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Ornithine carbamoyltransferase, mitochondrial (EC 2.1.3.3) (Ornithine transcarbamylase) (OTCase)

 OTC_HUMAN               Reviewed;         354 AA.
P00480; A8K9P2; D3DWB0; Q3KNR1; Q6B0I1; Q9NYJ5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 3.
20-JUN-2018, entry version 216.
RecName: Full=Ornithine carbamoyltransferase, mitochondrial;
EC=2.1.3.3;
AltName: Full=Ornithine transcarbamylase;
Short=OTCase;
Flags: Precursor;
Name=OTC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PRO-111 AND ARG-270.
TISSUE=Liver;
PubMed=6372096; DOI=10.1126/science.6372096;
Horwich A.L., Fenton W.A., Williams K.R., Kalousek F., Kraus J.P.,
Doolittle R.F., Konigsberg W., Rosenberg L.E.;
"Structure and expression of a complementary DNA for the nuclear coded
precursor of human mitochondrial ornithine transcarbamylase.";
Science 224:1068-1074(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-101.
TISSUE=Liver;
PubMed=2836378;
Hata A., Tsuzuki T., Shimada K., Takiguchi M., Mori M., Matsuda I.;
"Structure of the human ornithine transcarbamylase gene.";
J. Biochem. 103:302-308(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-46.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
PubMed=3895227; DOI=10.1073/pnas.82.15.4930;
Horwich A.L., Kalousek F., Rosenberg L.E.;
"Arginine in the leader peptide is required for both import and
proteolytic cleavage of a mitochondrial precursor.";
Proc. Natl. Acad. Sci. U.S.A. 82:4930-4933(1985).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
PubMed=3782067; DOI=10.1093/oxfordjournals.jbchem.a121764;
Hata A., Tsuzuki T., Shimada K., Takiguchi M., Mori M., Matsuda I.;
"Isolation and characterization of the human ornithine
transcarbamylase gene: structure of the 5'-end region.";
J. Biochem. 100:717-725(1986).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 269-289, AND VARIANT OTCD
GLN-277.
PubMed=8081373; DOI=10.1093/hmg/3.5.831;
Gilbert-Dussardier B., Rabier D., Strautnieks S., Segues B.,
Bonnefont J.-P., Munnich A.;
"A novel arginine (245) to glutamine change in exon 8 of the ornithine
carbamoyl transferase gene in two unrelated children presenting with
late onset deficiency and showing the same enzymatic pattern.";
Hum. Mol. Genet. 3:831-832(1994).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
CHARACTERIZATION OF VARIANTS OTCD ARG-195; VAL-196 AND ALA-264.
PubMed=8112735; DOI=10.1007/BF00210596;
Matsuura T., Hoshide R., Setoyama C., Komaki S., Kiwaki K., Endo F.,
Nishikawa S., Matsuda I.;
"Expression of four mutant human ornithine transcarbamylase genes in
cultured Cos 1 cells relates to clinical phenotypes.";
Hum. Genet. 93:129-134(1994).
[12]
ACETYLATION AT LYS-88, AND ENZYME REGULATION.
PubMed=19318352; DOI=10.1074/jbc.M901921200;
Yu W., Lin Y., Yao J., Huang W., Lei Q., Xiong Y., Zhao S., Guan K.L.;
"Lysine 88 acetylation negatively regulates ornithine
carbamoyltransferase activity in response to nutrient signals.";
J. Biol. Chem. 284:13669-13675(2009).
[13]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG.
PubMed=9852088; DOI=10.1074/jbc.273.51.34247;
Shi D., Morizono H., Ha Y., Aoyagi M., Tuchman M., Allewell N.M.;
"1.85-A resolution crystal structure of human ornithine
transcarbamoylase complexed with N-phosphonacetyl-L-ornithine.
Catalytic mechanism and correlation with inherited deficiency.";
J. Biol. Chem. 273:34247-34254(1998).
[14]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
PubMed=10813810;
DOI=10.1002/(SICI)1097-0134(20000601)39:4<271::AID-PROT10>3.0.CO;2-E;
Shi D., Morizono H., Aoyagi M., Tuchman M., Allewell N.M.;
"Crystal structure of human ornithine transcarbamylase complexed with
carbamoyl phosphate and L-norvaline at 1.9 A resolution.";
Proteins 39:271-277(2000).
[15]
REVIEW ON VARIANTS.
PubMed=8364586; DOI=10.1002/humu.1380020304;
Tuchman M.;
"Mutations and polymorphisms in the human ornithine transcarbamylase
gene.";
Hum. Mutat. 2:174-178(1993).
[16]
REVIEW ON VARIANTS.
PubMed=7627182; DOI=10.1002/humu.1380050404;
Tuchman M., Plante R.J.;
"Mutations and polymorphisms in the human ornithine transcarbamylase
gene: mutation update addendum.";
Hum. Mutat. 5:293-295(1995).
[17]
REVIEW ON VARIANTS, AND 3D-STRUCTURE MODELING.
PubMed=8544185; DOI=10.1136/jmg.32.9.680;
Tuchman M., Morizono H., Reish O., Yuan X., Allewell N.M.;
"The molecular basis of ornithine transcarbamylase deficiency:
modelling the human enzyme and the effects of mutations.";
J. Med. Genet. 32:680-688(1995).
[18]
VARIANT OTCD GLN-141.
PubMed=3170748; DOI=10.1172/JCI113738;
Maddalena A., Spence J.E., O'Brien W.E., Nussbaum R.L.;
"Characterization of point mutations in the same arginine codon in
three unrelated patients with ornithine transcarbamylase deficiency.";
J. Clin. Invest. 82:1353-1358(1988).
[19]
VARIANT OTCD GLN-141, AND CHARACTERIZATION OF VARIANT OTCD GLN-141.
PubMed=2556444; DOI=10.1172/JCI114360;
Lee J.T., Nussbaum R.L.;
"An arginine to glutamine mutation in residue 109 of human ornithine
transcarbamylase completely abolishes enzymatic activity in Cos1
cells.";
J. Clin. Invest. 84:1762-1766(1989).
[20]
VARIANTS OTCD GLN-26; PRO-45 AND GLU-216, AND VARIANT ARG-46.
PubMed=2474822; DOI=10.1073/pnas.86.15.5888;
Grompe M., Muzny D.M., Caskey C.T.;
"Scanning detection of mutations in human ornithine transcarbamoylase
by chemical mismatch cleavage.";
Proc. Natl. Acad. Sci. U.S.A. 86:5888-5892(1989).
[21]
VARIANT OTCD TRP-277.
PubMed=2347583; DOI=10.1016/0888-7543(90)90537-5;
Finkelstein J.E., Francomano C.A., Brusilow S.W., Traystman M.D.;
"Use of denaturing gradient gel electrophoresis for detection of
mutation and prospective diagnosis in late onset ornithine
transcarbamylase deficiency.";
Genomics 7:167-172(1990).
[22]
VARIANTS OTCD GLN-92 AND LEU-320, AND VARIANT PRO-111.
PubMed=1671317;
Grompe M., Caskey C.T., Fenwick R.G. Jr.;
"Improved molecular diagnostics for ornithine transcarbamylase
deficiency.";
Am. J. Hum. Genet. 48:212-222(1991).
[23]
VARIANT OTCD LEU-225.
PubMed=1721894; DOI=10.1007/BF00206063;
Hentzen D., Pelet A., Feldman D., Rabier D., Berthelot J., Munnich A.;
"Fatal hyperammonemia resulting from a C-to-T mutation at a MspI site
of the ornithine transcarbamylase gene.";
Hum. Genet. 88:153-156(1991).
[24]
VARIANTS OTCD GLU-79; THR-94; PHE-304 AND ASP-345.
PubMed=1480464; DOI=10.1203/00006450-199211000-00020;
Tuchman M., Holzknecht R.A., Gueron A.B., Berry S.A., Tsai M.Y.;
"Six new mutations in the ornithine transcarbamylase gene detected by
single-strand conformational polymorphism.";
Pediatr. Res. 32:600-604(1992).
[25]
VARIANT OTCD PRO-140.
PubMed=8099056; DOI=10.1007/BF00217350;
Tsai M.Y., Holzknecht R.A., Tuchman M.;
"Single-strand conformational polymorphism and direct sequencing
applied to carrier testing in families with ornithine transcarbamylase
deficiency.";
Hum. Genet. 91:321-325(1993).
[26]
VARIANTS OTCD LEU-117; LEU-182 AND CYS-203.
PubMed=8019569; DOI=10.1002/humu.1380030325;
Tuchman M., Plante R.J., Giguere Y., Lemieux B.;
"The ornithine transcarbamylase gene: new 'private' mutations in four
patients and study of a polymorphism.";
Hum. Mutat. 3:318-320(1994).
[27]
VARIANTS OTCD GLY-126; HIS-129 AND MET-172.
PubMed=8081398; DOI=10.1002/humu.1380030415;
Matsuura T., Hoshide R., Kiwaki K., Komaki S., Koike E., Endo F.,
Oyanagi K., Suzuki Y., Kato I., Ishikawa K., Yoda H., Kamitani S.,
Sakaki Y., Matsuda I.;
"Four newly identified ornithine transcarbamylase (OTC) mutations
(D126G, R129H, I172M and W332X) in Japanese male patients with early-
onset OTC deficiency.";
Hum. Mutat. 3:402-406(1994).
[28]
VARIANTS OTCD HIS-40; HIS-129; ARG-195; THR-225; GLN-277 AND GLU-309
DEL.
PubMed=7951259; DOI=10.1002/humu.1380040109;
Tuchman M., Plante R.J., McCann M.T., Qureshi A.A.;
"Seven new mutations in the human ornithine transcarbamylase gene.";
Hum. Mutat. 4:57-60(1994).
[29]
VARIANTS OTCD THR-159 AND VAL-209.
PubMed=8530002; DOI=10.1007/BF00197410;
Garcia-Perez M.A., Sanjurjo P., Briones P., Garcia-Munoz M.J.,
Rubio V.;
"A splicing mutation, a nonsense mutation (Y167X) and two missense
mutations (I159T and A209V) in Spanish patients with ornithine
transcarbamylase deficiency.";
Hum. Genet. 96:549-551(1995).
[30]
VARIANT OTCD GLU-269.
PubMed=7474905; DOI=10.1007/BF00710430;
Zimmer K.P., Matsuura T., Colombo J.-P., Koch H.G., Ullrich K.,
Deufel T., Harms E., Matsuda I.;
"A novel point mutation at codon 269 of the ornithine transcarbamylase
(OTC) gene causing neonatal onset of OTC deficiency.";
J. Inherit. Metab. Dis. 18:356-357(1995).
[31]
VARIANTS OTCD MET-125; ARG-188; VAL-209 AND LEU-302.
PubMed=8807340;
DOI=10.1002/(SICI)1098-1004(1996)8:1<74::AID-HUMU11>3.3.CO;2-6;
Gilbert-Dussardier B., Segues B., Rozet J.-M., Rabier D., Calvas P.,
de Lumley L., Bonnefont J.-P., Munnich A.;
"Partial duplication [dup. TCAC (178)] and novel point mutations
(T125M, G188R, A209V, and H302L) of the ornithine transcarbamylase
gene in congenital hyperammonemia.";
Hum. Mutat. 8:74-76(1996).
[32]
VARIANTS OTCD HIS-40; ASN-88; TYR-202 AND ASN-263.
Guardamagna O., Gatti E., Parini R., Plante R.J., Tuchman M.;
"Genotype-phenotype correlations in ornithine transcarbamylase
deficiency.";
Enzyme Protein 49:191-191(1996).
[33]
VARIANTS OTCD ASN-88; CYS-176; ALA-220; TYR-302 AND LYS-343.
PubMed=8956038;
DOI=10.1002/(SICI)1098-1004(1996)8:4<333::AID-HUMU6>3.0.CO;2-8;
Leibundgut E.O., Wermuth B., Colombo J.-P., Liechti-Gallati S.;
"Ornithine transcarbamylase deficiency: characterization of gene
mutations and polymorphisms.";
Hum. Mutat. 8:333-339(1996).
[34]
VARIANT OTCD GLU-272 DEL.
PubMed=8956045;
DOI=10.1002/(SICI)1098-1004(1996)8:4<373::AID-HUMU13>3.0.CO;2-#;
Segues B., Saugier Veber P., Rabier D., Calvas P., Saudubray J.-M.,
Gilbert-Dussardier B., Bonnefont J.-P., Munnich A.;
"A 3-base pair in-frame deletion in exon 8 (delGlu272/273) of the
ornithine transcarbamylase gene in late-onset hyperammonemic coma.";
Hum. Mutat. 8:373-374(1996).
[35]
VARIANTS OTCD ILE-44; GLN-141 AND TYR-214, AND VARIANT LEU-101.
PubMed=8830175; DOI=10.1007/BF01799346;
Yoo H.-W., Kim G.-H., Lee D.-H.;
"Identification of new mutations in the ornithine transcarbamylase
(OTC) gene in Korean families.";
J. Inherit. Metab. Dis. 19:31-42(1996).
[36]
VARIANTS OTCD.
PubMed=9286441;
DOI=10.1002/(SICI)1096-8628(19970905)71:4<378::AID-AJMG2>3.3.CO;2-9;
Matsuda I., Tanase S.;
"The ornithine transcarbamylase (OTC) gene: mutations in 50 Japanese
families with OTC deficiency.";
Am. J. Med. Genet. 71:378-383(1997).
[37]
CHARACTERIZATION OF VARIANT OTCD TRP-277.
PubMed=9065786; DOI=10.1042/bj3220625;
Morizono H., Tuchman M., Rajagopal B.S., McCann M.T., Listrom C.D.,
Yuan X., Venugopal D., Barany G., Allewell N.M.;
"Expression, purification and kinetic characterization of wild-type
human ornithine transcarbamylase and a recurrent mutant that produces
'late onset' hyperammonaemia.";
Biochem. J. 322:625-631(1997).
[38]
VARIANTS OTCD PRO-63; ASP-100; ASP-183; LYS-213 AND PRO-340, AND
VARIANT PHE-43.
PubMed=9143919;
DOI=10.1002/(SICI)1098-1004(1997)9:5<409::AID-HUMU5>3.3.CO;2-P;
Oppliger Leibundgut E., Liechti-Gallati S., Colombo J.-P., Wermuth B.;
"Ornithine transcarbamylase deficiency: ten new mutations and high
proportion of de novo mutations in heterozygous females.";
Hum. Mutat. 9:409-411(1997).
[39]
VARIANTS OTCD.
PubMed=9266388; DOI=10.1023/A:1005301513465;
Tuchman M., Morizono H., Rajagopal B.S., Plante R.J., Allewell N.M.;
"Identification of 'private' mutations in patients with ornithine
transcarbamylase deficiency.";
J. Inherit. Metab. Dis. 20:525-527(1997).
[40]
VARIANTS OTCD 178-THE-LEU-179 DEL; HIS-180; PRO-201; ARG-207; ILE-264
AND ARG-267.
PubMed=9452024;
Shimadzu M., Matsumoto H., Matsuura T., Kobayashi K., Komaki S.,
Kiwaki K., Hoshide R., Endo F., Saheki T., Matsuda I.;
"Ten novel mutations of the ornithine transcarbamylase (OTC) gene in
OTC deficiency.";
Hum. Mutat. Suppl. 1:S5-S7(1998).
[41]
VARIANTS OTCD CYS-39; GLN-244 AND ARG-303.
PubMed=9452049;
Calvas P., Seques B., Rozet J.-M., Rabier D., Bonnefont J.-P.,
Munnich A.;
"Novel intragenic deletions and point mutations of the ornithine
transcarbamylase gene in congenital hyperammonemia.";
Hum. Mutat. Suppl. 1:S81-S84(1998).
[42]
VARIANT OTCD ASP-55.
PubMed=9452065;
Nishiyori A., Yoshino M., Tananari Y., Matsuura T., Hoshide R.,
Matsuda I., Mori M., Kato H.;
"Y55D mutation in ornithine transcarbamylase associated with late-
onset hyperammonemia in a male.";
Hum. Mutat. Suppl. 1:S131-S133(1998).
[43]
VARIANT OTCD ASP-83.
Bartholomew D.W., McClellan J.;
"A novel missense mutation in the human ornithine transcarbamylase
gene.";
Hum. Mutat. 12:220-220(1998).
[44]
VARIANTS OTCD PHE-172; VAL-188 AND ARG-197.
PubMed=10502831;
DOI=10.1002/(SICI)1098-1004(199910)14:4<352::AID-HUMU15>3.3.CO;2-4;
Climent C., Garcia-Perez M.A., Sanjurjo P., Ruiz-Sanz J.-I.,
Vilaseca M.A., Pineda M., Campistol J., Rubio V.;
"Identification of a cytogenetic deletion and of four novel mutations
(Q69X, I172F, G188V, G197R) affecting the gene for ornithine
transcarbamylase (OTC) in Spanish patients with OTC deficiency.";
Hum. Mutat. 14:352-353(1999).
[45]
VARIANTS OTCD LYS-198; VAL-209 AND LYS-326, AND VARIANT ARG-270.
PubMed=10070627; DOI=10.1023/A:1005476021549;
Popowska E., Ciara E., Rokicki D., Pronicka E.;
"Three novel and one recurrent ornithine carbamoyltransferase gene
mutations in Polish patients.";
J. Inherit. Metab. Dis. 22:92-93(1999).
[46]
VARIANTS OTCD LYS-262; ALA-264 AND LEU-265.
PubMed=10737985;
DOI=10.1002/(SICI)1098-1004(200004)15:4<380::AID-HUMU12>3.0.CO;2-Q;
Giorgi M., Morrone A., Donati M.A., Ciani F., Bardelli T.,
Biasucci G., Zammarchi E.;
"Lymphocyte mRNA analysis of the ornithine transcarbamylase gene in
Italian OTCD male patients and manifesting carriers: identification of
novel mutations.";
Hum. Mutat. 15:380-381(2000).
[47]
VARIANTS OTCD SER-160; PHE-191; ILE-206; PHE-301; HIS-305 AND PRO-341,
AND VARIANT ALA-333.
PubMed=11793483; DOI=10.1002/humu.9011;
Climent C., Rubio V.;
"Identification of seven novel missense mutations, two splice-site
mutations, two microdeletions and a polymorphic amino acid
substitution in the gene for ornithine transcarbamylase (OTC) in
patients with OTC deficiency.";
Hum. Mutat. 19:185-186(2002).
[48]
VARIANT [LARGE SCALE ANALYSIS] ARG-270.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate
+ L-citrulline.
-!- ENZYME REGULATION: Negatively regulated by lysine acetylation.
{ECO:0000269|PubMed:19318352}.
-!- PATHWAY: Nitrogen metabolism; urea cycle; L-citrulline from L-
ornithine and carbamoyl phosphate: step 1/1.
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10813810,
ECO:0000269|PubMed:9852088}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- TISSUE SPECIFICITY: Mainly expressed in liver and intestinal
mucosa.
-!- PTM: Acetylation at Lys-88 negatively regulates ornithine
carbamoyltransferase activity in response to nutrient signals.
{ECO:0000269|PubMed:19318352}.
-!- DISEASE: Ornithine carbamoyltransferase deficiency (OTCD)
[MIM:311250]: An X-linked disorder of the urea cycle which causes
a form of hyperammonemia. Mutations with no residual enzyme
activity are always expressed in hemizygote males by a very severe
neonatal hyperammonemic coma that generally proves to be fatal.
Heterozygous females are either asymptomatic or express orotic
aciduria spontaneously or after protein intake. The disorder is
treatable with supplemental dietary arginine and low protein diet.
The arbitrary classification of patients into the 'neonatal' group
(clinical hyperammonemia in the first few days of life) and 'late'
onset (clinical presentation after the neonatal period) has been
used to differentiate severe from mild forms.
{ECO:0000269|PubMed:10070627, ECO:0000269|PubMed:10502831,
ECO:0000269|PubMed:10737985, ECO:0000269|PubMed:11793483,
ECO:0000269|PubMed:1480464, ECO:0000269|PubMed:1671317,
ECO:0000269|PubMed:1721894, ECO:0000269|PubMed:2347583,
ECO:0000269|PubMed:2474822, ECO:0000269|PubMed:2556444,
ECO:0000269|PubMed:3170748, ECO:0000269|PubMed:7474905,
ECO:0000269|PubMed:7951259, ECO:0000269|PubMed:8019569,
ECO:0000269|PubMed:8081373, ECO:0000269|PubMed:8081398,
ECO:0000269|PubMed:8099056, ECO:0000269|PubMed:8112735,
ECO:0000269|PubMed:8530002, ECO:0000269|PubMed:8807340,
ECO:0000269|PubMed:8830175, ECO:0000269|PubMed:8956038,
ECO:0000269|PubMed:8956045, ECO:0000269|PubMed:9065786,
ECO:0000269|PubMed:9143919, ECO:0000269|PubMed:9266388,
ECO:0000269|PubMed:9286441, ECO:0000269|PubMed:9452024,
ECO:0000269|PubMed:9452049, ECO:0000269|PubMed:9452065,
ECO:0000269|Ref.32, ECO:0000269|Ref.43}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ATCase/OTCase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; K02100; AAA59975.1; -; mRNA.
EMBL; D00230; BAA00161.1; -; Genomic_DNA.
EMBL; AK292757; BAF85446.1; -; mRNA.
EMBL; AF241726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL606748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL607040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471141; EAW59439.1; -; Genomic_DNA.
EMBL; CH471141; EAW59440.1; -; Genomic_DNA.
EMBL; BC074745; AAH74745.1; -; mRNA.
EMBL; BC107153; AAI07154.1; -; mRNA.
EMBL; BC107154; AAI07155.1; -; mRNA.
EMBL; BC114496; AAI14497.1; -; mRNA.
EMBL; M11235; AAA59976.1; -; Genomic_DNA.
EMBL; D00095; BAA00058.1; -; Genomic_DNA.
EMBL; X04443; CAA28039.1; -; Genomic_DNA.
EMBL; S73640; AAB31859.1; -; Genomic_DNA.
CCDS; CCDS14247.1; -.
PIR; A41444; OWHU.
RefSeq; NP_000522.3; NM_000531.5.
UniGene; Hs.117050; -.
PDB; 1C9Y; X-ray; 1.90 A; A=34-354.
PDB; 1EP9; X-ray; 2.40 A; A=34-354.
PDB; 1FVO; X-ray; 2.60 A; A/B=34-354.
PDB; 1OTH; X-ray; 1.85 A; A=34-354.
PDBsum; 1C9Y; -.
PDBsum; 1EP9; -.
PDBsum; 1FVO; -.
PDBsum; 1OTH; -.
ProteinModelPortal; P00480; -.
SMR; P00480; -.
BioGrid; 111050; 14.
CORUM; P00480; -.
STRING; 9606.ENSP00000039007; -.
BindingDB; P00480; -.
ChEMBL; CHEMBL2222; -.
DrugBank; DB03519; 2-Amino-Pentanoic Acid.
DrugBank; DB00155; L-Citrulline.
DrugBank; DB00129; L-Ornithine.
DrugBank; DB02011; N-(Phosphonoacetyl)-L-Ornithine.
DrugBank; DB04185; Norvaline.
iPTMnet; P00480; -.
PhosphoSitePlus; P00480; -.
BioMuta; OTC; -.
DMDM; 84028235; -.
REPRODUCTION-2DPAGE; P00480; -.
MaxQB; P00480; -.
PaxDb; P00480; -.
PeptideAtlas; P00480; -.
PRIDE; P00480; -.
ProteomicsDB; 51254; -.
Ensembl; ENST00000039007; ENSP00000039007; ENSG00000036473.
GeneID; 5009; -.
KEGG; hsa:5009; -.
UCSC; uc004def.5; human.
CTD; 5009; -.
DisGeNET; 5009; -.
EuPathDB; HostDB:ENSG00000036473.6; -.
GeneCards; OTC; -.
GeneReviews; OTC; -.
HGNC; HGNC:8512; OTC.
HPA; HPA000243; -.
HPA; HPA000570; -.
MalaCards; OTC; -.
MIM; 300461; gene.
MIM; 311250; phenotype.
neXtProt; NX_P00480; -.
OpenTargets; ENSG00000036473; -.
Orphanet; 664; Ornithine transcarbamylase deficiency.
PharmGKB; PA32840; -.
eggNOG; KOG1504; Eukaryota.
eggNOG; COG0078; LUCA.
GeneTree; ENSGT00510000047417; -.
HOGENOM; HOG000022686; -.
HOVERGEN; HBG007881; -.
InParanoid; P00480; -.
KO; K00611; -.
OMA; DGNNVCN; -.
OrthoDB; EOG091G0QB1; -.
PhylomeDB; P00480; -.
TreeFam; TF352580; -.
BioCyc; MetaCyc:HS00516-MONOMER; -.
BRENDA; 2.1.3.3; 2681.
Reactome; R-HSA-1268020; Mitochondrial protein import.
Reactome; R-HSA-70635; Urea cycle.
SABIO-RK; P00480; -.
SIGNOR; P00480; -.
UniPathway; UPA00158; UER00271.
EvolutionaryTrace; P00480; -.
GeneWiki; Ornithine_transcarbamylase; -.
GenomeRNAi; 5009; -.
PMAP-CutDB; P00480; -.
PRO; PR:P00480; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000036473; -.
CleanEx; HS_OTC; -.
Genevisible; P00480; HS.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
GO; GO:0016597; F:amino acid binding; IEA:Ensembl.
GO; GO:0004585; F:ornithine carbamoyltransferase activity; IDA:BHF-UCL.
GO; GO:0042301; F:phosphate ion binding; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0097272; P:ammonia homeostasis; IMP:BHF-UCL.
GO; GO:0055081; P:anion homeostasis; IEA:Ensembl.
GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
GO; GO:0019240; P:citrulline biosynthetic process; IDA:BHF-UCL.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0007494; P:midgut development; IEA:Ensembl.
GO; GO:0006593; P:ornithine catabolic process; IDA:BHF-UCL.
GO; GO:0070207; P:protein homotrimerization; IEA:Ensembl.
GO; GO:0070781; P:response to biotin; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
GO; GO:0000050; P:urea cycle; IDA:BHF-UCL.
Gene3D; 3.40.50.1370; -; 3.
InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
InterPro; IPR002292; Orn/put_carbamltrans.
Pfam; PF00185; OTCace; 1.
Pfam; PF02729; OTCace_N; 1.
PRINTS; PR00100; AOTCASE.
PRINTS; PR00102; OTCASE.
SUPFAM; SSF53671; SSF53671; 1.
TIGRFAMs; TIGR00658; orni_carb_tr; 1.
PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Amino-acid biosynthesis;
Arginine biosynthesis; Complete proteome; Disease mutation;
Mitochondrion; Phosphoprotein; Polymorphism; Reference proteome;
Transferase; Transit peptide; Urea cycle.
TRANSIT 1 32 Mitochondrion.
CHAIN 33 354 Ornithine carbamoyltransferase,
mitochondrial.
/FTId=PRO_0000020334.
REGION 90 94 Ornithine and carbamoyl phosphate
binding.
REGION 168 171 Ornithine and carbamoyl phosphate
binding.
REGION 263 267 Ornithine binding.
REGION 302 305 Ornithine binding. {ECO:0000250}.
ACT_SITE 303 303 {ECO:0000250}.
BINDING 141 141 Carbamoyl phosphate.
BINDING 141 141 Ornithine.
BINDING 199 199 Ornithine.
BINDING 330 330 Carbamoyl phosphate.
BINDING 330 330 Ornithine.
MOD_RES 70 70 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 70 70 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 80 80 N6-succinyllysine.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 88 88 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:19318352}.
MOD_RES 88 88 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 144 144 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 144 144 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 221 221 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 221 221 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 231 231 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 231 231 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 238 238 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 238 238 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 243 243 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 274 274 N6-succinyllysine.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 289 289 N6-succinyllysine.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 292 292 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 292 292 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 307 307 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
MOD_RES 307 307 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P11725}.
VARIANT 26 26 R -> Q (in OTCD; dbSNP:rs68031618).
{ECO:0000269|PubMed:2474822}.
/FTId=VAR_004843.
VARIANT 39 39 G -> C (in OTCD; late onset;
dbSNP:rs72554306).
{ECO:0000269|PubMed:9452049}.
/FTId=VAR_004844.
VARIANT 40 40 R -> C (in OTCD; late onset;
dbSNP:rs72554307).
/FTId=VAR_004845.
VARIANT 40 40 R -> H (in OTCD; late onset;
dbSNP:rs72554308).
{ECO:0000269|PubMed:7951259,
ECO:0000269|Ref.32}.
/FTId=VAR_004846.
VARIANT 43 43 L -> F (in dbSNP:rs72554309).
{ECO:0000269|PubMed:9143919}.
/FTId=VAR_004847.
VARIANT 44 44 T -> I (in OTCD; dbSNP:rs72554310).
{ECO:0000269|PubMed:8830175}.
/FTId=VAR_004848.
VARIANT 45 45 L -> P (in OTCD; dbSNP:rs72554312).
{ECO:0000269|PubMed:2474822}.
/FTId=VAR_004849.
VARIANT 45 45 L -> V (in OTCD; dbSNP:rs72554311).
/FTId=VAR_004850.
VARIANT 46 46 K -> R (in dbSNP:rs1800321).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2474822}.
/FTId=VAR_004851.
VARIANT 47 47 N -> I (in OTCD; neonatal;
dbSNP:rs67939655).
/FTId=VAR_004852.
VARIANT 50 50 G -> R (in OTCD; late onset;
dbSNP:rs67486158).
/FTId=VAR_004853.
VARIANT 55 55 Y -> D (in OTCD; late onset;
dbSNP:rs72554319).
{ECO:0000269|PubMed:9452065}.
/FTId=VAR_004854.
VARIANT 56 56 M -> T (in OTCD; late onset;
dbSNP:rs72554320).
/FTId=VAR_004855.
VARIANT 60 60 S -> L (in OTCD; dbSNP:rs72554323).
/FTId=VAR_004856.
VARIANT 63 63 L -> P (in OTCD; late onset;
dbSNP:rs72554324).
{ECO:0000269|PubMed:9143919}.
/FTId=VAR_004857.
VARIANT 79 79 G -> E (in OTCD; dbSNP:rs72554331).
{ECO:0000269|PubMed:1480464}.
/FTId=VAR_004858.
VARIANT 82 82 Missing (in OTCD).
/FTId=VAR_004859.
VARIANT 83 83 G -> D (in OTCD; dbSNP:rs72554337).
{ECO:0000269|Ref.43}.
/FTId=VAR_004860.
VARIANT 83 83 G -> R (in OTCD; neonatal;
dbSNP:rs72554336).
/FTId=VAR_004861.
VARIANT 87 87 E -> K (in OTCD; dbSNP:rs72554338).
/FTId=VAR_004862.
VARIANT 88 88 K -> N (in OTCD; late onset;
dbSNP:rs72554339).
{ECO:0000269|PubMed:8956038,
ECO:0000269|Ref.32}.
/FTId=VAR_004863.
VARIANT 90 90 S -> R (in OTCD; dbSNP:rs72554342).
/FTId=VAR_004864.
VARIANT 92 92 R -> Q (in OTCD; dbSNP:rs66550389).
{ECO:0000269|PubMed:1671317}.
/FTId=VAR_004865.
VARIANT 93 93 T -> A (in OTCD; late onset;
dbSNP:rs72554344).
/FTId=VAR_004866.
VARIANT 94 94 R -> T (in OTCD; dbSNP:rs72554345).
{ECO:0000269|PubMed:1480464}.
/FTId=VAR_004867.
VARIANT 100 100 G -> D (in OTCD; late onset;
dbSNP:rs72554349).
{ECO:0000269|PubMed:9143919}.
/FTId=VAR_004868.
VARIANT 101 101 F -> L (in dbSNP:rs1133135).
{ECO:0000269|PubMed:2836378,
ECO:0000269|PubMed:8830175}.
/FTId=VAR_004869.
VARIANT 102 102 A -> E (in OTCD; dbSNP:rs72554350).
/FTId=VAR_004870.
VARIANT 111 111 L -> P (in dbSNP:rs1800324).
{ECO:0000269|PubMed:1671317,
ECO:0000269|PubMed:6372096}.
/FTId=VAR_004871.
VARIANT 117 117 H -> L (in OTCD; dbSNP:rs66539573).
{ECO:0000269|PubMed:8019569}.
/FTId=VAR_004872.
VARIANT 117 117 H -> R (in OTCD; late onset;
dbSNP:rs66539573).
/FTId=VAR_004873.
VARIANT 125 125 T -> M (in OTCD; neonatal;
dbSNP:rs72554356).
{ECO:0000269|PubMed:8807340}.
/FTId=VAR_004874.
VARIANT 126 126 D -> G (in OTCD; 0.9% of wild-type
activity; early onset; dbSNP:rs72554358).
{ECO:0000269|PubMed:8081398}.
/FTId=VAR_004875.
VARIANT 129 129 R -> H (in OTCD; 2.1% of wild-type
activity; early onset; dbSNP:rs66656800).
{ECO:0000269|PubMed:7951259,
ECO:0000269|PubMed:8081398}.
/FTId=VAR_004876.
VARIANT 139 139 L -> S (in OTCD; dbSNP:rs72556259).
/FTId=VAR_004877.
VARIANT 140 140 A -> P (in OTCD; late onset;
dbSNP:rs72556260).
{ECO:0000269|PubMed:8099056}.
/FTId=VAR_010605.
VARIANT 141 141 R -> P (in OTCD; dbSNP:rs68026851).
/FTId=VAR_004878.
VARIANT 141 141 R -> Q (in OTCD; activity is 100-fold
lower; most common point mutation;
dbSNP:rs68026851).
{ECO:0000269|PubMed:2556444,
ECO:0000269|PubMed:3170748,
ECO:0000269|PubMed:8830175}.
/FTId=VAR_004879.
VARIANT 148 148 L -> F (in OTCD; dbSNP:rs66741318).
/FTId=VAR_004880.
VARIANT 159 159 I -> T (in OTCD; dbSNP:rs72556269).
{ECO:0000269|PubMed:8530002}.
/FTId=VAR_004881.
VARIANT 160 160 I -> S (in OTCD; dbSNP:rs67954347).
{ECO:0000269|PubMed:11793483}.
/FTId=VAR_012651.
VARIANT 161 161 N -> S (in OTCD; dbSNP:rs72556271).
/FTId=VAR_004882.
VARIANT 162 162 G -> R (in OTCD; dbSNP:rs66626662).
/FTId=VAR_004883.
VARIANT 168 168 H -> Q (in OTCD; late onset;
dbSNP:rs72556276).
/FTId=VAR_004884.
VARIANT 168 168 H -> R (in OTCD; late onset;
dbSNP:rs66867430).
/FTId=VAR_004885.
VARIANT 172 172 I -> F (in OTCD; dbSNP:rs72556279).
{ECO:0000269|PubMed:10502831}.
/FTId=VAR_009233.
VARIANT 172 172 I -> M (in OTCD; no activity; early
onset; dbSNP:rs72556280).
{ECO:0000269|PubMed:8081398}.
/FTId=VAR_004886.
VARIANT 174 174 A -> P (in OTCD; dbSNP:rs72556281).
/FTId=VAR_004887.
VARIANT 175 175 D -> V (in OTCD; dbSNP:rs68033093).
/FTId=VAR_004888.
VARIANT 176 176 Y -> C (in OTCD; late onset;
dbSNP:rs72556283).
{ECO:0000269|PubMed:8956038}.
/FTId=VAR_004889.
VARIANT 178 179 Missing (in OTCD; neonatal).
/FTId=VAR_004891.
VARIANT 178 178 T -> M (in OTCD; neonatal;
dbSNP:rs72556284).
/FTId=VAR_004890.
VARIANT 180 180 Q -> H (in OTCD; dbSNP:rs72556287).
{ECO:0000269|PubMed:9452024}.
/FTId=VAR_004892.
VARIANT 181 181 E -> G (in OTCD; neonatal;
dbSNP:rs72556290).
/FTId=VAR_004893.
VARIANT 182 182 H -> L (in OTCD; dbSNP:rs72556291).
{ECO:0000269|PubMed:8019569}.
/FTId=VAR_004894.
VARIANT 183 183 Y -> C (in OTCD; dbSNP:rs72556293).
/FTId=VAR_004895.
VARIANT 183 183 Y -> D (in OTCD; late onset;
dbSNP:rs72556292).
{ECO:0000269|PubMed:9143919}.
/FTId=VAR_004896.
VARIANT 188 188 G -> R (in OTCD; neonatal;
dbSNP:rs72556294).
{ECO:0000269|PubMed:8807340}.
/FTId=VAR_004897.
VARIANT 188 188 G -> V (in OTCD; dbSNP:rs72556295).
{ECO:0000269|PubMed:10502831}.
/FTId=VAR_009234.
VARIANT 191 191 L -> F (in OTCD; dbSNP:rs72556296).
{ECO:0000269|PubMed:11793483}.
/FTId=VAR_012652.
VARIANT 192 192 S -> R (in OTCD; neonatal;
dbSNP:rs72556298).
/FTId=VAR_004898.
VARIANT 195 195 G -> R (in OTCD; no activity;
dbSNP:rs67294955).
{ECO:0000269|PubMed:7951259,
ECO:0000269|PubMed:8112735}.
/FTId=VAR_004899.
VARIANT 196 196 D -> V (in OTCD; neonatal; 3.7% activity;
dbSNP:rs72556300).
{ECO:0000269|PubMed:8112735}.
/FTId=VAR_004900.
VARIANT 196 196 D -> Y (in OTCD; neonatal;
dbSNP:rs66642398).
/FTId=VAR_004901.
VARIANT 197 197 G -> E (in OTCD; dbSNP:rs72556302).
/FTId=VAR_004902.
VARIANT 197 197 G -> R (in OTCD; dbSNP:rs72556301).
{ECO:0000269|PubMed:10502831}.
/FTId=VAR_009235.
VARIANT 198 198 N -> K (in OTCD; dbSNP:rs72558404).
{ECO:0000269|PubMed:10070627}.
/FTId=VAR_010606.
VARIANT 201 201 L -> P (in OTCD; neonatal;
dbSNP:rs72558407).
{ECO:0000269|PubMed:9452024}.
/FTId=VAR_004903.
VARIANT 202 202 H -> Y (in OTCD; dbSNP:rs72558408).
{ECO:0000269|Ref.32}.
/FTId=VAR_004904.
VARIANT 203 203 S -> C (in OTCD; dbSNP:rs72558410).
{ECO:0000269|PubMed:8019569}.
/FTId=VAR_004905.
VARIANT 206 206 M -> I (in OTCD; dbSNP:rs72558413).
{ECO:0000269|PubMed:11793483}.
/FTId=VAR_012653.
VARIANT 206 206 M -> R (in OTCD; neonatal;
dbSNP:rs72558412).
/FTId=VAR_004906.
VARIANT 207 207 S -> R (in OTCD; neonatal;
dbSNP:rs72558415).
{ECO:0000269|PubMed:9452024}.
/FTId=VAR_004907.
VARIANT 208 208 A -> T (in OTCD; late onset;
dbSNP:rs72558416).
/FTId=VAR_004908.
VARIANT 209 209 A -> V (in OTCD; neonatal;
dbSNP:rs72558417).
{ECO:0000269|PubMed:10070627,
ECO:0000269|PubMed:8530002,
ECO:0000269|PubMed:8807340}.
/FTId=VAR_004909.
VARIANT 213 213 M -> K (in OTCD; late onset).
{ECO:0000269|PubMed:9143919}.
/FTId=VAR_004910.
VARIANT 214 214 H -> Y (in OTCD; neonatal;
dbSNP:rs72558420).
{ECO:0000269|PubMed:8830175}.
/FTId=VAR_010607.
VARIANT 216 216 Q -> E (in OTCD; dbSNP:rs72558423).
{ECO:0000269|PubMed:2474822}.
/FTId=VAR_004911.
VARIANT 220 220 P -> A (in OTCD; late onset;
dbSNP:rs72558425).
{ECO:0000269|PubMed:8956038}.
/FTId=VAR_004912.
VARIANT 225 225 P -> L (in OTCD; dbSNP:rs67120076).
{ECO:0000269|PubMed:1721894}.
/FTId=VAR_004913.
VARIANT 225 225 P -> R (in OTCD; neonatal;
dbSNP:rs67120076).
/FTId=VAR_004914.
VARIANT 225 225 P -> T (in OTCD; late onset;
dbSNP:rs72558428).
{ECO:0000269|PubMed:7951259}.
/FTId=VAR_004915.
VARIANT 242 242 T -> I (in OTCD; late onset;
dbSNP:rs72558435).
/FTId=VAR_004916.
VARIANT 244 244 L -> Q (in OTCD; late onset;
dbSNP:rs72558436).
{ECO:0000269|PubMed:9452049}.
/FTId=VAR_004917.
VARIANT 247 247 T -> K (in OTCD; neonatal/late onset;
dbSNP:rs72558437).
/FTId=VAR_004918.
VARIANT 255 255 H -> P (in OTCD; dbSNP:rs72558440).
/FTId=VAR_004919.
VARIANT 262 262 T -> K (in OTCD; mild; dbSNP:rs67333670).
{ECO:0000269|PubMed:10737985}.
/FTId=VAR_010608.
VARIANT 263 263 D -> G (in OTCD; dbSNP:rs72558443).
/FTId=VAR_004920.
VARIANT 263 263 D -> N (in OTCD; dbSNP:rs72558442).
{ECO:0000269|Ref.32}.
/FTId=VAR_004921.
VARIANT 264 264 T -> A (in OTCD; late onset; 8.9%
activity; dbSNP:rs72558444).
{ECO:0000269|PubMed:10737985,
ECO:0000269|PubMed:8112735}.
/FTId=VAR_004922.
VARIANT 264 264 T -> I (in OTCD; late onset;
dbSNP:rs67156896).
{ECO:0000269|PubMed:9452024}.
/FTId=VAR_004923.
VARIANT 265 265 W -> L (in OTCD; mild; dbSNP:rs72558446).
{ECO:0000269|PubMed:10737985}.
/FTId=VAR_010609.
VARIANT 267 267 S -> R (in OTCD; dbSNP:rs72558448).
{ECO:0000269|PubMed:9452024}.
/FTId=VAR_004924.
VARIANT 268 268 M -> T (in OTCD; late onset;
dbSNP:rs72558449).
/FTId=VAR_004925.
VARIANT 269 269 G -> E (in OTCD; neonatal;
dbSNP:rs72558450).
{ECO:0000269|PubMed:7474905}.
/FTId=VAR_004926.
VARIANT 270 270 Q -> R (in about 5% of population;
dbSNP:rs1800328).
{ECO:0000269|PubMed:10070627,
ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:6372096}.
/FTId=VAR_004927.
VARIANT 272 272 Missing (in OTCD; late onset).
{ECO:0000269|PubMed:8956045}.
/FTId=VAR_004928.
VARIANT 277 277 R -> Q (in OTCD; late onset;
dbSNP:rs66724222).
{ECO:0000269|PubMed:7951259,
ECO:0000269|PubMed:8081373}.
/FTId=VAR_004929.
VARIANT 277 277 R -> W (in OTCD; late onset;
dbSNP:rs72558454).
{ECO:0000269|PubMed:2347583,
ECO:0000269|PubMed:9065786}.
/FTId=VAR_004930.
VARIANT 301 301 L -> F (in OTCD; dbSNP:rs72558462).
{ECO:0000269|PubMed:11793483}.
/FTId=VAR_012654.
VARIANT 302 302 H -> L (in OTCD; female; late onset;
dbSNP:rs67993095).
{ECO:0000269|PubMed:8807340}.
/FTId=VAR_004931.
VARIANT 302 302 H -> Q (in OTCD; late onset;
dbSNP:rs67870244).
/FTId=VAR_004932.
VARIANT 302 302 H -> Y (in OTCD; neonatal;
dbSNP:rs72558463).
{ECO:0000269|PubMed:8956038}.
/FTId=VAR_004933.
VARIANT 303 303 C -> R (in OTCD; neonatal;
dbSNP:rs67468335).
{ECO:0000269|PubMed:9452049}.
/FTId=VAR_004934.
VARIANT 303 303 C -> Y (in OTCD; dbSNP:rs72558464).
/FTId=VAR_004935.
VARIANT 304 304 L -> F (in OTCD; dbSNP:rs72558465).
{ECO:0000269|PubMed:1480464}.
/FTId=VAR_004936.
VARIANT 305 305 P -> H (in OTCD; dbSNP:rs67501347).
{ECO:0000269|PubMed:11793483}.
/FTId=VAR_012655.
VARIANT 309 309 Missing (in OTCD; late onset).
{ECO:0000269|PubMed:7951259}.
/FTId=VAR_004937.
VARIANT 320 320 R -> L (in OTCD; dbSNP:rs72558474).
{ECO:0000269|PubMed:1671317}.
/FTId=VAR_004938.
VARIANT 326 326 E -> K (in OTCD; dbSNP:rs72558476).
{ECO:0000269|PubMed:10070627}.
/FTId=VAR_010610.
VARIANT 330 330 R -> G (in OTCD; dbSNP:rs72558478).
/FTId=VAR_004939.
VARIANT 333 333 T -> A. {ECO:0000269|PubMed:11793483}.
/FTId=VAR_012656.
VARIANT 336 336 A -> S (in OTCD; late onset;
dbSNP:rs72558486).
/FTId=VAR_004940.
VARIANT 337 337 V -> L (in OTCD; late onset;
dbSNP:rs72558487).
/FTId=VAR_004941.
VARIANT 339 339 V -> L (in OTCD; neonatal;
dbSNP:rs72558488).
/FTId=VAR_004942.
VARIANT 340 340 S -> P (in OTCD; late onset;
dbSNP:rs72558489).
{ECO:0000269|PubMed:9143919}.
/FTId=VAR_004943.
VARIANT 341 341 L -> P (in OTCD; dbSNP:rs72558490).
{ECO:0000269|PubMed:11793483}.
/FTId=VAR_012657.
VARIANT 343 343 T -> K (in OTCD; late onset;
dbSNP:rs72558491).
{ECO:0000269|PubMed:8956038}.
/FTId=VAR_004944.
VARIANT 345 345 Y -> C (in OTCD; neonatal;
dbSNP:rs72558492).
/FTId=VAR_004946.
VARIANT 345 345 Y -> D (in OTCD; dbSNP:rs66469337).
{ECO:0000269|PubMed:1480464}.
/FTId=VAR_004947.
VARIANT 354 354 F -> C (in OTCD; late onset;
dbSNP:rs72558495).
/FTId=VAR_004948.
CONFLICT 193 194 WI -> CF (in Ref. 1; AAA59975).
{ECO:0000305}.
HELIX 45 47 {ECO:0000244|PDB:1OTH}.
HELIX 50 68 {ECO:0000244|PDB:1OTH}.
TURN 76 79 {ECO:0000244|PDB:1OTH}.
STRAND 81 88 {ECO:0000244|PDB:1OTH}.
HELIX 92 103 {ECO:0000244|PDB:1OTH}.
STRAND 107 112 {ECO:0000244|PDB:1OTH}.
TURN 113 115 {ECO:0000244|PDB:1OTH}.
TURN 119 121 {ECO:0000244|PDB:1OTH}.
HELIX 124 134 {ECO:0000244|PDB:1OTH}.
STRAND 136 141 {ECO:0000244|PDB:1OTH}.
HELIX 145 154 {ECO:0000244|PDB:1OTH}.
STRAND 159 162 {ECO:0000244|PDB:1OTH}.
HELIX 169 183 {ECO:0000244|PDB:1OTH}.
STRAND 190 195 {ECO:0000244|PDB:1OTH}.
HELIX 199 205 {ECO:0000244|PDB:1OTH}.
TURN 206 208 {ECO:0000244|PDB:1OTH}.
HELIX 209 211 {ECO:0000244|PDB:1OTH}.
STRAND 214 218 {ECO:0000244|PDB:1OTH}.
HELIX 227 240 {ECO:0000244|PDB:1OTH}.
STRAND 244 248 {ECO:0000244|PDB:1OTH}.
HELIX 250 254 {ECO:0000244|PDB:1OTH}.
STRAND 258 262 {ECO:0000244|PDB:1OTH}.
HELIX 271 273 {ECO:0000244|PDB:1OTH}.
HELIX 274 280 {ECO:0000244|PDB:1OTH}.
TURN 281 283 {ECO:0000244|PDB:1OTH}.
HELIX 288 292 {ECO:0000244|PDB:1OTH}.
STRAND 299 302 {ECO:0000244|PDB:1OTH}.
TURN 308 310 {ECO:0000244|PDB:1OTH}.
HELIX 313 316 {ECO:0000244|PDB:1OTH}.
HELIX 323 342 {ECO:0000244|PDB:1OTH}.
SEQUENCE 354 AA; 39935 MW; AE15B734F6E27A3B CRC64;
MLFNLRILLN NAAFRNGHNF MVRNFRCGQP LQNKVQLKGR DLLTLKNFTG EEIKYMLWLS
ADLKFRIKQK GEYLPLLQGK SLGMIFEKRS TRTRLSTETG FALLGGHPCF LTTQDIHLGV
NESLTDTARV LSSMADAVLA RVYKQSDLDT LAKEASIPII NGLSDLYHPI QILADYLTLQ
EHYSSLKGLT LSWIGDGNNI LHSIMMSAAK FGMHLQAATP KGYEPDASVT KLAEQYAKEN
GTKLLLTNDP LEAAHGGNVL ITDTWISMGQ EEEKKKRLQA FQGYQVTMKT AKVAASDWTF
LHCLPRKPEE VDDEVFYSPR SLVFPEAENR KWTIMAVMVS LLTDYSPQLQ KPKF


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