UBIA1_DROME
ID UBIA1_DROME Reviewed; 359 AA.
AC Q9V3R8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=UbiA prenyltransferase domain-containing protein 1 homolog;
DE EC=2.5.1.-;
DE AltName: Full=Protein heixuedian;
GN Name=heix; ORFNames=CG5876;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA McGarvey T.W., Malkowicz S.B.;
RT "Full length sequencing of the BI357486/BI234095 clone containing the open
RT reading frame and 3' end of Drosophila heix.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22582012; DOI=10.1126/science.1218632;
RA Vos M., Esposito G., Edirisinghe J.N., Vilain S., Haddad D.M.,
RA Slabbaert J.R., Van Meensel S., Schaap O., De Strooper B., Meganathan R.,
RA Morais V.A., Verstreken P.;
RT "Vitamin K2 is a mitochondrial electron carrier that rescues pink1
RT deficiency.";
RL Science 336:1306-1310(2012).
CC -!- FUNCTION: Prenyltransferase that mediates the formation of menaquinone-
CC 4 (MK-4), a vitamin K2 isoform, thereby acting as a mitochondrial
CC electron carrier. Mediates the conversion of phylloquinone (PK) into
CC MK-4, probably by cleaving the side chain of phylloquinone (PK) to
CC release 2-methyl-1,4-naphthoquinone (menadione; K3) and then
CC prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4.
CC MK-4 acts as a membrane electron carrier downstream of a electron
CC transport chain complex, improving mitochondrial oxygen consumption.
CC {ECO:0000269|PubMed:22582012}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:22582012}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22582012}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF440356; AAL34085.1; -; mRNA.
DR EMBL; AE014134; AAF53515.1; -; Genomic_DNA.
DR EMBL; AY061093; AAL28641.1; -; mRNA.
DR RefSeq; NP_523581.1; NM_078857.4.
DR AlphaFoldDB; Q9V3R8; -.
DR SMR; Q9V3R8; -.
DR BioGRID; 60972; 6.
DR IntAct; Q9V3R8; 11.
DR STRING; 7227.FBpp0080409; -.
DR PaxDb; Q9V3R8; -.
DR PRIDE; Q9V3R8; -.
DR DNASU; 34961; -.
DR EnsemblMetazoa; FBtr0080852; FBpp0080409; FBgn0028375.
DR GeneID; 34961; -.
DR KEGG; dme:Dmel_CG5876; -.
DR UCSC; CG5876-RA; d. melanogaster.
DR CTD; 34961; -.
DR FlyBase; FBgn0028375; heix.
DR VEuPathDB; VectorBase:FBgn0028375; -.
DR eggNOG; KOG4581; Eukaryota.
DR GeneTree; ENSGT00390000012439; -.
DR HOGENOM; CLU_043611_0_0_1; -.
DR InParanoid; Q9V3R8; -.
DR OMA; QWIEGAR; -.
DR OrthoDB; 1146311at2759; -.
DR PhylomeDB; Q9V3R8; -.
DR Reactome; R-DME-6806664; Metabolism of vitamin K.
DR UniPathway; UPA00079; -.
DR BioGRID-ORCS; 34961; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 34961; -.
DR PRO; PR:Q9V3R8; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0028375; Expressed in cleaving embryo and 22 other tissues.
DR Genevisible; Q9V3R8; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IMP:FlyBase.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:FlyBase.
DR GO; GO:0045611; P:negative regulation of hemocyte differentiation; IMP:FlyBase.
DR GO; GO:0035207; P:negative regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0035204; P:negative regulation of lamellocyte differentiation; IMP:FlyBase.
DR GO; GO:0032194; P:ubiquinone biosynthetic process via 3,4-dihydroxy-5-polyprenylbenzoate; IBA:GO_Central.
DR GO; GO:0042371; P:vitamin K biosynthetic process; IBA:GO_Central.
DR CDD; cd13962; PT_UbiA_UBIAD1; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR InterPro; IPR026046; UBIAD1.
DR PANTHER; PTHR13929; PTHR13929; 1.
DR Pfam; PF01040; UbiA; 1.
DR PIRSF; PIRSF005355; UBIAD1; 1.
PE 2: Evidence at transcript level;
KW Membrane; Menaquinone biosynthesis; Mitochondrion; Prenyltransferase;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="UbiA prenyltransferase domain-containing protein 1
FT homolog"
FT /id="PRO_0000242631"
FT TRANSMEM 67..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 39216 MW; 7D707D1E85CE18A3 CRC64;
MATSSQLLPN GNLSRNGKTK TEDGEEVEAV VGARAAGADA GVALTGRLTG HPSTSGTFMK
LKTYLLALRP WSLSASLVPT LLGSALAYRS QWAEEFSLAT FFLTAFTVVT VHCAGNVVNT
YFDFIKGIDK QKADDRTLVD HILTKDEVVS LGAILYMAGC GGFVLLAVLS PAKMEHLALI
YFGGLSSSFL YTGGIGFKYI ALGDLVILIL FGPISVLFAF MSQTGHLDWT TMGYAIPLAL
NTEAILHSNN TRDADNDRRA GIVTLAILIG RTASHVLYAM LLFAPYSLFF IFGLKYSLWF
LLPLVTLPQA FQIEKRFRNE QTMHLVPRQT AKLNFFFGIL YVVACCCAHQ LPTFGLRRN
