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Protein

UbiA prenyltransferase domain-containing protein 1

Gene

Ubiad1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosyntetic enzyme: coenzyme Q10, also named ubiquinone, plays a important antioxidant role in the cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from NOS3/eNOS-dependent oxidative stress (By similarity).By similarity

Pathwayi: menaquinone biosynthesis

This protein is involved in the pathway menaquinone biosynthesis, which is part of Quinol/quinone metabolism.
View all proteins of this organism that are known to be involved in the pathway menaquinone biosynthesis and in Quinol/quinone metabolism.

Pathwayi: ubiquinone biosynthesis

This protein is involved in the pathway ubiquinone biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway ubiquinone biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Keywords - Biological processi

Menaquinone biosynthesis, Ubiquinone biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-6806664. Metabolism of vitamin K.
UniPathwayiUPA00079.
UPA00232.

Names & Taxonomyi

Protein namesi
Recommended name:
UbiA prenyltransferase domain-containing protein 1 (EC:2.5.1.-)
Gene namesi
Name:Ubiad1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1918957. Ubiad1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei81 – 10121HelicalSequence analysisAdd
BLAST
Transmembranei132 – 15221HelicalSequence analysisAdd
BLAST
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Transmembranei186 – 20621HelicalSequence analysisAdd
BLAST
Transmembranei207 – 22721HelicalSequence analysisAdd
BLAST
Transmembranei243 – 26523HelicalSequence analysisAdd
BLAST
Transmembranei275 – 29521HelicalSequence analysisAdd
BLAST
Transmembranei313 – 33321HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 336335UbiA prenyltransferase domain-containing protein 1PRO_0000242628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9DC60.
PRIDEiQ9DC60.

PTM databases

PhosphoSiteiQ9DC60.

Expressioni

Gene expression databases

BgeeiQ9DC60.
CleanExiMM_UBIAD1.
GenevisibleiQ9DC60. MM.

Interactioni

Subunit structurei

Interacts with HMGCR and SOAT1.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000058502.

Structurei

3D structure databases

ProteinModelPortaliQ9DC60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UbiA prenyltransferase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4581. Eukaryota.
COG1575. LUCA.
GeneTreeiENSGT00390000012439.
HOGENOMiHOG000231452.
HOVERGENiHBG080284.
InParanoidiQ9DC60.
OMAiMGLFYVF.
OrthoDBiEOG7XH6Q2.
PhylomeDBiQ9DC60.
TreeFamiTF323238.

Family and domain databases

InterProiIPR000537. UbiA_prenyltransferase.
IPR026046. UBIAD1.
[Graphical view]
PfamiPF01040. UbiA. 1 hit.
[Graphical view]
PIRSFiPIRSF005355. UBIAD1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DC60-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVQAPGEK INILAGETAK VGDPQKNEWP EQDRLPERSW RHKCASYVLA
60 70 80 90 100
LRPWSFSASL TPVALGSALA YRSQGVLDPR LLLGCAVAVL AVHGAGNLVN
110 120 130 140 150
TYYDFSKGID HKKSDDRTLV DRILEPQDVV RFGVFLYTLG CVCAACLYYL
160 170 180 190 200
SALKLEHLAL IYFGGLSGSF LYTGGIGFKY VALGDLVILI TFGPLAVMFA
210 220 230 240 250
YAVQVGSLAI FPLIYAIPLA LSTEAILHSN NTRDMESDRE AGIVTLAILI
260 270 280 290 300
GPTFSYVLYN TLLFVPYLIF TILATHCSIS LALPLLTIPM AFSLERQFRS
310 320 330
QAFNKLPQRT AKLNLLLGLF YVFGIILAPA GSLPRL
Length:336
Mass (Da):36,684
Last modified:June 1, 2001 - v1
Checksum:iCD0F2F8BE013FBF0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351L → F in CAQ51620 (PubMed:19468303).Curated
Sequence conflicti35 – 351L → F in EDL14817 (Ref. 3) Curated
Sequence conflicti35 – 351L → F in AAH71203 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004550 mRNA. Translation: BAB23364.1.
AK078442 mRNA. Translation: BAC37276.2.
AL731654 Genomic DNA. Translation: CAM22523.1.
CU210865 Genomic DNA. Translation: CAQ51620.1.
CH466594 Genomic DNA. Translation: EDL14817.1.
BC015303 mRNA. Translation: AAH15303.1.
BC071203 mRNA. Translation: AAH71203.1.
CCDSiCCDS18936.1.
RefSeqiNP_082149.1. NM_027873.2.
UniGeneiMm.292503.

Genome annotation databases

EnsembliENSMUST00000051633; ENSMUSP00000058502; ENSMUSG00000047719.
GeneIDi71707.
KEGGimmu:71707.
UCSCiuc008vup.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004550 mRNA. Translation: BAB23364.1.
AK078442 mRNA. Translation: BAC37276.2.
AL731654 Genomic DNA. Translation: CAM22523.1.
CU210865 Genomic DNA. Translation: CAQ51620.1.
CH466594 Genomic DNA. Translation: EDL14817.1.
BC015303 mRNA. Translation: AAH15303.1.
BC071203 mRNA. Translation: AAH71203.1.
CCDSiCCDS18936.1.
RefSeqiNP_082149.1. NM_027873.2.
UniGeneiMm.292503.

3D structure databases

ProteinModelPortaliQ9DC60.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000058502.

PTM databases

PhosphoSiteiQ9DC60.

Proteomic databases

PaxDbiQ9DC60.
PRIDEiQ9DC60.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000051633; ENSMUSP00000058502; ENSMUSG00000047719.
GeneIDi71707.
KEGGimmu:71707.
UCSCiuc008vup.1. mouse.

Organism-specific databases

CTDi29914.
MGIiMGI:1918957. Ubiad1.

Phylogenomic databases

eggNOGiKOG4581. Eukaryota.
COG1575. LUCA.
GeneTreeiENSGT00390000012439.
HOGENOMiHOG000231452.
HOVERGENiHBG080284.
InParanoidiQ9DC60.
OMAiMGLFYVF.
OrthoDBiEOG7XH6Q2.
PhylomeDBiQ9DC60.
TreeFamiTF323238.

Enzyme and pathway databases

UniPathwayiUPA00079.
UPA00232.
ReactomeiR-MMU-6806664. Metabolism of vitamin K.

Miscellaneous databases

ChiTaRSiUbiad1. mouse.
NextBioi334283.
PROiQ9DC60.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DC60.
CleanExiMM_UBIAD1.
GenevisibleiQ9DC60. MM.

Family and domain databases

InterProiIPR000537. UbiA_prenyltransferase.
IPR026046. UBIAD1.
[Graphical view]
PfamiPF01040. UbiA. 1 hit.
[Graphical view]
PIRSFiPIRSF005355. UBIAD1. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung and Wolffian duct.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney and Mammary gland.

Entry informationi

Entry nameiUBIA1_MOUSE
AccessioniPrimary (citable) accession number: Q9DC60
Secondary accession number(s): A2AH70
, B2KFZ5, Q6IR30, Q8BJX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.