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Database: UniProt
Entry: P07756
LinkDB: P07756
Original site: P07756 
ID   CPSM_RAT                Reviewed;        1500 AA.
AC   P07756;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   16-JAN-2019, entry version 170.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=2991241;
RA   Nyunoya H., Broglie K.E., Widgren E.E., Lusty C.J.;
RT   "Characterization and derivation of the gene coding for mitochondrial
RT   carbamyl phosphate synthetase I of rat.";
RL   J. Biol. Chem. 260:9346-9356(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
RX   PubMed=3038878;
RA   Lagace M., Howell B.W., Burak R., Lusty C.J., Shore G.C.;
RT   "Rat carbamyl-phosphate synthetase I gene. Promoter sequence and
RT   tissue-specific transcriptional regulation in vitro.";
RL   J. Biol. Chem. 262:10415-10418(1987).
RN   [3]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, ALLOSTERIC ACTIVATOR NAG
RP   BINDING SITE, KINETIC PARAMETERS, AND MUTAGENESIS OF THR-1391;
RP   THR-1394; TRP-1410; ASN-1437 AND ASN-1440.
RX   PubMed=19754428; DOI=10.1042/BJ20090888;
RA   Pekkala S., Martinez A.I., Barcelona B., Gallego J., Bendala E.,
RA   Yefimenko I., Rubio V., Cervera J.;
RT   "Structural insight on the control of urea synthesis: identification
RT   of the binding site for N-acetyl-L-glutamate, the essential allosteric
RT   activator of mitochondrial carbamoyl phosphate synthetase.";
RL   Biochem. J. 424:211-220(2009).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-189; SER-537;
RP   SER-540; SER-896; SER-898; SER-1036; SER-1090; SER-1093 AND SER-1431,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [5]
RP   PROTEOLYTIC CLEAVAGE.
RX   PubMed=23649895; DOI=10.1002/humu.22349;
RA   Diez-Fernandez C., Martinez A.I., Pekkala S., Barcelona B.,
RA   Perez-Arellano I., Guadalajara A.M., Summar M., Cervera J., Rubio V.;
RT   "Molecular characterization of carbamoyl-phosphate synthetase (CPS1)
RT   deficiency using human recombinant CPS1 as a key tool.";
RL   Hum. Mutat. 34:1149-1159(2013).
RN   [6]
RP   GLYCOSYLATION AT SER-537; SER-1331 AND THR-1332.
RX   PubMed=24098488; DOI=10.1371/journal.pone.0076399;
RA   Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
RT   "Discovery and confirmation of O-GlcNAcylated proteins in rat liver
RT   mitochondria by combination of mass spectrometry and immunological
RT   methods.";
RL   PLoS ONE 8:E76399-E76399(2013).
CC   -!- FUNCTION: Involved in the urea cycle of ureotelic animals where
CC       the enzyme plays an important role in removing excess ammonia from
CC       the cell.
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:0000269|PubMed:19754428};
CC   -!- ACTIVITY REGULATION: Requires N-acetyl-L-glutamate (NAG) as an
CC       allosteric activator. N-acetyl-L-beta-phenylglutamate (Phe-NAG)
CC       can also activate CPSase I, but with an activation constant that
CC       is 2-fold higher than that for NAG. {ECO:0000269|PubMed:19754428}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.06 mM for ATP {ECO:0000269|PubMed:19754428};
CC         KM=6.43 mM for HCO(3)(-) {ECO:0000269|PubMed:19754428};
CC         KM=1.07 mM for NH(4)(+) {ECO:0000269|PubMed:19754428};
CC         Note=The activation constant Ka of N-acetyl-L-glutamate for the
CC         reaction is 0.11 mM.;
CC   -!- SUBUNIT: Can form homooligomers (monomers as predominant form and
CC       dimers). {ECO:0000250|UniProtKB:P31327}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:P31327}.
CC   -!- TISSUE SPECIFICITY: Primarily in the liver and small intestine.
CC   -!- DOMAIN: The type-1 glutamine amidotransferase domain is defective.
CC   -!- PTM: 50% of the mature protein that was isolated had Leu-39 as its
CC       N-terminal residue and 50% had Ser-40 suggesting two adjacent
CC       processing sites. However, the possibility of proteolytic removal
CC       of Leu-39 during the isolation of the enzyme cannot be excluded.
CC       Undergoes proteolytic cleavage in the C-terminal region
CC       corresponding to the loss of approximately 12 AA residues from the
CC       C-terminus (PubMed:23649895). {ECO:0000269|PubMed:23649895}.
CC   -!- PTM: Succinylated at Lys-287 and Lys-1291. Desuccinylated at Lys-
CC       1291 by SIRT5, leading to activation (By similarity).
CC       {ECO:0000250|UniProtKB:Q8C196}.
CC   -!- PTM: Glutarylated. Glutarylation levels increase during fasting.
CC       Deglutarylated by SIRT5 at Lys-55, Lys-219, Lys-412, Lys-889, Lys-
CC       892, Lys-915, Lys-1360 and Lys-1486, leading to activation.
CC       {ECO:0000250|UniProtKB:P31327}.
DR   EMBL; M12335; AAB59717.1; -; Genomic_DNA.
DR   EMBL; M11710; AAB59717.1; JOINED; mRNA.
DR   EMBL; M12318; AAB59717.1; JOINED; Genomic_DNA.
DR   EMBL; M12319; AAB59717.1; JOINED; Genomic_DNA.
DR   EMBL; M12320; AAB59717.1; JOINED; Genomic_DNA.
DR   EMBL; M12321; AAB59717.1; JOINED; Genomic_DNA.
DR   EMBL; M12322; AAB59717.1; JOINED; Genomic_DNA.
DR   EMBL; M12323; AAB59717.1; JOINED; Genomic_DNA.
DR   EMBL; M12324; AAB59717.1; JOINED; Genomic_DNA.
DR   EMBL; M12325; AAB59717.1; JOINED; Genomic_DNA.
DR   EMBL; M12326; AAB59717.1; JOINED; mRNA.
DR   EMBL; M12327; AAB59717.1; JOINED; Genomic_DNA.
DR   EMBL; M12328; AAB59717.1; JOINED; Genomic_DNA.
DR   EMBL; J02805; AAA40959.1; -; Genomic_DNA.
DR   PIR; A28481; SYRTCA.
DR   RefSeq; NP_058768.1; NM_017072.2.
DR   RefSeq; XP_017452081.1; XM_017596592.1.
DR   UniGene; Rn.53968; -.
DR   ProteinModelPortal; P07756; -.
DR   SMR; P07756; -.
DR   STRING; 10116.ENSRNOP00000019021; -.
DR   CarbonylDB; P07756; -.
DR   iPTMnet; P07756; -.
DR   PhosphoSitePlus; P07756; -.
DR   SwissPalm; P07756; -.
DR   jPOST; P07756; -.
DR   PaxDb; P07756; -.
DR   PRIDE; P07756; -.
DR   Ensembl; ENSRNOT00000019023; ENSRNOP00000019021; ENSRNOG00000013704.
DR   GeneID; 497840; -.
DR   KEGG; rno:497840; -.
DR   UCSC; RGD:2395; rat.
DR   CTD; 1373; -.
DR   RGD; 2395; Cps1.
DR   eggNOG; KOG0370; Eukaryota.
DR   eggNOG; COG0458; LUCA.
DR   eggNOG; COG0505; LUCA.
DR   GeneTree; ENSGT00940000157192; -.
DR   HOGENOM; HOG000234583; -.
DR   HOVERGEN; HBG000279; -.
DR   InParanoid; P07756; -.
DR   KO; K01948; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 273358at2759; -.
DR   PhylomeDB; P07756; -.
DR   Reactome; R-RNO-70635; Urea cycle.
DR   SABIO-RK; P07756; -.
DR   PRO; PR:P07756; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000013704; Expressed in 6 organ(s), highest expression level in liver.
DR   Genevisible; P07756; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IDA:HGNC.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IPI:RGD.
DR   GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IDA:RGD.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR   GO; GO:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
DR   GO; GO:0016595; F:glutamate binding; IPI:RGD.
DR   GO; GO:0072341; F:modified amino acid binding; IEA:Ensembl.
DR   GO; GO:0005543; F:phospholipid binding; IDA:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR   GO; GO:0055081; P:anion homeostasis; IDA:RGD.
DR   GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:1903718; P:cellular response to ammonia; IBA:GO_Central.
DR   GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR   GO; GO:0071377; P:cellular response to glucagon stimulus; IEP:RGD.
DR   GO; GO:0071400; P:cellular response to oleic acid; IEP:RGD.
DR   GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR   GO; GO:0070365; P:hepatocyte differentiation; IEP:RGD.
DR   GO; GO:0050667; P:homocysteine metabolic process; IEA:Ensembl.
DR   GO; GO:0001889; P:liver development; IEP:RGD.
DR   GO; GO:0007494; P:midgut development; IEP:RGD.
DR   GO; GO:0046209; P:nitric oxide metabolic process; IEA:Ensembl.
DR   GO; GO:0014075; P:response to amine; IEP:RGD.
DR   GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR   GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR   GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0032094; P:response to food; IEP:RGD.
DR   GO; GO:0033762; P:response to glucagon; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR   GO; GO:0060416; P:response to growth hormone; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0034201; P:response to oleic acid; IEP:RGD.
DR   GO; GO:0042594; P:response to starvation; IEP:RGD.
DR   GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR   GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR   GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR   GO; GO:0019433; P:triglyceride catabolic process; IEA:Ensembl.
DR   GO; GO:0000050; P:urea cycle; IDA:RGD.
DR   GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; -; 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   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   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF52021; SSF52021; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
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.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; ATP-binding; Complete proteome;
KW   Glycoprotein; Ligase; Mitochondrion; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transit peptide;
KW   Urea cycle.
FT   TRANSIT       1     38       Mitochondrion.
FT   CHAIN        39   1500       Carbamoyl-phosphate synthase [ammonia],
FT                                mitochondrial.
FT                                /FTId=PRO_0000029899.
FT   DOMAIN      219    404       Glutamine amidotransferase type-1.
FT   DOMAIN      551    743       ATP-grasp 1.
FT   DOMAIN     1093   1284       ATP-grasp 2.
FT   DOMAIN     1355   1500       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   REGION       39    218       Anthranilate phosphoribosyltransferase
FT                                homolog.
FT   BINDING    1391   1391       Allosteric activator.
FT   BINDING    1394   1394       Allosteric activator.
FT   BINDING    1410   1410       Allosteric activator.
FT   BINDING    1437   1437       Allosteric activator.
FT   BINDING    1440   1440       Allosteric activator.
FT   BINDING    1449   1449       Allosteric activator.
FT   MOD_RES      55     55       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES      55     55       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES      55     55       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES      57     57       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES      57     57       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     119    119       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     119    119       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     148    148       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     157    157       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     157    157       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     171    171       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     171    171       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     176    176       N6-glutaryllysine.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     182    182       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     189    189       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     197    197       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     207    207       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     207    207       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     207    207       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     210    210       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     210    210       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     214    214       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     214    214       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     214    214       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     219    219       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     219    219       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     228    228       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     228    228       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     237    237       N6-glutaryllysine.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     279    279       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     280    280       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     280    280       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     287    287       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     287    287       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     307    307       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     307    307       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     307    307       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     310    310       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     310    310       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     400    400       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     402    402       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     402    402       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     412    412       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     412    412       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     412    412       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     453    453       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     453    453       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     458    458       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     458    458       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     458    458       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     522    522       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     522    522       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     527    527       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     527    527       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     527    527       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     532    532       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     532    532       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     537    537       Phosphoserine; alternate.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     540    540       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     553    553       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     553    553       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     553    553       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     560    560       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     560    560       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     569    569       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     575    575       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     575    575       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     603    603       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     603    603       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     612    612       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     612    612       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     630    630       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     728    728       N6-glutaryllysine.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     751    751       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     751    751       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     757    757       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     757    757       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     757    757       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     772    772       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     772    772       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     793    793       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     793    793       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     793    793       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     811    811       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     811    811       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     831    831       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     831    831       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     841    841       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     841    841       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     856    856       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     856    856       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     869    869       N6-glutaryllysine.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     875    875       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     875    875       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     875    875       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     889    889       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     889    889       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     889    889       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     892    892       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     892    892       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     892    892       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     896    896       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     898    898       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     908    908       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     908    908       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     915    915       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     915    915       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     915    915       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     919    919       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     919    919       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES     919    919       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     935    935       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1036   1036       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1074   1074       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1074   1074       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES    1074   1074       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1079   1079       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES    1090   1090       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1093   1093       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1100   1100       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1100   1100       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1149   1149       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1168   1168       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1168   1168       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES    1168   1168       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1183   1183       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1183   1183       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES    1183   1183       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1203   1203       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES    1222   1222       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1224   1224       N6-glutaryllysine.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES    1232   1232       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1232   1232       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1269   1269       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1269   1269       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1291   1291       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1291   1291       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1356   1356       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1356   1356       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES    1356   1356       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1360   1360       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES    1360   1360       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1419   1419       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES    1431   1431       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1444   1444       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1444   1444       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1471   1471       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1471   1471       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1479   1479       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1479   1479       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES    1479   1479       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1486   1486       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1486   1486       N6-glutaryllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31327}.
FT   MOD_RES    1486   1486       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   CARBOHYD    537    537       O-linked (GlcNAc) serine; alternate.
FT                                {ECO:0000269|PubMed:24098488}.
FT   CARBOHYD   1331   1331       O-linked (GlcNAc) serine.
FT                                {ECO:0000269|PubMed:24098488}.
FT   CARBOHYD   1332   1332       O-linked (GlcNAc) threonine.
FT                                {ECO:0000269|PubMed:24098488}.
FT   MUTAGEN    1391   1391       T->V: 400-fold increase in the activation
FT                                constant of NAG. 3-fold decrease in the
FT                                reaction rate at saturation of NAG.
FT                                {ECO:0000269|PubMed:19754428}.
FT   MUTAGEN    1394   1394       T->A: 900-fold increase in the activation
FT                                constant of NAG. 3-fold decrease in the
FT                                reaction rate at saturation of NAG.
FT                                {ECO:0000269|PubMed:19754428}.
FT   MUTAGEN    1410   1410       W->K: 60-fold increase in the activation
FT                                constant of NAG.
FT                                {ECO:0000269|PubMed:19754428}.
FT   MUTAGEN    1437   1437       N->D: 70-fold increase in the activation
FT                                constant of NAG.
FT                                {ECO:0000269|PubMed:19754428}.
FT   MUTAGEN    1440   1440       N->D: 110-fold increase in the activation
FT                                constant of NAG. Modifies the specificity
FT                                for the activator: Binds Phe-NAG
FT                                considerably better than NAG.
FT                                {ECO:0000269|PubMed:19754428}.
SQ   SEQUENCE   1500 AA;  164580 MW;  038E8F893DE1C34D CRC64;
     MTRILTACKV VKTLKSGFGL ANVTSKRQWD FSRPGIRLLS VKAQTAHIVL EDGTKMKGYS
     FGHPSSVAGE VVFNTGLGGY SEALTDPAYK GQILTMANPI IGNGGAPDTT ARDELGLNKY
     MESDGIKVAG LLVLNYSHDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML
     GKIEFEGQSV DFVDPNKQNL IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA
     EVHLVPWNHD FTQMDYDGLL 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
     PNKETLMDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT
     GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS
     RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR
     FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLR
     KELSEPSSTR IYAIAKALEN NMSLDEIVKL TSIDKWFLYK MRDILNMDKT LKGLNSESVT
     EETLRQAKEI 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 EHPVVLTKFI EGAREVEMDA VGKEGRVISH AISEHVEDAG
     VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA
     SRSFPFVSKT LGVDFIDVAT KVMIGESVDE KHLPTLEQPI IPSDYVAIKA PMFSWPRLRD
     ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ
     LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN
     NNTKFVHDNY VIRRTAVDSG IALLTNFQVT KLFAEAVQKA RTVDSKSLFH YRQYSAGKAA
//
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