UBIA1_HUMAN
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 03-AUG-2022, entry version 161.
DE RecName: Full=UbiA prenyltransferase domain-containing protein 1;
DE EC=2.5.1.-;
DE AltName: Full=Transitional epithelial response protein 1;
GN Name=UBIAD1; Synonyms=TERE1;
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, 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, AND CHARACTERIZATION OF VARIANTS SCCD
RP 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. MK-4 is a vitamin K2 isoform present at high
CC concentrations in the brain, kidney and pancreas, and is 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. {ECO:0000269|PubMed:20953171,
CC ECO:0000269|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; Multi-pass
CC membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC protein. Mitochondrion membrane. Cytoplasm. Nucleus.
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}.
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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; 102.
DR IntAct; Q9Y5Z9; 55.
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; Q9Y5Z9; -.
DR PeptideAtlas; Q9Y5Z9; -.
DR PRIDE; Q9Y5Z9; -.
DR ProteomicsDB; 86555; -. [Q9Y5Z9-1]
DR ProteomicsDB; 86556; -. [Q9Y5Z9-2]
DR Antibodypedia; 13750; 121 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 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; 1146311at2759; -.
DR PhylomeDB; Q9Y5Z9; -.
DR TreeFam; TF323238; -.
DR BioCyc; MetaCyc:ENSG00000120942-MON; -.
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; 179 hits in 1087 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 162 other tissues.
DR ExpressionAtlas; Q9Y5Z9; baseline and differential.
DR Genevisible; Q9Y5Z9; HS.
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:0030173; C:integral component of 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: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; -; 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 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
