UBIA1_AILME
ID UBIA1_AILME Reviewed; 337 AA.
AC D2HKB0;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=UbiA prenyltransferase domain-containing protein 1;
DE EC=2.5.1.-;
GN Name=UBIAD1; ORFNames=PANDA_011808;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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; GL192942; EFB24843.1; -; Genomic_DNA.
DR RefSeq; XP_002922794.1; XM_002922748.3.
DR AlphaFoldDB; D2HKB0; -.
DR SMR; D2HKB0; -.
DR STRING; 9646.ENSAMEP00000010146; -.
DR Ensembl; ENSAMET00000046470; ENSAMEP00000023886; ENSAMEG00000023578.
DR GeneID; 100467850; -.
DR KEGG; aml:100467850; -.
DR CTD; 29914; -.
DR eggNOG; KOG4581; Eukaryota.
DR GeneTree; ENSGT00390000012439; -.
DR HOGENOM; CLU_043611_0_0_1; -.
DR InParanoid; D2HKB0; -.
DR OMA; QWIEGAR; -.
DR OrthoDB; 1146311at2759; -.
DR TreeFam; TF323238; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
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: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..337
FT /note="UbiA prenyltransferase domain-containing protein 1"
FT /id="PRO_0000403782"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Z9"
SQ SEQUENCE 337 AA; 36535 MW; 922055AFF4AB9A1A CRC64;
MAASQVPGEI NIQAGETAKS GDRDLLGNDC RDQDRLPQRS WRQKCASYVL ALRPWSFSAS
LTPVALGSAL AYRSQGVLDP RLLVGCAVAV LAVHGAGNLV NTYYDFSKGI DHKKSDDRTL
VDRILEPQDV VLFGVFLYTL GCVCAACLYC LSPLKLEHLA LIYFGGLSGS FLYTGGIGFK
YVALGDLVIL ITFGPLAVMF AYAVQVGSLA VFPLVYAIPL ALSTEAVLHS NNTRDMESDR
EAGIVTLAIL IGPTLSYVLY NTLLFLPYLI FSILATHCSI SLALPLLTVP MAFSLERQFR
SQTFNKLPQR TAKLNLLLGL FYVFGIILAP AGSLPKL
