303|PubMed:23369713, ECO:0000312|FlyBase:FBgn0036147};
GN ORFNames=CG6199 {ECO:0000312|FlyBase:FBgn0036147};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAO41443.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO41443.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAO41443.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAM49928.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 440-721.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=20888931; DOI=10.1016/j.gep.2010.09.006;
RA Bunt S., Denholm B., Skaer H.;
RT "Characterisation of the Drosophila procollagen lysyl hydroxylase, dPlod.";
RL Gene Expr. Patterns 11:72-78(2011).
RN [6] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-75.
RX PubMed=23369713; DOI=10.1016/j.devcel.2012.12.005;
RA Lerner D.W., McCoy D., Isabella A.J., Mahowald A.P., Gerlach G.F.,
RA Chaudhry T.A., Horne-Badovinac S.;
RT "A Rab10-dependent mechanism for polarized basement membrane secretion
RT during organ morphogenesis.";
RL Dev. Cell 24:159-168(2013).
CC -!- FUNCTION: Forms hydroxylysine residues in collagen type IV (By
CC similarity). Required for the secretion of collagen type IV (vkg) from
CC haemocytes, fat body and follicle cells (PubMed:23369713,
CC PubMed:20888931). {ECO:0000250|UniProtKB:Q20679,
CC ECO:0000269|PubMed:20888931, ECO:0000269|PubMed:23369713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-
CC lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA-
CC COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4;
CC Evidence={ECO:0000250|UniProtKB:Q02809};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q02809};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:20888931}. Secreted, extracellular space
CC {ECO:0000269|PubMed:20888931}. Note=Detected in the ER of fat body
CC cells and haemocytes. Also detected in small puncta in the
CC extracellular space, particularly in the region surrounding the
CC haemocytes. {ECO:0000269|PubMed:20888931}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis (at protein
CC level). First detected at stage 12 in the haemocytes and in the fat
CC body at stage 13 (at protein level). High levels also detected in the
CC anal pads of stage 16 embryos (at protein level).
CC {ECO:0000269|PubMed:20888931}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in follicle cells results
CC in round eggs. Collagen type IV protein vkg accumulates in the basal
CC cytoplasm of the follicle cells and is likely to cause the distended ER
CC region in the basal cytoplasm. {ECO:0000269|PubMed:23369713}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO41443.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF50079.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11883.1; -; Genomic_DNA.
DR EMBL; BT003764; AAO41443.1; ALT_FRAME; mRNA.
DR EMBL; AY118559; AAM49928.1; -; mRNA.
DR RefSeq; NP_648451.1; NM_140194.2.
DR RefSeq; NP_729687.1; NM_168452.2.
DR AlphaFoldDB; Q9VTH0; -.
DR SMR; Q9VTH0; -.
DR STRING; 7227.FBpp0075917; -.
DR GlyGen; Q9VTH0; 5 sites.
DR PaxDb; Q9VTH0; -.
DR PRIDE; Q9VTH0; -.
DR DNASU; 39265; -.
DR EnsemblMetazoa; FBtr0076187; FBpp0075917; FBgn0036147.
DR EnsemblMetazoa; FBtr0076188; FBpp0075918; FBgn0036147.
DR GeneID; 39265; -.
DR KEGG; dme:Dmel_CG6199; -.
DR UCSC; CG6199-RA; d. melanogaster.
DR CTD; 39265; -.
DR FlyBase; FBgn0036147; Plod.
DR VEuPathDB; VectorBase:FBgn0036147; -.
DR eggNOG; KOG1971; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR HOGENOM; CLU_022320_1_0_1; -.
DR InParanoid; Q9VTH0; -.
DR OMA; CTYYFSM; -.
DR OrthoDB; 194164at2759; -.
DR PhylomeDB; Q9VTH0; -.
DR Reactome; R-DME-1650814; Collagen biosynthesis and modifying enzymes.
DR SignaLink; Q9VTH0; -.
DR BioGRID-ORCS; 39265; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39265; -.
DR PRO; PR:Q9VTH0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036147; Expressed in embryonic fat body (Drosophila) and 20 other tissues.
DR ExpressionAtlas; Q9VTH0; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0050211; F:procollagen galactosyltransferase activity; IMP:FlyBase.
DR GO; GO:0033823; F:procollagen glucosyltransferase activity; IMP:FlyBase.
DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; ISS:FlyBase.
DR GO; GO:0007295; P:growth of a germarium-derived egg chamber; IMP:FlyBase.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IBA:GO_Central.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome; Secreted; Signal; Vitamin C.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..721
FT /note="Procollagen-lysine,2-oxoglutarate 5-dioxygenase"
FT /evidence="ECO:0000255"
FT /id="PRO_5015100590"
FT DOMAIN 627..721
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 650
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 652
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 702
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 712
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 75
FT /note="G->D: Forms round eggs. Intracellular vkg
FT accumulates at the basal surface of follicle cells, and vkg
FT levels are reduced in the basal membrane."
FT /evidence="ECO:0000269|PubMed:23369713"
FT CONFLICT 141
FT /note="N -> D (in Ref. 3; AAO41443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 721 AA; 82510 MW; 01208211B39C9E5A CRC64;
MRIQQSALLL LLLAVTSQGD AESNWNDKIK VFTVATEPTD GYTRYIRSAR VYDIEVTTLG
LGEEWKGGDM QKPGGGFKLN LLREAIAPYK NEPETIILFT DSYDVIITTT LDEIFEKFKE
SGAKILFSAE KYCWPDKSLA NDYPEVEGKA SRFLNSGAFI GYAPQVFALL VDPIEDTADD
QLYFTKIFLD ETKRAKLGLK LDVQSRLFQN LHGAKNDVKL KVDLESNQGV LQNVDFMTTP
SIIHGNGLSK VDLNAYGNYL ARTFNGVCLL CQENLLDLEE TNLPVISLAL MVTQPVPFFD
QFLEGIESLN YPKEKLHLLI YSNVAFHDDD IKSFVNKHAK EYATAKFALS TDELDERQGR
QLALDKARLH QSDYIFFVDA DAHIDDGEVL RELLRLNKQF VAPIFSKHKE LWSNFWGALS
EGGYYARSHD YVDIVKRELI GMFNVPHVTS IYLVKKTAFD AISFKHKEFD PDMAMCESLR
NAGIFMYASN LRIFGHLVNA DDFNTTVTRP DFYTLFSNEI DWTEKYIHPN YSLQLNESNK
IQQPCPDVYW FQIVSDAFCD DLVAIMEAHN GWSDGSNNDN RLEGGYEAVP TRDIHMKQVG
LERLYLKFLQ MFVRPLQERA FTGYFHNPPR ALMNFMVRYR PDEQPSLRPH HDSSTYTINI
AMNRAGIDYQ GGGCRFIRYN CSVTDTKKGW MLMHPGRLTH YHEGLLVTNG TRYIMISFID
P
