ID   UBIA1_RAT               Reviewed;         338 AA.
AC   D3ZG27;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=UbiA prenyltransferase domain-containing protein 1;
DE            EC=2.5.1.-;
GN   Name=Ubiad1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Prenyltransferase that mediates the formation of menaquinone-
CC       4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform required for
CC       endothelial cell development. Mediates the conversion of phylloquinone
CC       (PK) into MK-4, probably by cleaving the side chain of phylloquinone
CC       (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then
CC       prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4.
CC       Also plays a role in cardiovascular development independently of MK-4
CC       biosynthesis, by acting as a coenzyme Q10 biosynthetic enzyme: coenzyme
CC       Q10, also named ubiquinone, plays an important antioxidant role in the
CC       cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the
CC       Golgi membrane, leading to protect cardiovascular tissues from
CC       NOS3/eNOS-dependent oxidative stress (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC   -!- SUBUNIT: Interacts with HMGCR and SOAT1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Mitochondrion
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CH473968; EDL81120.1; -; Genomic_DNA.
DR   RefSeq; NP_001101463.1; NM_001107993.1.
DR   AlphaFoldDB; D3ZG27; -.
DR   SMR; D3ZG27; -.
DR   STRING; 10116.ENSRNOP00000012691; -.
DR   iPTMnet; D3ZG27; -.
DR   PhosphoSitePlus; D3ZG27; -.
DR   PaxDb; D3ZG27; -.
DR   Ensembl; ENSRNOT00000012692; ENSRNOP00000012691; ENSRNOG00000009575.
DR   GeneID; 313706; -.
DR   KEGG; rno:313706; -.
DR   CTD; 29914; -.
DR   RGD; 1309588; Ubiad1.
DR   eggNOG; KOG4581; Eukaryota.
DR   GeneTree; ENSGT00390000012439; -.
DR   HOGENOM; CLU_043611_0_0_1; -.
DR   InParanoid; D3ZG27; -.
DR   OMA; QWIEGAR; -.
DR   OrthoDB; 1146311at2759; -.
DR   PhylomeDB; D3ZG27; -.
DR   TreeFam; TF323238; -.
DR   Reactome; R-RNO-6806664; Metabolism of vitamin K.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA00232; -.
DR   PRO; PR:D3ZG27; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Proteomes; UP000234681; Chromosome 5.
DR   Bgee; ENSRNOG00000009575; Expressed in skeletal muscle tissue and 18 other tissues.
DR   Genevisible; D3ZG27; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0016209; F:antioxidant activity; ISS:UniProtKB.
DR   GO; GO:0004659; F:prenyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0072359; P:circulatory system development; ISS:UniProtKB.
DR   GO; GO:0001885; P:endothelial cell development; ISS:UniProtKB.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:UniProtKB.
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; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Acetylation; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW   Menaquinone biosynthesis; Mitochondrion; Prenyltransferase;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Ubiquinone biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5Z9"
FT   CHAIN           2..338
FT                   /note="UbiA prenyltransferase domain-containing protein 1"
FT                   /id="PRO_0000403783"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5Z9"
SQ   SEQUENCE   338 AA;  37026 MW;  CE818C5C7CD3DF9C CRC64;
     MAAVQAPGEK INIQAGETTQ VGDTDQQRND WPEEDRLPER SWRQKCASYV LALRPWSFSA
     SLTPVALGSA LAYRSQGVLD PRLLLGCAVA VLAVHGAGNL VNTYYDFSKG IDHKKSDDRT
     LVDRILEPQD VVRFGVFLYT LGCVCAAYLY YLSTLKLEHL ALIYFGGLSG SFLYTGGIGF
     KYVALGDLVI LITFGPLAVM FAYAVQVGSL AIFPLVYAIP LALSTEAILH SNNTRDMESD
     REAGIVTLAI LIGPTLSYIL YNTLLFLPYL IFTILATHCS ISLALPLLTS PMAFSLERQF
     RSQAFNKLPQ RTAKLNLLLG LFYVFGIILA PAGSLPRL