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 27-MAR-2024, entry version 247. 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>3.3.co;2-5; 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 RT OTC 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>3.3.co;2-9; 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-THR-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 RT OTC 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 RT OTC 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 EMDB; EMD-35535; -. DR SMR; P00480; -. DR BioGRID; 111050; 143. DR CORUM; P00480; -. DR IntAct; P00480; 12. DR MINT; P00480; -. 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; 9606-ENSP00000039007; -. DR PeptideAtlas; P00480; -. DR ProteomicsDB; 51254; -. DR Antibodypedia; 336; 834 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 AGR; HGNC:8512; -. 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; 2782890at2759; -. DR PhylomeDB; P00480; -. DR TreeFam; TF352580; -. DR BioCyc; MetaCyc:HS00516-MONOMER; -. 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 786 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 92 other cell types or tissues. DR ExpressionAtlas; P00480; baseline and differential. 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: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:0055081; P:monoatomic anion homeostasis; 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; Aspartate/ornithine carbamoyltransferase; 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 NCBIfam; TIGR00658; orni_carb_tr; 1. DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR45753:SF3; ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL; 1. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00102; OTCASE. DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. DR Genevisible; P00480; HS. 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 FT 100-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 /evidence="ECO:0000269|PubMed:9452024" 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 //