UBIA1_MOUSE
ID UBIA1_MOUSE Reviewed; 336 AA.
AC Q9DC60; A2AH70; B2KFZ5; Q6IR30; Q8BJX7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=UbiA prenyltransferase domain-containing protein 1;
DE EC=2.5.1.-;
GN Name=Ubiad1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
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 EMBL; AK004550; BAB23364.1; -; mRNA.
DR EMBL; AK078442; BAC37276.2; -; mRNA.
DR EMBL; AL731654; CAM22523.1; -; Genomic_DNA.
DR EMBL; CU210865; CAQ51620.1; -; Genomic_DNA.
DR EMBL; CH466594; EDL14817.1; -; Genomic_DNA.
DR EMBL; BC015303; AAH15303.1; -; mRNA.
DR EMBL; BC071203; AAH71203.1; -; mRNA.
DR CCDS; CCDS18936.1; -.
DR RefSeq; NP_082149.1; NM_027873.2.
DR AlphaFoldDB; Q9DC60; -.
DR SMR; Q9DC60; -.
DR STRING; 10090.ENSMUSP00000058502; -.
DR iPTMnet; Q9DC60; -.
DR PhosphoSitePlus; Q9DC60; -.
DR MaxQB; Q9DC60; -.
DR PaxDb; Q9DC60; -.
DR PRIDE; Q9DC60; -.
DR ProteomicsDB; 298089; -.
DR Antibodypedia; 13750; 121 antibodies from 24 providers.
DR Ensembl; ENSMUST00000051633; ENSMUSP00000058502; ENSMUSG00000047719.
DR GeneID; 71707; -.
DR KEGG; mmu:71707; -.
DR UCSC; uc008vup.1; mouse.
DR CTD; 29914; -.
DR MGI; MGI:1918957; Ubiad1.
DR VEuPathDB; HostDB:ENSMUSG00000047719; -.
DR eggNOG; KOG4581; Eukaryota.
DR GeneTree; ENSGT00390000012439; -.
DR HOGENOM; CLU_043611_0_0_1; -.
DR InParanoid; Q9DC60; -.
DR OMA; QWIEGAR; -.
DR OrthoDB; 1146311at2759; -.
DR PhylomeDB; Q9DC60; -.
DR TreeFam; TF323238; -.
DR Reactome; R-MMU-6806664; Metabolism of vitamin K.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 71707; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Ubiad1; mouse.
DR PRO; PR:Q9DC60; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9DC60; protein.
DR Bgee; ENSMUSG00000047719; Expressed in animal zygote and 209 other tissues.
DR Genevisible; Q9DC60; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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 2: Evidence at transcript level;
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..336
FT /note="UbiA prenyltransferase domain-containing protein 1"
FT /id="PRO_0000242628"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Z9"
FT CONFLICT 35
FT /note="L -> F (in Ref. 2; CAQ51620, 3; EDL14817 and 4;
FT AAH71203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 36684 MW; CD0F2F8BE013FBF0 CRC64;
MAAVQAPGEK INILAGETAK VGDPQKNEWP EQDRLPERSW RHKCASYVLA LRPWSFSASL
TPVALGSALA YRSQGVLDPR LLLGCAVAVL AVHGAGNLVN TYYDFSKGID HKKSDDRTLV
DRILEPQDVV RFGVFLYTLG CVCAACLYYL SALKLEHLAL IYFGGLSGSF LYTGGIGFKY
VALGDLVILI TFGPLAVMFA YAVQVGSLAI FPLIYAIPLA LSTEAILHSN NTRDMESDRE
AGIVTLAILI GPTFSYVLYN TLLFVPYLIF TILATHCSIS LALPLLTIPM AFSLERQFRS
QAFNKLPQRT AKLNLLLGLF YVFGIILAPA GSLPRL
