ID UBIA1_HUMAN Reviewed; 338 AA. AC Q9Y5Z9; B3KQG3; Q53GX3; Q5THD4; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 170. DE RecName: Full=UbiA prenyltransferase domain-containing protein 1; DE EC=2.5.1.- {ECO:0000269|PubMed:20953171}; DE EC=2.5.1.39 {ECO:0000305|PubMed:23374346}; DE AltName: Full=Transitional epithelial response protein 1 {ECO:0000303|PubMed:11314041}; GN Name=UBIAD1 {ECO:0000303|PubMed:20953171, GN ECO:0000312|HGNC:HGNC:30791}; GN Synonyms=TERE1 {ECO:0000303|PubMed:11314041}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RC TISSUE=Spleen; RX PubMed=11314041; DOI=10.1038/sj.onc.1204143; RA McGarvey T.W., Nguyen T., Tomaszewski J.E., Monson F.C., Malkowicz S.B.; RT "Isolation and characterization of the TERE1 gene, a gene down-regulated in RT transitional cell carcinoma of the bladder."; RL Oncogene 20:1042-1051(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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). RN [8] RP INVOLVEMENT IN CARCINOMA, AND SUBCELLULAR LOCATION. RX PubMed=12497587; DOI=10.1002/pros.10174; RA McGarvey T.W., Nguyen T., Puthiyaveettil R., Tomaszewski J.E., RA Malkowicz S.B.; RT "TERE1, a novel gene affecting growth regulation in prostate carcinoma."; RL Prostate 54:144-155(2003). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION. RX PubMed=20953171; DOI=10.1038/nature09464; RA Nakagawa K., Hirota Y., Sawada N., Yuge N., Watanabe M., Uchino Y., RA Okuda N., Shimomura Y., Suhara Y., Okano T.; RT "Identification of UBIAD1 as a novel human menaquinone-4 biosynthetic RT enzyme."; RL Nature 468:117-121(2010). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF RP VARIANTS SCCD SER-102 AND GLY-112. RX PubMed=23374346; DOI=10.1016/j.cell.2013.01.013; RA Mugoni V., Postel R., Catanzaro V., De Luca E., Turco E., Digilio G., RA Silengo L., Murphy M.P., Medana C., Stainier D.Y., Bakkers J., RA Santoro M.M.; RT "Ubiad1 is an antioxidant enzyme that regulates eNOS activity by CoQ10 RT synthesis."; RL Cell 152:504-518(2013). RN [13] RP VARIANTS SCCD SER-102 AND ARG-177. RX PubMed=17962451; DOI=10.1167/iovs.07-0845; RA Weiss J.S., Kruth H.S., Kuivaniemi H., Tromp G., White P.S., Winters R.S., RA Lisch W., Henn W., Denninger E., Krause M., Wasson P., Ebenezer N., RA Mahurkar S., Nickerson M.L.; RT "Mutations in the UBIAD1 gene on chromosome short arm 1, region 36, cause RT Schnyder crystalline corneal dystrophy."; RL Invest. Ophthalmol. Vis. Sci. 48:5007-5012(2007). RN [14] RP VARIANTS SCCD SER-102; GLY-112; GLY-119; ILE-175 AND SER-232, AND VARIANT RP PHE-75. RX PubMed=17668063; DOI=10.1371/journal.pone.0000685; RA Orr A., Dube M.-P., Marcadier J., Jiang H., Federico A., George S., RA Seamone C., Andrews D., Dubord P., Holland S., Provost S., Mongrain V., RA Evans S., Higgins B., Bowman S., Guernsey D., Samuels M.; RT "Mutations in the UBIAD1 gene, encoding a potential prenyltransferase, are RT causal for Schnyder crystalline corneal dystrophy."; RL PLoS ONE 2:E685-E685(2007). RN [15] RP VARIANTS SCCD SER-102; GLY-118; PHE-121; PRO-171; ILE-175; ARG-177; ARG-186 RP AND GLU-236. RX PubMed=18176953; DOI=10.1002/ajmg.a.32201; RA Weiss J.S., Kruth H.S., Kuivaniemi H., Tromp G., Karkera J., Mahurkar S., RA Lisch W., Dupps W.J. Jr., White P.S., Winters R.S., Kim C., Rapuano C.J., RA Sutphin J., Reidy J., Hu F.-R., Lu da W., Ebenezer N., Nickerson M.L.; RT "Genetic analysis of 14 families with Schnyder crystalline corneal RT dystrophy reveals clues to UBIAD1 protein function."; RL Am. J. Med. Genet. A 146:271-283(2008). RN [16] RP VARIANT SCCD PRO-171. RX PubMed=19429578; DOI=10.1136/bjo.2008.152140; RA Mehta J.S., Vithana E.N., Venkataraman D., Venkatraman A., Yong V.H., RA Aung T., Tan D.T.; RT "Surgical management and genetic analysis of a Chinese family with the RT S171P mutation in the UBIAD1 gene, the gene for Schnyder corneal RT dystrophy."; RL Br. J. Ophthalmol. 93:926-931(2009). RN [17] RP VARIANT SCCD SER-98. RX PubMed=19649163; RA Jing Y., Liu C., Xu J., Wang L.; RT "A novel UBIAD1 mutation identified in a Chinese family with Schnyder RT crystalline corneal dystrophy."; RL Mol. Vis. 15:1463-1469(2009). RN [18] RP VARIANT SCCD ASN-240. RX PubMed=20489584; DOI=10.1097/ico.0b013e3181c84bcf; RA Weiss J.S., Wiaux C., Yellore V., Raber I., Eagle R., Mequio M., Aldave A.; RT "Newly reported p.Asp240Asn mutation in UBIAD1 suggests central discoid RT corneal dystrophy is a variant of Schnyder corneal dystrophy."; RL Cornea 29:777-780(2010). RN [19] RP VARIANTS SCCD THR-97; SER-102; ASN-112; GLY-122; GLU-122 AND HIS-188, AND RP SUBCELLULAR LOCATION. RX PubMed=20505825; DOI=10.1371/journal.pone.0010760; RA Nickerson M.L., Kostiha B.N., Brandt W., Fredericks W., Xu K.P., Yu F.S., RA Gold B., Chodosh J., Goldberg M., Lu da W., Yamada M., Tervo T.M., RA Grutzmacher R., Croasdale C., Hoeltzenbein M., Sutphin J., Malkowicz S.B., RA Wessjohann L., Kruth H.S., Dean M., Weiss J.S.; RT "UBIAD1 mutation alters a mitochondrial prenyltransferase to cause Schnyder RT corneal dystrophy."; RL PLoS ONE 5:E10760-E10760(2010). RN [20] RP VARIANT GLU-177, CHARACTERIZATION OF VARIANTS SCCD SER-102; ASN-112; RP GLU-177 AND ARG-177, AND INTERACTION WITH HMGCR AND SOAT1. RX PubMed=23169578; DOI=10.1002/humu.22230; RA Nickerson M.L., Bosley A.D., Weiss J.S., Kostiha B.N., Hirota Y., RA Brandt W., Esposito D., Kinoshita S., Wessjohann L., Morham S.G., RA Andresson T., Kruth H.S., Okano T., Dean M.; RT "The UBIAD1 prenyltransferase links menaquione-4 synthesis to cholesterol RT metabolic enzymes."; RL Hum. Mutat. 34:317-329(2013). CC -!- FUNCTION: Prenyltransferase that mediates the formation of menaquinone- CC 4 (MK-4) and coenzyme Q10 (PubMed:20953171, PubMed:23374346). MK-4 is a CC vitamin K2 isoform present at high concentrations in the brain, kidney CC and pancreas, and is required for endothelial cell development CC (PubMed:20953171). 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 (PubMed:20953171). Also plays a role in cardiovascular development CC independently of MK-4 biosynthesis, by acting as a coenzyme Q10 CC biosynthetic enzyme: coenzyme Q10, also named ubiquinone, plays an CC important antioxidant role in the cardiovascular system CC (PubMed:23374346). Mediates biosynthesis of coenzyme Q10 in the Golgi CC membrane, leading to protect cardiovascular tissues from NOS3/eNOS- CC dependent oxidative stress (PubMed:23374346). CC {ECO:0000269|PubMed:20953171, ECO:0000269|PubMed:23374346}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + menadiol = CC diphosphate + menaquinol-4; Xref=Rhea:RHEA:74083, ChEBI:CHEBI:6746, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:193091; CC Evidence={ECO:0000269|PubMed:20953171}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74084; CC Evidence={ECO:0000269|PubMed:20953171}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-hydroxybenzoate + all-trans-decaprenyl diphosphate = 4- CC hydroxy-3-all-trans-decaprenylbenzoate + diphosphate; CC Xref=Rhea:RHEA:44564, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:60721, ChEBI:CHEBI:84503; EC=2.5.1.39; CC Evidence={ECO:0000305|PubMed:23374346}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44565; CC Evidence={ECO:0000305|PubMed:23374346}; CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000269|PubMed:20953171}. CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000269|PubMed:20953171}. CC -!- SUBUNIT: Interacts with HMGCR and SOAT1. {ECO:0000269|PubMed:23169578}. CC -!- INTERACTION: CC Q9Y5Z9; Q8IVF2-3: AHNAK2; NbExp=3; IntAct=EBI-2819725, EBI-12078468; CC Q9Y5Z9; P07307-3: ASGR2; NbExp=3; IntAct=EBI-2819725, EBI-12808270; CC Q9Y5Z9; Q13323: BIK; NbExp=3; IntAct=EBI-2819725, EBI-700794; CC Q9Y5Z9; P20138: CD33; NbExp=3; IntAct=EBI-2819725, EBI-3906571; CC Q9Y5Z9; P19397: CD53; NbExp=3; IntAct=EBI-2819725, EBI-6657396; CC Q9Y5Z9; P11912: CD79A; NbExp=3; IntAct=EBI-2819725, EBI-7797864; CC Q9Y5Z9; O95471: CLDN7; NbExp=3; IntAct=EBI-2819725, EBI-740744; CC Q9Y5Z9; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-2819725, EBI-18013275; CC Q9Y5Z9; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-2819725, EBI-17233035; CC Q9Y5Z9; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2819725, EBI-6942903; CC Q9Y5Z9; P00387: CYB5R3; NbExp=3; IntAct=EBI-2819725, EBI-1046040; CC Q9Y5Z9; Q15125: EBP; NbExp=3; IntAct=EBI-2819725, EBI-3915253; CC Q9Y5Z9; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2819725, EBI-781551; CC Q9Y5Z9; P22794: EVI2A; NbExp=3; IntAct=EBI-2819725, EBI-2870359; CC Q9Y5Z9; P34910-2: EVI2B; NbExp=3; IntAct=EBI-2819725, EBI-17640610; CC Q9Y5Z9; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2819725, EBI-18304435; CC Q9Y5Z9; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-2819725, EBI-3918971; CC Q9Y5Z9; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-2819725, EBI-12142257; CC Q9Y5Z9; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2819725, EBI-13345167; CC Q9Y5Z9; P31937: HIBADH; NbExp=3; IntAct=EBI-2819725, EBI-11427100; CC Q9Y5Z9; P04035: HMGCR; NbExp=3; IntAct=EBI-2819725, EBI-465513; CC Q9Y5Z9; P01112: HRAS; NbExp=9; IntAct=EBI-2819725, EBI-350145; CC Q9Y5Z9; P48051: KCNJ6; NbExp=3; IntAct=EBI-2819725, EBI-12017638; CC Q9Y5Z9; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-2819725, EBI-2820517; CC Q9Y5Z9; O14880: MGST3; NbExp=3; IntAct=EBI-2819725, EBI-724754; CC Q9Y5Z9; Q9HC36: MRM3; NbExp=3; IntAct=EBI-2819725, EBI-1045440; CC Q9Y5Z9; Q6IBW4-4: NCAPH2; NbExp=3; IntAct=EBI-2819725, EBI-10247000; CC Q9Y5Z9; Q96KR7: PHACTR3; NbExp=3; IntAct=EBI-2819725, EBI-717068; CC Q9Y5Z9; P57054: PIGP; NbExp=3; IntAct=EBI-2819725, EBI-17630288; CC Q9Y5Z9; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-2819725, EBI-7545592; CC Q9Y5Z9; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-2819725, EBI-10192441; CC Q9Y5Z9; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-2819725, EBI-3920694; CC Q9Y5Z9; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-2819725, EBI-17247926; CC Q9Y5Z9; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-2819725, EBI-5235586; CC Q9Y5Z9; P35610: SOAT1; NbExp=2; IntAct=EBI-2819725, EBI-6621955; CC Q9Y5Z9; P35610-1: SOAT1; NbExp=3; IntAct=EBI-2819725, EBI-6621997; CC Q9Y5Z9; P21579: SYT1; NbExp=3; IntAct=EBI-2819725, EBI-524909; CC Q9Y5Z9; Q9UIK5: TMEFF2; NbExp=3; IntAct=EBI-2819725, EBI-11423693; CC Q9Y5Z9; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-2819725, EBI-7238458; CC Q9Y5Z9; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2819725, EBI-8638294; CC Q9Y5Z9-1; P04035: HMGCR; NbExp=5; IntAct=EBI-6621921, EBI-465513; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:20953171}; Multi-pass membrane protein CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:23374346}; CC Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane CC {ECO:0000269|PubMed:20505825}; Multi-pass membrane protein CC {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:11314041}. Nucleus CC {ECO:0000269|PubMed:11314041, ECO:0000269|PubMed:12497587}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y5Z9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y5Z9-2; Sequence=VSP_019455, VSP_019456; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:11314041}. CC -!- DISEASE: Corneal dystrophy, Schnyder type (SCCD) [MIM:121800]: A form CC of stromal corneal dystrophy characterized by corneal clouding, CC resulting from abnormal deposition of cholesterol and phospholipids, CC and decreased visual acuity. Typically, ring-shaped yellow-white CC opacities composed of innumerable fine needle-shaped crystals form in CC Bowman layer and the adjacent anterior stroma of the central cornea. CC The crystals usually remain in the anterior third of the cornea. The CC corneal epithelium and endothelium as well as Descemet membrane are CC spared. {ECO:0000269|PubMed:17668063, ECO:0000269|PubMed:17962451, CC ECO:0000269|PubMed:18176953, ECO:0000269|PubMed:19429578, CC ECO:0000269|PubMed:19649163, ECO:0000269|PubMed:20489584, CC ECO:0000269|PubMed:20505825, ECO:0000269|PubMed:23169578, CC ECO:0000269|PubMed:23374346}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Strongly down-regulated in transitional cell carcinoma CC of the bladder and in prostate carcinoma (at protein level) CC (PubMed:11314041, PubMed:12497587). {ECO:0000305|PubMed:11314041, CC ECO:0000305|PubMed:12497587}. 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; AF117064; AAD27581.1; -; mRNA. DR EMBL; BT006832; AAP35478.1; -; mRNA. DR EMBL; AK222808; BAD96528.1; -; mRNA. DR EMBL; AK074890; BAG52025.1; -; mRNA. DR EMBL; AL031291; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471130; EAW71686.1; -; Genomic_DNA. DR EMBL; BC004468; AAH04468.1; -; mRNA. DR CCDS; CCDS129.1; -. [Q9Y5Z9-1] DR CCDS; CCDS81260.1; -. [Q9Y5Z9-2] DR RefSeq; NP_001317279.1; NM_001330350.1. [Q9Y5Z9-2] DR RefSeq; NP_037451.1; NM_013319.2. [Q9Y5Z9-1] DR AlphaFoldDB; Q9Y5Z9; -. DR SMR; Q9Y5Z9; -. DR BioGRID; 118958; 115. DR IntAct; Q9Y5Z9; 59. DR MINT; Q9Y5Z9; -. DR STRING; 9606.ENSP00000366006; -. DR DrugBank; DB01022; Phylloquinone. DR iPTMnet; Q9Y5Z9; -. DR PhosphoSitePlus; Q9Y5Z9; -. DR SwissPalm; Q9Y5Z9; -. DR BioMuta; UBIAD1; -. DR DMDM; 74753514; -. DR EPD; Q9Y5Z9; -. DR jPOST; Q9Y5Z9; -. DR MassIVE; Q9Y5Z9; -. DR MaxQB; Q9Y5Z9; -. DR PaxDb; 9606-ENSP00000366006; -. DR PeptideAtlas; Q9Y5Z9; -. DR ProteomicsDB; 86555; -. [Q9Y5Z9-1] DR ProteomicsDB; 86556; -. [Q9Y5Z9-2] DR Pumba; Q9Y5Z9; -. DR Antibodypedia; 13750; 149 antibodies from 24 providers. DR DNASU; 29914; -. DR Ensembl; ENST00000376804.2; ENSP00000366000.1; ENSG00000120942.14. [Q9Y5Z9-2] DR Ensembl; ENST00000376810.6; ENSP00000366006.5; ENSG00000120942.14. [Q9Y5Z9-1] DR GeneID; 29914; -. DR KEGG; hsa:29914; -. DR MANE-Select; ENST00000376810.6; ENSP00000366006.5; NM_013319.3; NP_037451.1. DR UCSC; uc001asg.4; human. [Q9Y5Z9-1] DR AGR; HGNC:30791; -. DR CTD; 29914; -. DR DisGeNET; 29914; -. DR GeneCards; UBIAD1; -. DR HGNC; HGNC:30791; UBIAD1. DR HPA; ENSG00000120942; Low tissue specificity. DR MalaCards; UBIAD1; -. DR MIM; 121800; phenotype. DR MIM; 611632; gene. DR neXtProt; NX_Q9Y5Z9; -. DR OpenTargets; ENSG00000120942; -. DR Orphanet; 98967; Schnyder corneal dystrophy. DR PharmGKB; PA142670660; -. DR VEuPathDB; HostDB:ENSG00000120942; -. DR eggNOG; KOG4581; Eukaryota. DR GeneTree; ENSGT00390000012439; -. DR HOGENOM; CLU_043611_0_0_1; -. DR InParanoid; Q9Y5Z9; -. DR OMA; QWIEGAR; -. DR OrthoDB; 5490123at2759; -. DR PhylomeDB; Q9Y5Z9; -. DR TreeFam; TF323238; -. DR BioCyc; MetaCyc:ENSG00000120942-MONOMER; -. DR PathwayCommons; Q9Y5Z9; -. DR Reactome; R-HSA-6806664; Metabolism of vitamin K. DR SignaLink; Q9Y5Z9; -. DR SIGNOR; Q9Y5Z9; -. DR UniPathway; UPA00079; -. DR UniPathway; UPA00232; -. DR BioGRID-ORCS; 29914; 185 hits in 1166 CRISPR screens. DR ChiTaRS; UBIAD1; human. DR GeneWiki; UBIAD1; -. DR GenomeRNAi; 29914; -. DR Pharos; Q9Y5Z9; Tbio. DR PRO; PR:Q9Y5Z9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y5Z9; Protein. DR Bgee; ENSG00000120942; Expressed in gastrocnemius and 164 other cell types or tissues. DR ExpressionAtlas; Q9Y5Z9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; IEA:RHEA. DR GO; GO:0016209; F:antioxidant activity; IMP:UniProtKB. DR GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB. DR GO; GO:0009234; P:menaquinone biosynthetic process; IMP:UniProtKB. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP: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; IDA:UniProtKB. DR GO; GO:0042373; P:vitamin K metabolic process; TAS:Reactome. DR CDD; cd13962; PT_UbiA_UBIAD1; 1. DR Gene3D; 1.10.357.140; UbiA prenyltransferase; 1. DR InterPro; IPR000537; UbiA_prenyltransferase. DR InterPro; IPR044878; UbiA_sf. DR InterPro; IPR026046; UBIAD1. DR PANTHER; PTHR13929; 1,4-DIHYDROXY-2-NAPHTHOATE OCTAPRENYLTRANSFERASE; 1. DR PANTHER; PTHR13929:SF0; UBIA PRENYLTRANSFERASE DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF01040; UbiA; 1. DR PIRSF; PIRSF005355; UBIAD1; 1. DR Genevisible; Q9Y5Z9; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Corneal dystrophy; Cytoplasm; KW Disease variant; Endoplasmic reticulum; Golgi apparatus; Membrane; KW Menaquinone biosynthesis; Mitochondrion; Nucleus; Prenyltransferase; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix; KW Ubiquinone biosynthesis. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT CHAIN 2..338 FT /note="UbiA prenyltransferase domain-containing protein 1" FT /id="PRO_0000242627" 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 MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT VAR_SEQ 177..179 FT /note="GIG -> VLI (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_019455" FT VAR_SEQ 180..338 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_019456" FT VARIANT 75 FT /note="S -> F (in dbSNP:rs114000606)" FT /evidence="ECO:0000269|PubMed:17668063" FT /id="VAR_043713" FT VARIANT 97 FT /note="A -> T (in SCCD)" FT /evidence="ECO:0000269|PubMed:20505825" FT /id="VAR_064337" FT VARIANT 98 FT /note="G -> S (in SCCD)" FT /evidence="ECO:0000269|PubMed:19649163" FT /id="VAR_064338" FT VARIANT 102 FT /note="N -> S (in SCCD; reduced menaquinone-4 (MK-4) FT synthesis; does not affect coenzyme Q10 synthesis; FT dbSNP:rs118203945)" FT /evidence="ECO:0000269|PubMed:17668063, FT ECO:0000269|PubMed:17962451, ECO:0000269|PubMed:18176953, FT ECO:0000269|PubMed:20505825, ECO:0000269|PubMed:23169578, FT ECO:0000269|PubMed:23374346" FT /id="VAR_043714" FT VARIANT 112 FT /note="D -> G (in SCCD; does not affect coenzyme Q10 FT synthesis; dbSNP:rs118203950)" FT /evidence="ECO:0000269|PubMed:17668063, FT ECO:0000269|PubMed:23374346" FT /id="VAR_043715" FT VARIANT 112 FT /note="D -> N (in SCCD; reduced menaquinone-4 (MK-4) FT synthesis)" FT /evidence="ECO:0000269|PubMed:20505825, FT ECO:0000269|PubMed:23169578" FT /id="VAR_064339" FT VARIANT 118 FT /note="D -> G (in SCCD)" FT /evidence="ECO:0000269|PubMed:18176953" FT /id="VAR_043716" FT VARIANT 119 FT /note="R -> G (in SCCD; dbSNP:rs118203947)" FT /evidence="ECO:0000269|PubMed:17668063" FT /id="VAR_043717" FT VARIANT 121 FT /note="L -> F (in SCCD)" FT /evidence="ECO:0000269|PubMed:18176953" FT /id="VAR_043718" FT VARIANT 122 FT /note="V -> E (in SCCD)" FT /evidence="ECO:0000269|PubMed:20505825" FT /id="VAR_064340" FT VARIANT 122 FT /note="V -> G (in SCCD)" FT /evidence="ECO:0000269|PubMed:20505825" FT /id="VAR_064341" FT VARIANT 171 FT /note="S -> P (in SCCD; dbSNP:rs118203951)" FT /evidence="ECO:0000269|PubMed:18176953, FT ECO:0000269|PubMed:19429578" FT /id="VAR_043719" FT VARIANT 175 FT /note="T -> I (in SCCD; dbSNP:rs118203948)" FT /evidence="ECO:0000269|PubMed:17668063, FT ECO:0000269|PubMed:18176953" FT /id="VAR_043720" FT VARIANT 177 FT /note="G -> E (in SCCD; reduced menaquinone-4 (MK-4) FT synthesis; dbSNP:rs397514669)" FT /evidence="ECO:0000269|PubMed:23169578" FT /id="VAR_069267" FT VARIANT 177 FT /note="G -> R (in SCCD; reduced menaquinone-4 (MK-4) FT synthesis; dbSNP:rs118203946)" FT /evidence="ECO:0000269|PubMed:17962451, FT ECO:0000269|PubMed:18176953, ECO:0000269|PubMed:23169578" FT /id="VAR_043721" FT VARIANT 186 FT /note="G -> R (in SCCD; dbSNP:rs118203952)" FT /evidence="ECO:0000269|PubMed:18176953" FT /id="VAR_043722" FT VARIANT 188 FT /note="L -> H (in SCCD)" FT /evidence="ECO:0000269|PubMed:20505825" FT /id="VAR_064342" FT VARIANT 232 FT /note="N -> S (in SCCD; dbSNP:rs118203949)" FT /evidence="ECO:0000269|PubMed:17668063" FT /id="VAR_043723" FT VARIANT 236 FT /note="D -> E (in SCCD; dbSNP:rs118203953)" FT /evidence="ECO:0000269|PubMed:18176953" FT /id="VAR_043724" FT VARIANT 240 FT /note="D -> N (in SCCD; dbSNP:rs371811409)" FT /evidence="ECO:0000269|PubMed:20489584" FT /id="VAR_064343" FT CONFLICT 163 FT /note="I -> V (in Ref. 3; BAD96528)" FT /evidence="ECO:0000305" SQ SEQUENCE 338 AA; 36831 MW; 02808542DB9EA249 CRC64; MAASQVLGEK INILSGETVK AGDRDPLGND CPEQDRLPQR SWRQKCASYV LALRPWSFSA SLTPVALGSA LAYRSHGVLD PRLLVGCAVA VLAVHGAGNL VNTYYDFSKG IDHKKSDDRT LVDRILEPQD VVRFGVFLYT LGCVCAACLY YLSPLKLEHL ALIYFGGLSG SFLYTGGIGF KYVALGDLII LITFGPLAVM FAYAIQVGSL AIFPLVYAIP LALSTEAILH SNNTRDMESD REAGIVTLAI LIGPTFSYIL YNTLLFLPYL VFSILATHCT ISLALPLLTI PMAFSLERQF RSQAFNKLPQ RTAKLNLLLG LFYVFGIILA PAGSLPKI //