ID CPSM_MOUSE Reviewed; 1500 AA. AC Q8C196; A0JNU4; Q6NX75; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 2. DT 27-MAR-2024, entry version 171. DE RecName: Full=Carbamoyl-phosphate synthase [ammonia], mitochondrial; DE EC=6.3.4.16; DE AltName: Full=Carbamoyl-phosphate synthetase I; DE Short=CPSase I; DE Flags: Precursor; GN Name=Cps1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; 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 [3] RP PROTEIN SEQUENCE OF 113-167; 183-207; 287-307; 317-328; 403-419; 459-522; RP 533-624; 631-638; 683-689; 729-740; 794-811; 815-826; 842-850; 857-880; RP 883-889; 893-905; 1030-1039; 1075-1085; 1090-1100; 1158-1168; 1175-1183; RP 1233-1259; 1270-1317; 1320-1326; 1349-1356; 1361-1387; 1429-1444 AND RP 1455-1479, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Liver; RA Bienvenut W.V.; RL Submitted (JUL-2005) to UniProtKB. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 753-1500. RC STRAIN=C57BL/6J; TISSUE=Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537 AND SER-1079, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP ACETYLATION AT LYS-1291, AND DEACETYLATION. RX PubMed=19410549; DOI=10.1016/j.cell.2009.02.026; RA Nakagawa T., Lomb D.J., Haigis M.C., Guarente L.; RT "SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea RT cycle."; RL Cell 137:560-570(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and RC Pancreas; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [8] RP ACETYLATION AT LYS-44; LYS-287 AND LYS-1291, SUCCINYLATION AT LYS-44; RP LYS-287 AND LYS-1291, AND DESUCCINYLATION BY SIRT5. RX PubMed=22076378; DOI=10.1126/science.1207861; RA Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., RA Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., RA Hao Q., Lin H.; RT "Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."; RL Science 334:806-809(2011). RN [9] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-44; LYS-55; LYS-57; LYS-119; RP LYS-157; LYS-207; LYS-214; LYS-287; LYS-307; LYS-400; LYS-402; LYS-412; RP LYS-458; LYS-522; LYS-527; LYS-553; LYS-560; LYS-575; LYS-603; LYS-612; RP LYS-751; LYS-757; LYS-793; LYS-831; LYS-840; LYS-875; LYS-889; LYS-892; RP LYS-915; LYS-919; LYS-1074; LYS-1100; LYS-1149; LYS-1168; LYS-1183; RP LYS-1232; LYS-1269; LYS-1291; LYS-1356; LYS-1360; LYS-1444; LYS-1471; RP LYS-1479 AND LYS-1486, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44; LYS-55; LYS-57; LYS-119; RP LYS-157; LYS-171; LYS-182; LYS-197; LYS-207; LYS-210; LYS-214; LYS-219; RP LYS-228; LYS-279; LYS-280; LYS-287; LYS-307; LYS-310; LYS-412; LYS-453; RP LYS-458; LYS-522; LYS-527; LYS-532; LYS-553; LYS-560; LYS-575; LYS-603; RP LYS-612; LYS-630; LYS-751; LYS-757; LYS-772; LYS-793; LYS-811; LYS-831; RP LYS-840; LYS-841; LYS-856; LYS-875; LYS-889; LYS-892; LYS-908; LYS-915; RP LYS-919; LYS-935; LYS-1074; LYS-1100; LYS-1168; LYS-1183; LYS-1222; RP LYS-1232; LYS-1269; LYS-1291; LYS-1356; LYS-1444; LYS-1471; LYS-1479 AND RP LYS-1486, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria RT identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). RN [11] RP FUNCTION, AND GLUTARYLATION. RX PubMed=24703693; DOI=10.1016/j.cmet.2014.03.014; RA Tan M., Peng C., Anderson K.A., Chhoy P., Xie Z., Dai L., Park J., Chen Y., RA Huang H., Zhang Y., Ro J., Wagner G.R., Green M.F., Madsen A.S., RA Schmiesing J., Peterson B.S., Xu G., Ilkayeva O.R., Muehlbauer M.J., RA Braulke T., Muehlhausen C., Backos D.S., Olsen C.A., McGuire P.J., RA Pletcher S.D., Lombard D.B., Hirschey M.D., Zhao Y.; RT "Lysine glutarylation is a protein posttranslational modification regulated RT by SIRT5."; RL Cell Metab. 19:605-617(2014). RN [12] RP INTERACTION WITH P.BERGHEI PLSCR (MICROBIAL INFECTION), SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=34799567; DOI=10.1038/s41467-021-27109-7; RA Cha S.J., Kim M.S., Na C.H., Jacobs-Lorena M.; RT "Plasmodium sporozoite phospholipid scramblase interacts with mammalian RT carbamoyl-phosphate synthetase 1 to infect hepatocytes."; RL Nat. Commun. 12:6773-6773(2021). CC -!- FUNCTION: Involved in the urea cycle of ureotelic animals where the CC enzyme plays an important role in removing excess ammonia from the CC cell. {ECO:0000269|PubMed:24703693}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, CC ChEBI:CHEBI:456216; EC=6.3.4.16; CC Evidence={ECO:0000250|UniProtKB:P07756}; CC -!- ACTIVITY REGULATION: Requires N-acetyl-L-glutamate (NAG) as an CC allosteric activator. {ECO:0000250}. CC -!- SUBUNIT: Can form homooligomers (monomers as predominant form and CC dimers). {ECO:0000250|UniProtKB:P31327}. CC -!- SUBUNIT: (Microbial infection) Interacts with P.berghei (ANKA strain) CC phospholipid scramblase PLSCR; the interaction is involved in the CC interaction between parasite sporozoites and host hepatocytes. CC {ECO:0000269|PubMed:34799567}. CC -!- INTERACTION: CC Q8C196; Q8K2C6: Sirt5; NbExp=2; IntAct=EBI-2348828, EBI-2348809; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P31327}. CC Nucleus, nucleolus {ECO:0000250|UniProtKB:P31327}. Cell membrane CC {ECO:0000269|PubMed:34799567}; Peripheral membrane protein CC {ECO:0000305}; Extracellular side {ECO:0000269|PubMed:34799567}. CC Note=Localizes to the cell surface of hepatocytes. CC {ECO:0000269|PubMed:34799567}. CC -!- TISSUE SPECIFICITY: Expressed in hepatocytes (at protein level). CC {ECO:0000269|PubMed:34799567}. CC -!- DOMAIN: The type-1 glutamine amidotransferase domain is defective. CC {ECO:0000250}. CC -!- PTM: Undergoes proteolytic cleavage in the C-terminal region CC corresponding to the loss of approximately 12 AA residues from the C- CC terminus. {ECO:0000250|UniProtKB:P31327}. CC -!- PTM: Acetylation of Lys-287, Lys-603, Lys-841 and Lys-1291 is observed CC in liver mitochondria from fasted mice but not from fed mice. CC {ECO:0000269|PubMed:19410549, ECO:0000269|PubMed:22076378}. CC -!- PTM: Succinylated at Lys-44, Lys-287 and Lys-1291. Desuccinylated at CC Lys-1291 by SIRT5, leading to activation. CC {ECO:0000269|PubMed:22076378}. CC -!- PTM: Glutarylated. Glutarylation levels increase during fasting. CC Deglutarylated by SIRT5 at Lys-55, Lys-219, Lys-412, Lys-889, Lys-892, CC Lys-915, Lys-1360 and Lys-1486, leading to activation. CC {ECO:0000250|UniProtKB:P31327, ECO:0000269|PubMed:24703693}. CC -!- CAUTION: Was initially reported to be deacetylated by Sirt5 CC (PubMed:19410549). However, it was later shown that Sirt5 has poor CC deacetylase activity and mediates desuccinylation of Cps1 instead CC (PubMed:22076378). {ECO:0000305|PubMed:19410549, CC ECO:0000305|PubMed:22076378}. 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; AC101854; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC133187; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC067211; AAH67211.1; -; mRNA. DR EMBL; BC126969; AAI26970.1; -; mRNA. DR EMBL; AK028683; BAC26064.1; -; mRNA. DR CCDS; CCDS35605.1; -. DR RefSeq; NP_001074278.1; NM_001080809.2. DR RefSeq; XP_011236802.1; XM_011238500.1. DR AlphaFoldDB; Q8C196; -. DR SMR; Q8C196; -. DR BioGRID; 230602; 6. DR IntAct; Q8C196; 2. DR STRING; 10090.ENSMUSP00000027144; -. DR GlyCosmos; Q8C196; 3 sites, No reported glycans. DR GlyGen; Q8C196; 7 sites, 1 O-linked glycan (7 sites). DR iPTMnet; Q8C196; -. DR PhosphoSitePlus; Q8C196; -. DR SwissPalm; Q8C196; -. DR jPOST; Q8C196; -. DR MaxQB; Q8C196; -. DR PaxDb; 10090-ENSMUSP00000027144; -. DR PeptideAtlas; Q8C196; -. DR ProteomicsDB; 285294; -. DR Antibodypedia; 20025; 553 antibodies from 33 providers. DR Ensembl; ENSMUST00000027144.8; ENSMUSP00000027144.8; ENSMUSG00000025991.9. DR GeneID; 227231; -. DR KEGG; mmu:227231; -. DR UCSC; uc007biy.2; mouse. DR AGR; MGI:891996; -. DR CTD; 1373; -. DR MGI; MGI:891996; Cps1. DR VEuPathDB; HostDB:ENSMUSG00000025991; -. DR eggNOG; KOG0370; Eukaryota. DR GeneTree; ENSGT00940000157192; -. DR HOGENOM; CLU_000513_0_2_1; -. DR InParanoid; Q8C196; -. DR OMA; FPFNKFP; -. DR OrthoDB; 309at2759; -. DR PhylomeDB; Q8C196; -. DR TreeFam; TF331485; -. DR BRENDA; 6.3.4.16; 3474. DR Reactome; R-MMU-70635; Urea cycle. DR SABIO-RK; Q8C196; -. DR BioGRID-ORCS; 227231; 2 hits in 77 CRISPR screens. DR PRO; PR:Q8C196; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q8C196; Protein. DR Bgee; ENSMUSG00000025991; Expressed in left lobe of liver and 63 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI. DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0005524; F:ATP binding; ISO:MGI. DR GO; GO:0005509; F:calcium ion binding; ISO:MGI. DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IMP:MGI. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI. DR GO; GO:0016595; F:glutamate binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; ISO:MGI. DR GO; GO:0072341; F:modified amino acid binding; ISO:MGI. DR GO; GO:0005543; F:phospholipid binding; ISO:MGI. DR GO; GO:0030955; F:potassium ion binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0036094; F:small molecule binding; ISO:MGI. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; ISO:MGI. DR GO; GO:0071242; P:cellular response to ammonium ion; ISO:MGI. DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl. DR GO; GO:0071377; P:cellular response to glucagon stimulus; IEA:Ensembl. DR GO; GO:0071400; P:cellular response to oleic acid; IEA:Ensembl. DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central. DR GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl. DR GO; GO:0050667; P:homocysteine metabolic process; ISO:MGI. DR GO; GO:0007494; P:midgut development; IEA:Ensembl. DR GO; GO:0055081; P:monoatomic anion homeostasis; ISO:MGI. DR GO; GO:0046209; P:nitric oxide metabolic process; ISO:MGI. DR GO; GO:0014075; P:response to amine; IEA:Ensembl. DR GO; GO:0043200; P:response to amino acid; IEA:Ensembl. DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl. DR GO; GO:0032094; P:response to food; IEA:Ensembl. DR GO; GO:0060416; P:response to growth hormone; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI. DR GO; GO:0042594; P:response to starvation; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; 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:0019433; P:triglyceride catabolic process; ISO:MGI. DR GO; GO:0000050; P:urea cycle; ISO:MGI. DR GO; GO:0042311; P:vasodilation; ISO:MGI. DR CDD; cd01744; GATase1_CPSase; 1. DR CDD; cd01423; MGS_CPS_I_III; 1. DR Gene3D; 3.40.50.20; -; 2. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2. DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1. DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1. DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1. DR HAMAP; MF_01209; CPSase_S_chain; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR006275; CarbamoylP_synth_lsu. DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo. DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf. DR InterPro; IPR006274; CarbamoylP_synth_ssu. DR InterPro; IPR002474; CarbamoylP_synth_ssu_N. DR InterPro; IPR036480; CarbP_synth_ssu_N_sf. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR035686; CPSase_GATase1. DR InterPro; IPR017926; GATASE. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR036914; MGS-like_dom_sf. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR NCBIfam; TIGR01369; CPSaseII_lrg; 1. DR NCBIfam; TIGR01368; CPSaseIIsmall; 1. DR PANTHER; PTHR11405:SF57; CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL; 1. DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1. DR Pfam; PF02786; CPSase_L_D2; 2. DR Pfam; PF02787; CPSase_L_D3; 1. DR Pfam; PF00988; CPSase_sm_chain; 1. DR Pfam; PF00117; GATase; 1. DR Pfam; PF02142; MGS; 1. DR PRINTS; PR00098; CPSASE. DR PRINTS; PR00099; CPSGATASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SMART; SM01097; CPSase_sm_chain; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1. DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2. DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 2. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00866; CPSASE_1; 2. DR PROSITE; PS00867; CPSASE_2; 2. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS51855; MGS; 1. DR Genevisible; Q8C196; MM. PE 1: Evidence at protein level; KW Acetylation; Allosteric enzyme; ATP-binding; Cell membrane; KW Direct protein sequencing; Glycoprotein; Ligase; Membrane; Mitochondrion; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Transit peptide; Urea cycle. FT TRANSIT 1..38 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 39..1500 FT /note="Carbamoyl-phosphate synthase [ammonia], FT mitochondrial" FT /evidence="ECO:0000250" FT /id="PRO_0000029898" FT DOMAIN 219..404 FT /note="Glutamine amidotransferase type-1" FT DOMAIN 551..743 FT /note="ATP-grasp 1" FT DOMAIN 1093..1284 FT /note="ATP-grasp 2" FT DOMAIN 1355..1500 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" FT REGION 39..218 FT /note="Anthranilate phosphoribosyltransferase homolog" FT BINDING 1391 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250" FT BINDING 1394 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250" FT BINDING 1410 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250" FT BINDING 1437 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250" FT BINDING 1440 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250" FT BINDING 1449 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250" FT MOD_RES 44 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378, FT ECO:0007744|PubMed:23576753" FT MOD_RES 44 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378, FT ECO:0007744|PubMed:23806337" FT MOD_RES 55 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 55 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 55 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 57 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 57 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 119 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 119 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 148 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 157 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 157 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 171 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 171 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 176 FT /note="N6-glutaryllysine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 182 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 189 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07756" FT MOD_RES 197 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 207 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 207 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 207 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 210 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 210 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 214 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 214 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 214 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 219 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 219 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 228 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 228 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 237 FT /note="N6-glutaryllysine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 279 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 280 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 280 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 287 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378, FT ECO:0007744|PubMed:23576753" FT MOD_RES 287 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378, FT ECO:0007744|PubMed:23806337" FT MOD_RES 307 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 307 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 307 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 310 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 310 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 400 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 402 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 402 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 412 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 412 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 412 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 453 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 453 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 458 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 458 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 458 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 522 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 522 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 527 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 527 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 527 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 532 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 532 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 537 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 540 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07756" FT MOD_RES 553 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 553 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 553 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 560 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 560 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 569 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 575 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 575 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 603 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 603 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 612 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 612 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 630 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 728 FT /note="N6-glutaryllysine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 751 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 751 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 757 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 757 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 757 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 772 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 772 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 793 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 793 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 793 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 811 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 811 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 831 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 831 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 840 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 840 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 841 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 841 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 856 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 856 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 875 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 875 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 875 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 889 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 889 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 889 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 892 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 892 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 892 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 896 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07756" FT MOD_RES 898 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07756" FT MOD_RES 908 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 908 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 915 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 915 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 915 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 919 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 919 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 919 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 935 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1036 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1074 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1074 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1074 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1079 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 1090 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07756" FT MOD_RES 1093 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07756" FT MOD_RES 1100 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1100 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1149 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1168 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1168 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1168 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1183 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1183 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1183 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1203 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1222 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1224 FT /note="N6-glutaryllysine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1232 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1232 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1269 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1269 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1291 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:19410549, FT ECO:0000269|PubMed:22076378, ECO:0007744|PubMed:23576753" FT MOD_RES 1291 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378, FT ECO:0007744|PubMed:23806337" FT MOD_RES 1356 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1356 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1356 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1360 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1360 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1419 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1431 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1444 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1444 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1471 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1471 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1479 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1479 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1479 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1486 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 1486 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1486 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT CARBOHYD 537 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250" FT CARBOHYD 1331 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT CARBOHYD 1332 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000250" FT CONFLICT 931..934 FT /note="LRLK -> HASE (in Ref. 2; AAH67211)" FT /evidence="ECO:0000305" SQ SEQUENCE 1500 AA; 164618 MW; 84A7268C1D7E8101 CRC64; MTRILTACKV VKTLKSGFGF ANVTTKRQWD FSRPGIRLLS VKAKTAHIVL EDGTKMKGYS FGHPSSVAGE VVFNTGLGGY PEALTDPAYK GQILTMANPI IGNGGAPDTT ARDELGLNKY MESDGIKVAG LLVLNYSNDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML GKIEFEGQSV DFVDPNKQNL IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA EVHLVPWNHD FTQMEYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK GKGTTITSVL PKPALVASRV EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD AVYFLPITPQ FVTEVIKAER PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES IMATEDRQLF SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC PNKETLIDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT GDSVVVAPAQ TLSNAEFQML RRTSVNVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLK KELSEPSSTR IYAIAKALEN NMSLDEIVRL TSIDKWFLYK MRDILNMDKT LKGLNSDSVT EETLRKAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV STDFDECDKL YFEELSLERI LDIYHQEACN GCIISVGGQI PNNLAVPLYK NGVKIMGTSP LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN VVFSEDEMKR FLEEATRVSQ EHPVVLTKFV EGAREVEMDA VGKEGRVISH AISEHVEDAG VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA SRSFPFVSKT LGVDFIDVAT KVMIGESIDE KRLPTLEQPI IPSDYVAIKA PMFSWPRLRD ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN NNTKFVHDNY VIRRTAVDSG IALLTNFQVT KLFAEAVQKS RTVDSKSLFH YRQYSAGKAA //