OTC_HUMAN
ID OTC_HUMAN Reviewed; 354 AA.
AC P00480; A8K9P2; D3DWB0; Q3KNR1; Q6B0I1; Q9NYJ5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 238.
DE RecName: Full=Ornithine transcarbamylase, mitochondrial {ECO:0000305|PubMed:3895227, ECO:0000305|PubMed:6372096};
DE Short=OTCase {ECO:0000303|PubMed:6372096};
DE EC=2.1.3.3 {ECO:0000269|PubMed:2556444, ECO:0000269|PubMed:6372096, ECO:0000269|PubMed:8112735};
DE AltName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE Flags: Precursor;
GN Name=OTC {ECO:0000312|HGNC:HGNC:8512};
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], VARIANTS PRO-111 AND ARG-270, FUNCTION,
RP CATALYTIC ACTIVITY, AND TRANSIT PEPTIDE.
RC TISSUE=Liver;
RX PubMed=6372096; DOI=10.1126/science.6372096;
RA Horwich A.L., Fenton W.A., Williams K.R., Kalousek F., Kraus J.P.,
RA Doolittle R.F., Konigsberg W., Rosenberg L.E.;
RT "Structure and expression of a complementary DNA for the nuclear coded
RT precursor of human mitochondrial ornithine transcarbamylase.";
RL Science 224:1068-1074(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-101.
RC TISSUE=Liver;
RX PubMed=2836378; DOI=10.1093/oxfordjournals.jbchem.a122265;
RA Hata A., Tsuzuki T., Shimada K., Takiguchi M., Mori M., Matsuda I.;
RT "Structure of the human ornithine transcarbamylase gene.";
RL J. Biochem. 103:302-308(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-46.
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-15; ARG-23 AND ARG-26.
RX PubMed=3895227; DOI=10.1073/pnas.82.15.4930;
RA Horwich A.L., Kalousek F., Rosenberg L.E.;
RT "Arginine in the leader peptide is required for both import and proteolytic
RT cleavage of a mitochondrial precursor.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4930-4933(1985).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX PubMed=3782067; DOI=10.1093/oxfordjournals.jbchem.a121764;
RA Hata A., Tsuzuki T., Shimada K., Takiguchi M., Mori M., Matsuda I.;
RT "Isolation and characterization of the human ornithine transcarbamylase
RT gene: structure of the 5'-end region.";
RL J. Biochem. 100:717-725(1986).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 269-289, AND VARIANT OTCD GLN-277.
RX PubMed=8081373; DOI=10.1093/hmg/3.5.831;
RA Gilbert-Dussardier B., Rabier D., Strautnieks S., Segues B.,
RA Bonnefont J.-P., Munnich A.;
RT "A novel arginine (245) to glutamine change in exon 8 of the ornithine
RT carbamoyl transferase gene in two unrelated children presenting with late
RT onset deficiency and showing the same enzymatic pattern.";
RL Hum. Mol. Genet. 3:831-832(1994).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP CHARACTERIZATION OF VARIANTS OTCD ARG-195; VAL-196 AND ALA-264, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RX PubMed=8112735; DOI=10.1007/bf00210596;
RA Matsuura T., Hoshide R., Setoyama C., Komaki S., Kiwaki K., Endo F.,
RA Nishikawa S., Matsuda I.;
RT "Expression of four mutant human ornithine transcarbamylase genes in
RT cultured Cos 1 cells relates to clinical phenotypes.";
RL Hum. Genet. 93:129-134(1994).
RN [12]
RP ACETYLATION AT LYS-88, AND ACTIVITY REGULATION.
RX PubMed=19318352; DOI=10.1074/jbc.m901921200;
RA Yu W., Lin Y., Yao J., Huang W., Lei Q., Xiong Y., Zhao S., Guan K.L.;
RT "Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase
RT activity in response to nutrient signals.";
RL J. Biol. Chem. 284:13669-13675(2009).
RN [13] {ECO:0007744|PDB:1OTH}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG
RP N-(PHOSPHONOACETYL)-L-ORNITHINE.
RX PubMed=9852088; DOI=10.1074/jbc.273.51.34247;
RA Shi D., Morizono H., Ha Y., Aoyagi M., Tuchman M., Allewell N.M.;
RT "1.85-A resolution crystal structure of human ornithine transcarbamoylase
RT complexed with N-phosphonacetyl-L-ornithine. Catalytic mechanism and
RT correlation with inherited deficiency.";
RL J. Biol. Chem. 273:34247-34254(1998).
RN [14] {ECO:0007744|PDB:1C9Y}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH L-2-AMINOPENTANOATE
RP AND CARBAMOYL PHOSPHATE, ACTIVE SITE, AND REACTION MECHANISM.
RX PubMed=10813810;
RX DOI=10.1002/(sici)1097-0134(20000601)39:4<271::aid-prot10>3.0.co;2-e;
RA Shi D., Morizono H., Aoyagi M., Tuchman M., Allewell N.M.;
RT "Crystal structure of human ornithine transcarbamylase complexed with
RT carbamoyl phosphate and L-norvaline at 1.9 A resolution.";
RL Proteins 39:271-277(2000).
RN [15]
RP REVIEW ON VARIANTS.
RX PubMed=8364586; DOI=10.1002/humu.1380020304;
RA Tuchman M.;
RT "Mutations and polymorphisms in the human ornithine transcarbamylase
RT gene.";
RL Hum. Mutat. 2:174-178(1993).
RN [16]
RP REVIEW ON VARIANTS.
RX PubMed=7627182; DOI=10.1002/humu.1380050404;
RA Tuchman M., Plante R.J.;
RT "Mutations and polymorphisms in the human ornithine transcarbamylase gene:
RT mutation update addendum.";
RL Hum. Mutat. 5:293-295(1995).
RN [17]
RP REVIEW ON VARIANTS, AND 3D-STRUCTURE MODELING.
RX PubMed=8544185; DOI=10.1136/jmg.32.9.680;
RA Tuchman M., Morizono H., Reish O., Yuan X., Allewell N.M.;
RT "The molecular basis of ornithine transcarbamylase deficiency: modelling
RT the human enzyme and the effects of mutations.";
RL J. Med. Genet. 32:680-688(1995).
RN [18]
RP VARIANT OTCD GLN-141.
RX PubMed=3170748; DOI=10.1172/jci113738;
RA Maddalena A., Spence J.E., O'Brien W.E., Nussbaum R.L.;
RT "Characterization of point mutations in the same arginine codon in three
RT unrelated patients with ornithine transcarbamylase deficiency.";
RL J. Clin. Invest. 82:1353-1358(1988).
RN [19]
RP VARIANT OTCD GLN-141, CHARACTERIZATION OF VARIANT OTCD GLN-141, FUNCTION,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=2556444; DOI=10.1172/jci114360;
RA Lee J.T., Nussbaum R.L.;
RT "An arginine to glutamine mutation in residue 109 of human ornithine
RT transcarbamylase completely abolishes enzymatic activity in Cos1 cells.";
RL J. Clin. Invest. 84:1762-1766(1989).
RN [20]
RP VARIANTS OTCD GLN-26; PRO-45 AND GLU-216, AND VARIANT ARG-46.
RX PubMed=2474822; DOI=10.1073/pnas.86.15.5888;
RA Grompe M., Muzny D.M., Caskey C.T.;
RT "Scanning detection of mutations in human ornithine transcarbamoylase by
RT chemical mismatch cleavage.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5888-5892(1989).
RN [21]
RP VARIANT OTCD TRP-277.
RX PubMed=2347583; DOI=10.1016/0888-7543(90)90537-5;
RA Finkelstein J.E., Francomano C.A., Brusilow S.W., Traystman M.D.;
RT "Use of denaturing gradient gel electrophoresis for detection of mutation
RT and prospective diagnosis in late onset ornithine transcarbamylase
RT deficiency.";
RL Genomics 7:167-172(1990).
RN [22]
RP VARIANTS OTCD GLN-92 AND LEU-320, AND VARIANT PRO-111.
RX PubMed=1671317;
RA Grompe M., Caskey C.T., Fenwick R.G. Jr.;
RT "Improved molecular diagnostics for ornithine transcarbamylase
RT deficiency.";
RL Am. J. Hum. Genet. 48:212-222(1991).
RN [23]
RP VARIANT OTCD LEU-225.
RX PubMed=1721894; DOI=10.1007/bf00206063;
RA Hentzen D., Pelet A., Feldman D., Rabier D., Berthelot J., Munnich A.;
RT "Fatal hyperammonemia resulting from a C-to-T mutation at a MspI site of
RT the ornithine transcarbamylase gene.";
RL Hum. Genet. 88:153-156(1991).
RN [24]
RP VARIANTS OTCD GLU-79; THR-94; PHE-304 AND ASP-345.
RX PubMed=1480464; DOI=10.1203/00006450-199211000-00024;
RA Tuchman M., Holzknecht R.A., Gueron A.B., Berry S.A., Tsai M.Y.;
RT "Six new mutations in the ornithine transcarbamylase gene detected by
RT single-strand conformational polymorphism.";
RL Pediatr. Res. 32:600-604(1992).
RN [25]
RP VARIANT OTCD PRO-140.
RX PubMed=8099056; DOI=10.1007/bf00217350;
RA Tsai M.Y., Holzknecht R.A., Tuchman M.;
RT "Single-strand conformational polymorphism and direct sequencing applied to
RT carrier testing in families with ornithine transcarbamylase deficiency.";
RL Hum. Genet. 91:321-325(1993).
RN [26]
RP VARIANTS OTCD LEU-117; LEU-182 AND CYS-203.
RX PubMed=8019569; DOI=10.1002/humu.1380030325;
RA Tuchman M., Plante R.J., Giguere Y., Lemieux B.;
RT "The ornithine transcarbamylase gene: new 'private' mutations in four
RT patients and study of a polymorphism.";
RL Hum. Mutat. 3:318-320(1994).
RN [27]
RP VARIANTS OTCD GLY-126; HIS-129 AND MET-172.
RX PubMed=8081398; DOI=10.1002/humu.1380030415;
RA Matsuura T., Hoshide R., Kiwaki K., Komaki S., Koike E., Endo F.,
RA Oyanagi K., Suzuki Y., Kato I., Ishikawa K., Yoda H., Kamitani S.,
RA Sakaki Y., Matsuda I.;
RT "Four newly identified ornithine transcarbamylase (OTC) mutations (D126G,
RT R129H, I172M and W332X) in Japanese male patients with early-onset OTC
RT deficiency.";
RL Hum. Mutat. 3:402-406(1994).
RN [28]
RP VARIANTS OTCD HIS-40; HIS-129; ARG-195; THR-225; GLN-277 AND GLU-309 DEL.
RX PubMed=7951259; DOI=10.1002/humu.1380040109;
RA Tuchman M., Plante R.J., McCann M.T., Qureshi A.A.;
RT "Seven new mutations in the human ornithine transcarbamylase gene.";
RL Hum. Mutat. 4:57-60(1994).
RN [29]
RP VARIANTS OTCD THR-159 AND VAL-209.
RX PubMed=8530002; DOI=10.1007/bf00197410;
RA Garcia-Perez M.A., Sanjurjo P., Briones P., Garcia-Munoz M.J., Rubio V.;
RT "A splicing mutation, a nonsense mutation (Y167X) and two missense
RT mutations (I159T and A209V) in Spanish patients with ornithine
RT transcarbamylase deficiency.";
RL Hum. Genet. 96:549-551(1995).
RN [30]
RP VARIANT OTCD GLU-269.
RX PubMed=7474905; DOI=10.1007/bf00710430;
RA Zimmer K.P., Matsuura T., Colombo J.-P., Koch H.G., Ullrich K., Deufel T.,
RA Harms E., Matsuda I.;
RT "A novel point mutation at codon 269 of the ornithine transcarbamylase
RT (OTC) gene causing neonatal onset of OTC deficiency.";
RL J. Inherit. Metab. Dis. 18:356-357(1995).
RN [31]
RP VARIANTS OTCD MET-125; ARG-188; VAL-209 AND LEU-302.
RX PubMed=8807340;
RX DOI=10.1002/(sici)1098-1004(1996)8:1<74::aid-humu11>3.0.co;2-o;
RA Gilbert-Dussardier B., Segues B., Rozet J.-M., Rabier D., Calvas P.,
RA de Lumley L., Bonnefont J.-P., Munnich A.;
RT "Partial duplication [dup. TCAC (178)] and novel point mutations (T125M,
RT G188R, A209V, and H302L) of the ornithine transcarbamylase gene in
RT congenital hyperammonemia.";
RL Hum. Mutat. 8:74-76(1996).
RN [32]
RP VARIANTS OTCD HIS-40; ASN-88; TYR-202 AND ASN-263.
RA Guardamagna O., Gatti E., Parini R., Plante R.J., Tuchman M.;
RT "Genotype-phenotype correlations in ornithine transcarbamylase
RT deficiency.";
RL Enzyme Protein 49:191-191(1996).
RN [33]
RP VARIANTS OTCD ASN-88; CYS-176; ALA-220; TYR-302 AND LYS-343.
RX PubMed=8956038;
RX DOI=10.1002/(sici)1098-1004(1996)8:4<333::aid-humu6>3.0.co;2-8;
RA Leibundgut E.O., Wermuth B., Colombo J.-P., Liechti-Gallati S.;
RT "Ornithine transcarbamylase deficiency: characterization of gene mutations
RT and polymorphisms.";
RL Hum. Mutat. 8:333-339(1996).
RN [34]
RP VARIANT OTCD GLU-272 DEL.
RX PubMed=8956045;
RX DOI=10.1002/(sici)1098-1004(1996)8:4<373::aid-humu13>3.0.co;2-#;
RA Segues B., Saugier Veber P., Rabier D., Calvas P., Saudubray J.-M.,
RA Gilbert-Dussardier B., Bonnefont J.-P., Munnich A.;
RT "A 3-base pair in-frame deletion in exon 8 (delGlu272/273) of the ornithine
RT transcarbamylase gene in late-onset hyperammonemic coma.";
RL Hum. Mutat. 8:373-374(1996).
RN [35]
RP VARIANTS OTCD ILE-44; GLN-141 AND TYR-214, AND VARIANT LEU-101.
RX PubMed=8830175; DOI=10.1007/bf01799346;
RA Yoo H.-W., Kim G.-H., Lee D.-H.;
RT "Identification of new mutations in the ornithine transcarbamylase (OTC)
RT gene in Korean families.";
RL J. Inherit. Metab. Dis. 19:31-42(1996).
RN [36]
RP VARIANTS OTCD.
RX PubMed=9286441;
RX DOI=10.1002/(sici)1096-8628(19970905)71:4<378::aid-ajmg2>3.0.co;2-q;
RA Matsuda I., Tanase S.;
RT "The ornithine transcarbamylase (OTC) gene: mutations in 50 Japanese
RT families with OTC deficiency.";
RL Am. J. Med. Genet. 71:378-383(1997).
RN [37]
RP CHARACTERIZATION OF VARIANT OTCD TRP-277.
RX PubMed=9065786; DOI=10.1042/bj3220625;
RA Morizono H., Tuchman M., Rajagopal B.S., McCann M.T., Listrom C.D.,
RA Yuan X., Venugopal D., Barany G., Allewell N.M.;
RT "Expression, purification and kinetic characterization of wild-type human
RT ornithine transcarbamylase and a recurrent mutant that produces 'late
RT onset' hyperammonaemia.";
RL Biochem. J. 322:625-631(1997).
RN [38]
RP VARIANTS OTCD PRO-63; ASP-100; ASP-183; LYS-213 AND PRO-340, AND VARIANT
RP PHE-43.
RX PubMed=9143919;
RX DOI=10.1002/(sici)1098-1004(1997)9:5<409::aid-humu5>3.0.co;2-z;
RA Oppliger Leibundgut E., Liechti-Gallati S., Colombo J.-P., Wermuth B.;
RT "Ornithine transcarbamylase deficiency: ten new mutations and high
RT proportion of de novo mutations in heterozygous females.";
RL Hum. Mutat. 9:409-411(1997).
RN [39]
RP VARIANTS OTCD.
RX PubMed=9266388; DOI=10.1023/a:1005301513465;
RA Tuchman M., Morizono H., Rajagopal B.S., Plante R.J., Allewell N.M.;
RT "Identification of 'private' mutations in patients with ornithine
RT transcarbamylase deficiency.";
RL J. Inherit. Metab. Dis. 20:525-527(1997).
RN [40]
RP VARIANTS OTCD 178-THE-LEU-179 DEL; HIS-180; PRO-201; ARG-207; ILE-264 AND
RP ARG-267.
RX PubMed=9452024; DOI=10.1002/humu.1380110103;
RA Shimadzu M., Matsumoto H., Matsuura T., Kobayashi K., Komaki S., Kiwaki K.,
RA Hoshide R., Endo F., Saheki T., Matsuda I.;
RT "Ten novel mutations of the ornithine transcarbamylase (OTC) gene in OTC
RT deficiency.";
RL Hum. Mutat. Suppl. 1:S5-S7(1998).
RN [41]
RP VARIANTS OTCD CYS-39; GLN-244 AND ARG-303.
RX PubMed=9452049; DOI=10.1002/humu.1380110128;
RA Calvas P., Seques B., Rozet J.-M., Rabier D., Bonnefont J.-P., Munnich A.;
RT "Novel intragenic deletions and point mutations of the ornithine
RT transcarbamylase gene in congenital hyperammonemia.";
RL Hum. Mutat. Suppl. 1:S81-S84(1998).
RN [42]
RP VARIANT OTCD ASP-55.
RX PubMed=9452065; DOI=10.1002/humu.1380110144;
RA Nishiyori A., Yoshino M., Tananari Y., Matsuura T., Hoshide R., Matsuda I.,
RA Mori M., Kato H.;
RT "Y55D mutation in ornithine transcarbamylase associated with late-onset
RT hyperammonemia in a male.";
RL Hum. Mutat. Suppl. 1:S131-S133(1998).
RN [43]
RP VARIANT OTCD ASP-83.
RA Bartholomew D.W., McClellan J.;
RT "A novel missense mutation in the human ornithine transcarbamylase gene.";
RL Hum. Mutat. 12:220-220(1998).
RN [44]
RP VARIANTS OTCD PHE-172; VAL-188 AND ARG-197.
RX PubMed=10502831;
RX DOI=10.1002/(sici)1098-1004(199910)14:4<352::aid-humu15>3.0.co;2-d;
RA Climent C., Garcia-Perez M.A., Sanjurjo P., Ruiz-Sanz J.-I., Vilaseca M.A.,
RA Pineda M., Campistol J., Rubio V.;
RT "Identification of a cytogenetic deletion and of four novel mutations
RT (Q69X, I172F, G188V, G197R) affecting the gene for ornithine
RT transcarbamylase (OTC) in Spanish patients with OTC deficiency.";
RL Hum. Mutat. 14:352-353(1999).
RN [45]
RP VARIANTS OTCD LYS-198; VAL-209 AND LYS-326, AND VARIANT ARG-270.
RX PubMed=10070627; DOI=10.1023/a:1005476021549;
RA Popowska E., Ciara E., Rokicki D., Pronicka E.;
RT "Three novel and one recurrent ornithine carbamoyltransferase gene
RT mutations in Polish patients.";
RL J. Inherit. Metab. Dis. 22:92-93(1999).
RN [46]
RP VARIANTS OTCD LYS-262; ALA-264 AND LEU-265.
RX PubMed=10737985;
RX DOI=10.1002/(sici)1098-1004(200004)15:4<380::aid-humu12>3.0.co;2-q;
RA Giorgi M., Morrone A., Donati M.A., Ciani F., Bardelli T., Biasucci G.,
RA Zammarchi E.;
RT "Lymphocyte mRNA analysis of the ornithine transcarbamylase gene in Italian
RT OTCD male patients and manifesting carriers: identification of novel
RT mutations.";
RL Hum. Mutat. 15:380-381(2000).
RN [47]
RP VARIANTS OTCD SER-160; PHE-191; ILE-206; PHE-301; HIS-305 AND PRO-341, AND
RP VARIANT ALA-333.
RX PubMed=11793483; DOI=10.1002/humu.9011;
RA Climent C., Rubio V.;
RT "Identification of seven novel missense mutations, two splice-site
RT mutations, two microdeletions and a polymorphic amino acid substitution in
RT the gene for ornithine transcarbamylase (OTC) in patients with OTC
RT deficiency.";
RL Hum. Mutat. 19:185-186(2002).
RN [48]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-270.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Catalyzes the second step of the urea cycle, the condensation
CC of carbamoyl phosphate with L-ornithine to form L-citrulline
CC (PubMed:6372096, PubMed:8112735, PubMed:2556444). The urea cycle
CC ensures the detoxification of ammonia by converting it to urea for
CC excretion (PubMed:2556444). {ECO:0000269|PubMed:2556444,
CC ECO:0000269|PubMed:6372096, ECO:0000269|PubMed:8112735}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000269|PubMed:2556444,
CC ECO:0000269|PubMed:6372096, ECO:0000269|PubMed:8112735};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19515;
CC Evidence={ECO:0000305|PubMed:6372096};
CC -!- ACTIVITY REGULATION: Negatively regulated by lysine acetylation.
CC {ECO:0000269|PubMed:19318352}.
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-citrulline from L-ornithine
CC and carbamoyl phosphate: step 1/1. {ECO:0000269|PubMed:2556444}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10813810,
CC ECO:0000269|PubMed:9852088}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:3895227}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in liver and intestinal mucosa.
CC -!- PTM: Acetylation at Lys-88 negatively regulates ornithine
CC carbamoyltransferase activity in response to nutrient signals.
CC {ECO:0000269|PubMed:19318352}.
CC -!- DISEASE: Ornithine carbamoyltransferase deficiency (OTCD) [MIM:311250]:
CC An X-linked disorder of the urea cycle which causes a form of
CC hyperammonemia. Mutations with no residual enzyme activity are always
CC expressed in hemizygote males by a very severe neonatal hyperammonemic
CC coma that generally proves to be fatal. Heterozygous females are either
CC asymptomatic or express orotic aciduria spontaneously or after protein
CC intake. The disorder is treatable with supplemental dietary arginine
CC and low protein diet. The arbitrary classification of patients into the
CC 'neonatal' group (clinical hyperammonemia in the first few days of
CC life) and 'late' onset (clinical presentation after the neonatal
CC period) has been used to differentiate severe from mild forms.
CC {ECO:0000269|PubMed:10070627, ECO:0000269|PubMed:10502831,
CC ECO:0000269|PubMed:10737985, ECO:0000269|PubMed:11793483,
CC ECO:0000269|PubMed:1480464, ECO:0000269|PubMed:1671317,
CC ECO:0000269|PubMed:1721894, ECO:0000269|PubMed:2347583,
CC ECO:0000269|PubMed:2474822, ECO:0000269|PubMed:2556444,
CC ECO:0000269|PubMed:3170748, ECO:0000269|PubMed:7474905,
CC ECO:0000269|PubMed:7951259, ECO:0000269|PubMed:8019569,
CC ECO:0000269|PubMed:8081373, ECO:0000269|PubMed:8081398,
CC ECO:0000269|PubMed:8099056, ECO:0000269|PubMed:8112735,
CC ECO:0000269|PubMed:8530002, ECO:0000269|PubMed:8807340,
CC ECO:0000269|PubMed:8830175, ECO:0000269|PubMed:8956038,
CC ECO:0000269|PubMed:8956045, ECO:0000269|PubMed:9065786,
CC ECO:0000269|PubMed:9143919, ECO:0000269|PubMed:9266388,
CC ECO:0000269|PubMed:9286441, ECO:0000269|PubMed:9452024,
CC ECO:0000269|PubMed:9452049, ECO:0000269|PubMed:9452065,
CC ECO:0000269|Ref.32, ECO:0000269|Ref.43}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
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DR EMBL; K02100; AAA59975.1; -; mRNA.
DR EMBL; D00230; BAA00161.1; -; Genomic_DNA.
DR EMBL; AK292757; BAF85446.1; -; mRNA.
DR EMBL; AF241726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL607040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471141; EAW59439.1; -; Genomic_DNA.
DR EMBL; CH471141; EAW59440.1; -; Genomic_DNA.
DR EMBL; BC074745; AAH74745.1; -; mRNA.
DR EMBL; BC107153; AAI07154.1; -; mRNA.
DR EMBL; BC107154; AAI07155.1; -; mRNA.
DR EMBL; BC114496; AAI14497.1; -; mRNA.
DR EMBL; M11235; AAA59976.1; -; Genomic_DNA.
DR EMBL; D00095; BAA00058.1; -; Genomic_DNA.
DR EMBL; X04443; CAA28039.1; -; Genomic_DNA.
DR EMBL; S73640; AAB31859.1; -; Genomic_DNA.
DR CCDS; CCDS14247.1; -.
DR PIR; A41444; OWHU.
DR RefSeq; NP_000522.3; NM_000531.5.
DR PDB; 1C9Y; X-ray; 1.90 A; A=34-354.
DR PDB; 1EP9; X-ray; 2.40 A; A=34-354.
DR PDB; 1FVO; X-ray; 2.60 A; A/B=34-354.
DR PDB; 1OTH; X-ray; 1.85 A; A=34-354.
DR PDBsum; 1C9Y; -.
DR PDBsum; 1EP9; -.
DR PDBsum; 1FVO; -.
DR PDBsum; 1OTH; -.
DR AlphaFoldDB; P00480; -.
DR SMR; P00480; -.
DR BioGRID; 111050; 142.
DR CORUM; P00480; -.
DR IntAct; P00480; 11.
DR STRING; 9606.ENSP00000039007; -.
DR BindingDB; P00480; -.
DR ChEMBL; CHEMBL2222; -.
DR DrugBank; DB00155; Citrulline.
DR DrugBank; DB02011; N-(Phosphonoacetyl)-L-Ornithine.
DR DrugBank; DB04185; Norvaline.
DR DrugBank; DB00129; Ornithine.
DR iPTMnet; P00480; -.
DR PhosphoSitePlus; P00480; -.
DR BioMuta; OTC; -.
DR DMDM; 84028235; -.
DR REPRODUCTION-2DPAGE; P00480; -.
DR jPOST; P00480; -.
DR MassIVE; P00480; -.
DR MaxQB; P00480; -.
DR PaxDb; P00480; -.
DR PeptideAtlas; P00480; -.
DR PRIDE; P00480; -.
DR ProteomicsDB; 51254; -.
DR Antibodypedia; 336; 736 antibodies from 30 providers.
DR DNASU; 5009; -.
DR Ensembl; ENST00000039007.5; ENSP00000039007.4; ENSG00000036473.8.
DR GeneID; 5009; -.
DR KEGG; hsa:5009; -.
DR MANE-Select; ENST00000039007.5; ENSP00000039007.4; NM_000531.6; NP_000522.3.
DR UCSC; uc004def.5; human.
DR CTD; 5009; -.
DR DisGeNET; 5009; -.
DR GeneCards; OTC; -.
DR GeneReviews; OTC; -.
DR HGNC; HGNC:8512; OTC.
DR HPA; ENSG00000036473; Group enriched (intestine, liver).
DR MalaCards; OTC; -.
DR MIM; 300461; gene.
DR MIM; 311250; phenotype.
DR neXtProt; NX_P00480; -.
DR OpenTargets; ENSG00000036473; -.
DR Orphanet; 664; Ornithine transcarbamylase deficiency.
DR PharmGKB; PA32840; -.
DR VEuPathDB; HostDB:ENSG00000036473; -.
DR eggNOG; KOG1504; Eukaryota.
DR GeneTree; ENSGT00510000047417; -.
DR HOGENOM; CLU_043846_3_0_1; -.
DR InParanoid; P00480; -.
DR OMA; DGNNVCN; -.
DR OrthoDB; 1404554at2759; -.
DR PhylomeDB; P00480; -.
DR TreeFam; TF352580; -.
DR BioCyc; MetaCyc:HS00516-MON; -.
DR BRENDA; 2.1.3.3; 2681.
DR PathwayCommons; P00480; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-70635; Urea cycle.
DR SABIO-RK; P00480; -.
DR SignaLink; P00480; -.
DR SIGNOR; P00480; -.
DR UniPathway; UPA00158; UER00271.
DR BioGRID-ORCS; 5009; 4 hits in 701 CRISPR screens.
DR ChiTaRS; OTC; human.
DR EvolutionaryTrace; P00480; -.
DR GeneWiki; Ornithine_transcarbamylase; -.
DR GenomeRNAi; 5009; -.
DR Pharos; P00480; Tchem.
DR PRO; PR:P00480; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P00480; protein.
DR Bgee; ENSG00000036473; Expressed in jejunal mucosa and 91 other tissues.
DR ExpressionAtlas; P00480; baseline and differential.
DR Genevisible; P00480; HS.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0016597; F:amino acid binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0042301; F:phosphate ion binding; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0097272; P:ammonium homeostasis; IMP:BHF-UCL.
DR GO; GO:0055081; P:anion homeostasis; IEA:Ensembl.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019240; P:citrulline biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0007494; P:midgut development; IEA:Ensembl.
DR GO; GO:0006593; P:ornithine catabolic process; IDA:BHF-UCL.
DR GO; GO:0070781; P:response to biotin; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
DR GO; GO:0000050; P:urea cycle; IDA:BHF-UCL.
DR Gene3D; 3.40.50.1370; -; 2.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR002292; Orn/put_carbamltrans.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00102; OTCASE.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00658; orni_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis; Arginine biosynthesis;
KW Disease variant; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transferase; Transit peptide; Urea cycle.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:6372096"
FT CHAIN 33..354
FT /note="Ornithine transcarbamylase, mitochondrial"
FT /id="PRO_0000020334"
FT ACT_SITE 303
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:10813810"
FT BINDING 90..93
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10813810,
FT ECO:0007744|PDB:1C9Y"
FT BINDING 141
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10813810,
FT ECO:0007744|PDB:1C9Y"
FT BINDING 168
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10813810,
FT ECO:0007744|PDB:1C9Y"
FT BINDING 171
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10813810,
FT ECO:0007744|PDB:1C9Y"
FT BINDING 199
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000305|PubMed:10813810,
FT ECO:0007744|PDB:1C9Y"
FT BINDING 263
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000305|PubMed:10813810,
FT ECO:0007744|PDB:1C9Y"
FT BINDING 267
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000305|PubMed:10813810,
FT ECO:0007744|PDB:1C9Y"
FT BINDING 268
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000305|PubMed:10813810,
FT ECO:0007744|PDB:1C9Y"
FT BINDING 303..304
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10813810,
FT ECO:0007744|PDB:1C9Y"
FT BINDING 330
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10813810,
FT ECO:0007744|PDB:1C9Y"
FT MOD_RES 70
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 70
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 80
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 88
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19318352"
FT MOD_RES 88
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 144
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 144
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 221
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 221
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 231
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 231
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 238
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 238
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 274
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 289
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 292
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 292
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 307
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 307
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT VARIANT 26
FT /note="R -> Q (in OTCD; dbSNP:rs68031618)"
FT /evidence="ECO:0000269|PubMed:2474822"
FT /id="VAR_004843"
FT VARIANT 39
FT /note="G -> C (in OTCD; late onset; dbSNP:rs72554306)"
FT /evidence="ECO:0000269|PubMed:9452049"
FT /id="VAR_004844"
FT VARIANT 40
FT /note="R -> C (in OTCD; late onset; dbSNP:rs72554307)"
FT /id="VAR_004845"
FT VARIANT 40
FT /note="R -> H (in OTCD; late onset; dbSNP:rs72554308)"
FT /evidence="ECO:0000269|PubMed:7951259, ECO:0000269|Ref.32"
FT /id="VAR_004846"
FT VARIANT 43
FT /note="L -> F (in dbSNP:rs72554309)"
FT /evidence="ECO:0000269|PubMed:9143919"
FT /id="VAR_004847"
FT VARIANT 44
FT /note="T -> I (in OTCD; dbSNP:rs72554310)"
FT /evidence="ECO:0000269|PubMed:8830175"
FT /id="VAR_004848"
FT VARIANT 45
FT /note="L -> P (in OTCD; dbSNP:rs72554312)"
FT /evidence="ECO:0000269|PubMed:2474822"
FT /id="VAR_004849"
FT VARIANT 45
FT /note="L -> V (in OTCD; dbSNP:rs72554311)"
FT /id="VAR_004850"
FT VARIANT 46
FT /note="K -> R (in dbSNP:rs1800321)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2474822"
FT /id="VAR_004851"
FT VARIANT 47
FT /note="N -> I (in OTCD; neonatal; dbSNP:rs67939655)"
FT /id="VAR_004852"
FT VARIANT 50
FT /note="G -> R (in OTCD; late onset; dbSNP:rs67486158)"
FT /id="VAR_004853"
FT VARIANT 55
FT /note="Y -> D (in OTCD; late onset; dbSNP:rs72554319)"
FT /evidence="ECO:0000269|PubMed:9452065"
FT /id="VAR_004854"
FT VARIANT 56
FT /note="M -> T (in OTCD; late onset; dbSNP:rs72554320)"
FT /id="VAR_004855"
FT VARIANT 60
FT /note="S -> L (in OTCD; dbSNP:rs72554323)"
FT /id="VAR_004856"
FT VARIANT 63
FT /note="L -> P (in OTCD; late onset; dbSNP:rs72554324)"
FT /evidence="ECO:0000269|PubMed:9143919"
FT /id="VAR_004857"
FT VARIANT 79
FT /note="G -> E (in OTCD; dbSNP:rs72554331)"
FT /evidence="ECO:0000269|PubMed:1480464"
FT /id="VAR_004858"
FT VARIANT 82
FT /note="Missing (in OTCD)"
FT /id="VAR_004859"
FT VARIANT 83
FT /note="G -> D (in OTCD; dbSNP:rs72554337)"
FT /evidence="ECO:0000269|Ref.43"
FT /id="VAR_004860"
FT VARIANT 83
FT /note="G -> R (in OTCD; neonatal; dbSNP:rs72554336)"
FT /id="VAR_004861"
FT VARIANT 87
FT /note="E -> K (in OTCD; dbSNP:rs72554338)"
FT /id="VAR_004862"
FT VARIANT 88
FT /note="K -> N (in OTCD; late onset; dbSNP:rs72554339)"
FT /evidence="ECO:0000269|PubMed:8956038, ECO:0000269|Ref.32"
FT /id="VAR_004863"
FT VARIANT 90
FT /note="S -> R (in OTCD; dbSNP:rs72554342)"
FT /id="VAR_004864"
FT VARIANT 92
FT /note="R -> Q (in OTCD; dbSNP:rs66550389)"
FT /evidence="ECO:0000269|PubMed:1671317"
FT /id="VAR_004865"
FT VARIANT 93
FT /note="T -> A (in OTCD; late onset; dbSNP:rs72554344)"
FT /id="VAR_004866"
FT VARIANT 94
FT /note="R -> T (in OTCD; dbSNP:rs72554345)"
FT /evidence="ECO:0000269|PubMed:1480464"
FT /id="VAR_004867"
FT VARIANT 100
FT /note="G -> D (in OTCD; late onset; dbSNP:rs72554349)"
FT /evidence="ECO:0000269|PubMed:9143919"
FT /id="VAR_004868"
FT VARIANT 101
FT /note="F -> L (in dbSNP:rs1133135)"
FT /evidence="ECO:0000269|PubMed:2836378,
FT ECO:0000269|PubMed:8830175"
FT /id="VAR_004869"
FT VARIANT 102
FT /note="A -> E (in OTCD; dbSNP:rs72554350)"
FT /id="VAR_004870"
FT VARIANT 111
FT /note="L -> P (in dbSNP:rs1800324)"
FT /evidence="ECO:0000269|PubMed:1671317,
FT ECO:0000269|PubMed:6372096"
FT /id="VAR_004871"
FT VARIANT 117
FT /note="H -> L (in OTCD; dbSNP:rs66539573)"
FT /evidence="ECO:0000269|PubMed:8019569"
FT /id="VAR_004872"
FT VARIANT 117
FT /note="H -> R (in OTCD; late onset; dbSNP:rs66539573)"
FT /id="VAR_004873"
FT VARIANT 125
FT /note="T -> M (in OTCD; neonatal; dbSNP:rs72554356)"
FT /evidence="ECO:0000269|PubMed:8807340"
FT /id="VAR_004874"
FT VARIANT 126
FT /note="D -> G (in OTCD; early onset; loss of ornithine
FT carbamoyltransferase activity; 0.9% of wild-type activity;
FT dbSNP:rs72554358)"
FT /evidence="ECO:0000269|PubMed:8081398"
FT /id="VAR_004875"
FT VARIANT 129
FT /note="R -> H (in OTCD; early onset; decreased ornithine
FT carbamoyltransferase activity; 2.1% of wild-type activity;
FT dbSNP:rs66656800)"
FT /evidence="ECO:0000269|PubMed:7951259,
FT ECO:0000269|PubMed:8081398"
FT /id="VAR_004876"
FT VARIANT 139
FT /note="L -> S (in OTCD; dbSNP:rs72556259)"
FT /id="VAR_004877"
FT VARIANT 140
FT /note="A -> P (in OTCD; late onset; dbSNP:rs72556260)"
FT /evidence="ECO:0000269|PubMed:8099056"
FT /id="VAR_010605"
FT VARIANT 141
FT /note="R -> P (in OTCD; dbSNP:rs68026851)"
FT /id="VAR_004878"
FT VARIANT 141
FT /note="R -> Q (in OTCD; most common variant; loss of
FT ornithine carbamoyltransferase activity; activity is 100-
FT fold lower; dbSNP:rs68026851)"
FT /evidence="ECO:0000269|PubMed:2556444,
FT ECO:0000269|PubMed:3170748, ECO:0000269|PubMed:8830175"
FT /id="VAR_004879"
FT VARIANT 148
FT /note="L -> F (in OTCD; dbSNP:rs66741318)"
FT /id="VAR_004880"
FT VARIANT 159
FT /note="I -> T (in OTCD; dbSNP:rs72556269)"
FT /evidence="ECO:0000269|PubMed:8530002"
FT /id="VAR_004881"
FT VARIANT 160
FT /note="I -> S (in OTCD; dbSNP:rs67954347)"
FT /evidence="ECO:0000269|PubMed:11793483"
FT /id="VAR_012651"
FT VARIANT 161
FT /note="N -> S (in OTCD; dbSNP:rs72556271)"
FT /id="VAR_004882"
FT VARIANT 162
FT /note="G -> R (in OTCD; dbSNP:rs66626662)"
FT /id="VAR_004883"
FT VARIANT 168
FT /note="H -> Q (in OTCD; late onset; dbSNP:rs72556276)"
FT /id="VAR_004884"
FT VARIANT 168
FT /note="H -> R (in OTCD; late onset; dbSNP:rs66867430)"
FT /id="VAR_004885"
FT VARIANT 172
FT /note="I -> F (in OTCD; dbSNP:rs72556279)"
FT /evidence="ECO:0000269|PubMed:10502831"
FT /id="VAR_009233"
FT VARIANT 172
FT /note="I -> M (in OTCD; early onset; loss of ornithine
FT carbamoyltransferase activity; dbSNP:rs72556280)"
FT /evidence="ECO:0000269|PubMed:8081398"
FT /id="VAR_004886"
FT VARIANT 174
FT /note="A -> P (in OTCD; dbSNP:rs72556281)"
FT /id="VAR_004887"
FT VARIANT 175
FT /note="D -> V (in OTCD; dbSNP:rs68033093)"
FT /id="VAR_004888"
FT VARIANT 176
FT /note="Y -> C (in OTCD; late onset; dbSNP:rs72556283)"
FT /evidence="ECO:0000269|PubMed:8956038"
FT /id="VAR_004889"
FT VARIANT 178..179
FT /note="Missing (in OTCD; neonatal)"
FT /id="VAR_004891"
FT VARIANT 178
FT /note="T -> M (in OTCD; neonatal; dbSNP:rs72556284)"
FT /id="VAR_004890"
FT VARIANT 180
FT /note="Q -> H (in OTCD; dbSNP:rs72556287)"
FT /evidence="ECO:0000269|PubMed:9452024"
FT /id="VAR_004892"
FT VARIANT 181
FT /note="E -> G (in OTCD; neonatal; dbSNP:rs72556290)"
FT /id="VAR_004893"
FT VARIANT 182
FT /note="H -> L (in OTCD; dbSNP:rs72556291)"
FT /evidence="ECO:0000269|PubMed:8019569"
FT /id="VAR_004894"
FT VARIANT 183
FT /note="Y -> C (in OTCD; dbSNP:rs72556293)"
FT /id="VAR_004895"
FT VARIANT 183
FT /note="Y -> D (in OTCD; late onset; dbSNP:rs72556292)"
FT /evidence="ECO:0000269|PubMed:9143919"
FT /id="VAR_004896"
FT VARIANT 188
FT /note="G -> R (in OTCD; neonatal; dbSNP:rs72556294)"
FT /evidence="ECO:0000269|PubMed:8807340"
FT /id="VAR_004897"
FT VARIANT 188
FT /note="G -> V (in OTCD; dbSNP:rs72556295)"
FT /evidence="ECO:0000269|PubMed:10502831"
FT /id="VAR_009234"
FT VARIANT 191
FT /note="L -> F (in OTCD; dbSNP:rs72556296)"
FT /evidence="ECO:0000269|PubMed:11793483"
FT /id="VAR_012652"
FT VARIANT 192
FT /note="S -> R (in OTCD; neonatal; dbSNP:rs72556298)"
FT /id="VAR_004898"
FT VARIANT 195
FT /note="G -> R (in OTCD; loss of ornithine
FT carbamoyltransferase activity; dbSNP:rs67294955)"
FT /evidence="ECO:0000269|PubMed:7951259,
FT ECO:0000269|PubMed:8112735"
FT /id="VAR_004899"
FT VARIANT 196
FT /note="D -> V (in OTCD; neonatal; decreased ornithine
FT carbamoyltransferase activity; 3.7% activity;
FT dbSNP:rs72556300)"
FT /evidence="ECO:0000269|PubMed:8112735"
FT /id="VAR_004900"
FT VARIANT 196
FT /note="D -> Y (in OTCD; neonatal; dbSNP:rs66642398)"
FT /id="VAR_004901"
FT VARIANT 197
FT /note="G -> E (in OTCD; dbSNP:rs72556302)"
FT /id="VAR_004902"
FT VARIANT 197
FT /note="G -> R (in OTCD; dbSNP:rs72556301)"
FT /evidence="ECO:0000269|PubMed:10502831"
FT /id="VAR_009235"
FT VARIANT 198
FT /note="N -> K (in OTCD; dbSNP:rs72558404)"
FT /evidence="ECO:0000269|PubMed:10070627"
FT /id="VAR_010606"
FT VARIANT 201
FT /note="L -> P (in OTCD; neonatal; dbSNP:rs72558407)"
FT /evidence="ECO:0000269|PubMed:9452024"
FT /id="VAR_004903"
FT VARIANT 202
FT /note="H -> Y (in OTCD; dbSNP:rs72558408)"
FT /evidence="ECO:0000269|Ref.32"
FT /id="VAR_004904"
FT VARIANT 203
FT /note="S -> C (in OTCD; dbSNP:rs72558410)"
FT /evidence="ECO:0000269|PubMed:8019569"
FT /id="VAR_004905"
FT VARIANT 206
FT /note="M -> I (in OTCD; dbSNP:rs72558413)"
FT /evidence="ECO:0000269|PubMed:11793483"
FT /id="VAR_012653"
FT VARIANT 206
FT /note="M -> R (in OTCD; neonatal; dbSNP:rs72558412)"
FT /id="VAR_004906"
FT VARIANT 207
FT /note="S -> R (in OTCD; neonatal; dbSNP:rs72558415)"
FT /evidence="ECO:0000269|PubMed:9452024"
FT /id="VAR_004907"
FT VARIANT 208
FT /note="A -> T (in OTCD; late onset; dbSNP:rs72558416)"
FT /id="VAR_004908"
FT VARIANT 209
FT /note="A -> V (in OTCD; neonatal; dbSNP:rs72558417)"
FT /evidence="ECO:0000269|PubMed:10070627,
FT ECO:0000269|PubMed:8530002, ECO:0000269|PubMed:8807340"
FT /id="VAR_004909"
FT VARIANT 213
FT /note="M -> K (in OTCD; late onset)"
FT /evidence="ECO:0000269|PubMed:9143919"
FT /id="VAR_004910"
FT VARIANT 214
FT /note="H -> Y (in OTCD; neonatal; dbSNP:rs72558420)"
FT /evidence="ECO:0000269|PubMed:8830175"
FT /id="VAR_010607"
FT VARIANT 216
FT /note="Q -> E (in OTCD; dbSNP:rs72558423)"
FT /evidence="ECO:0000269|PubMed:2474822"
FT /id="VAR_004911"
FT VARIANT 220
FT /note="P -> A (in OTCD; late onset; dbSNP:rs72558425)"
FT /evidence="ECO:0000269|PubMed:8956038"
FT /id="VAR_004912"
FT VARIANT 225
FT /note="P -> L (in OTCD; dbSNP:rs67120076)"
FT /evidence="ECO:0000269|PubMed:1721894"
FT /id="VAR_004913"
FT VARIANT 225
FT /note="P -> R (in OTCD; neonatal; dbSNP:rs67120076)"
FT /id="VAR_004914"
FT VARIANT 225
FT /note="P -> T (in OTCD; late onset; dbSNP:rs72558428)"
FT /evidence="ECO:0000269|PubMed:7951259"
FT /id="VAR_004915"
FT VARIANT 242
FT /note="T -> I (in OTCD; late onset; dbSNP:rs72558435)"
FT /id="VAR_004916"
FT VARIANT 244
FT /note="L -> Q (in OTCD; late onset; dbSNP:rs72558436)"
FT /evidence="ECO:0000269|PubMed:9452049"
FT /id="VAR_004917"
FT VARIANT 247
FT /note="T -> K (in OTCD; neonatal/late onset;
FT dbSNP:rs72558437)"
FT /id="VAR_004918"
FT VARIANT 255
FT /note="H -> P (in OTCD; dbSNP:rs72558440)"
FT /id="VAR_004919"
FT VARIANT 262
FT /note="T -> K (in OTCD; mild; dbSNP:rs67333670)"
FT /evidence="ECO:0000269|PubMed:10737985"
FT /id="VAR_010608"
FT VARIANT 263
FT /note="D -> G (in OTCD; dbSNP:rs72558443)"
FT /id="VAR_004920"
FT VARIANT 263
FT /note="D -> N (in OTCD; dbSNP:rs72558442)"
FT /evidence="ECO:0000269|Ref.32"
FT /id="VAR_004921"
FT VARIANT 264
FT /note="T -> A (in OTCD; late onset; decreased ornithine
FT carbamoyltransferase activity; 8.9% activity;
FT dbSNP:rs72558444)"
FT /evidence="ECO:0000269|PubMed:10737985,
FT ECO:0000269|PubMed:8112735"
FT /id="VAR_004922"
FT VARIANT 264
FT /note="T -> I (in OTCD; late onset; dbSNP:rs67156896)"
FT /evidence="ECO:0000269|PubMed:9452024"
FT /id="VAR_004923"
FT VARIANT 265
FT /note="W -> L (in OTCD; mild; dbSNP:rs72558446)"
FT /evidence="ECO:0000269|PubMed:10737985"
FT /id="VAR_010609"
FT VARIANT 267
FT /note="S -> R (in OTCD; dbSNP:rs72558448)"
FT /evidence="ECO:0000269|PubMed:9452024"
FT /id="VAR_004924"
FT VARIANT 268
FT /note="M -> T (in OTCD; late onset; dbSNP:rs72558449)"
FT /id="VAR_004925"
FT VARIANT 269
FT /note="G -> E (in OTCD; neonatal; dbSNP:rs72558450)"
FT /evidence="ECO:0000269|PubMed:7474905"
FT /id="VAR_004926"
FT VARIANT 270
FT /note="Q -> R (in dbSNP:rs1800328)"
FT /evidence="ECO:0000269|PubMed:10070627,
FT ECO:0000269|PubMed:16959974, ECO:0000269|PubMed:6372096"
FT /id="VAR_004927"
FT VARIANT 272
FT /note="Missing (in OTCD; late onset; dbSNP:rs72558452)"
FT /evidence="ECO:0000269|PubMed:8956045"
FT /id="VAR_004928"
FT VARIANT 277
FT /note="R -> Q (in OTCD; late onset; dbSNP:rs66724222)"
FT /evidence="ECO:0000269|PubMed:7951259,
FT ECO:0000269|PubMed:8081373"
FT /id="VAR_004929"
FT VARIANT 277
FT /note="R -> W (in OTCD; late onset; dbSNP:rs72558454)"
FT /evidence="ECO:0000269|PubMed:2347583,
FT ECO:0000269|PubMed:9065786"
FT /id="VAR_004930"
FT VARIANT 301
FT /note="L -> F (in OTCD; dbSNP:rs72558462)"
FT /evidence="ECO:0000269|PubMed:11793483"
FT /id="VAR_012654"
FT VARIANT 302
FT /note="H -> L (in OTCD; female; late onset;
FT dbSNP:rs67993095)"
FT /evidence="ECO:0000269|PubMed:8807340"
FT /id="VAR_004931"
FT VARIANT 302
FT /note="H -> Q (in OTCD; late onset; dbSNP:rs67870244)"
FT /id="VAR_004932"
FT VARIANT 302
FT /note="H -> Y (in OTCD; neonatal; dbSNP:rs72558463)"
FT /evidence="ECO:0000269|PubMed:8956038"
FT /id="VAR_004933"
FT VARIANT 303
FT /note="C -> R (in OTCD; neonatal; dbSNP:rs67468335)"
FT /evidence="ECO:0000269|PubMed:9452049"
FT /id="VAR_004934"
FT VARIANT 303
FT /note="C -> Y (in OTCD; dbSNP:rs72558464)"
FT /id="VAR_004935"
FT VARIANT 304
FT /note="L -> F (in OTCD; dbSNP:rs72558465)"
FT /evidence="ECO:0000269|PubMed:1480464"
FT /id="VAR_004936"
FT VARIANT 305
FT /note="P -> H (in OTCD; dbSNP:rs67501347)"
FT /evidence="ECO:0000269|PubMed:11793483"
FT /id="VAR_012655"
FT VARIANT 309
FT /note="Missing (in OTCD; late onset)"
FT /evidence="ECO:0000269|PubMed:7951259"
FT /id="VAR_004937"
FT VARIANT 320
FT /note="R -> L (in OTCD; dbSNP:rs72558474)"
FT /evidence="ECO:0000269|PubMed:1671317"
FT /id="VAR_004938"
FT VARIANT 326
FT /note="E -> K (in OTCD; dbSNP:rs72558476)"
FT /evidence="ECO:0000269|PubMed:10070627"
FT /id="VAR_010610"
FT VARIANT 330
FT /note="R -> G (in OTCD; dbSNP:rs72558478)"
FT /id="VAR_004939"
FT VARIANT 333
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:11793483"
FT /id="VAR_012656"
FT VARIANT 336
FT /note="A -> S (in OTCD; late onset; dbSNP:rs72558486)"
FT /id="VAR_004940"
FT VARIANT 337
FT /note="V -> L (in OTCD; late onset; dbSNP:rs72558487)"
FT /id="VAR_004941"
FT VARIANT 339
FT /note="V -> L (in OTCD; neonatal; dbSNP:rs72558488)"
FT /id="VAR_004942"
FT VARIANT 340
FT /note="S -> P (in OTCD; late onset; dbSNP:rs72558489)"
FT /evidence="ECO:0000269|PubMed:9143919"
FT /id="VAR_004943"
FT VARIANT 341
FT /note="L -> P (in OTCD; dbSNP:rs72558490)"
FT /evidence="ECO:0000269|PubMed:11793483"
FT /id="VAR_012657"
FT VARIANT 343
FT /note="T -> K (in OTCD; late onset; dbSNP:rs72558491)"
FT /evidence="ECO:0000269|PubMed:8956038"
FT /id="VAR_004944"
FT VARIANT 345
FT /note="Y -> C (in OTCD; neonatal; dbSNP:rs72558492)"
FT /id="VAR_004946"
FT VARIANT 345
FT /note="Y -> D (in OTCD; dbSNP:rs66469337)"
FT /evidence="ECO:0000269|PubMed:1480464"
FT /id="VAR_004947"
FT VARIANT 354
FT /note="F -> C (in OTCD; late onset; dbSNP:rs72558495)"
FT /id="VAR_004948"
FT MUTAGEN 15
FT /note="R->G: Loss of cleavage of the transit peptide and
FT loss of localization to mitochondrial matrix; when
FT associated with G-23 and G-26."
FT /evidence="ECO:0000269|PubMed:6372096"
FT MUTAGEN 23
FT /note="R->G: Loss of cleavage of the transit peptide and
FT loss of localization to mitochondrial matrix; when
FT associated with G-15 and G-26."
FT /evidence="ECO:0000269|PubMed:3895227"
FT MUTAGEN 26
FT /note="R->G: Loss of cleavage of the transit peptide and
FT loss of localization to mitochondrial matrix; when
FT associated with G-15 and G-23."
FT /evidence="ECO:0000269|PubMed:3895227"
FT CONFLICT 193..194
FT /note="WI -> CF (in Ref. 1; AAA59975)"
FT /evidence="ECO:0000305"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:1OTH"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:1OTH"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:1OTH"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1OTH"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1OTH"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:1OTH"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:1OTH"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:1OTH"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:1OTH"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1OTH"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:1OTH"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:1OTH"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:1OTH"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:1OTH"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:1OTH"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:1OTH"
FT HELIX 323..342
FT /evidence="ECO:0007829|PDB:1OTH"
SQ 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
