ID PUR9_MOUSE Reviewed; 592 AA. AC Q9CWJ9; Q3UTQ3; Q80UH0; Q8BPF0; Q8BQV9; Q9CRI1; Q9CZW9; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 27-MAR-2024, entry version 172. DE RecName: Full=Bifunctional purine biosynthesis protein ATIC; DE AltName: Full=AICAR transformylase/inosine monophosphate cyclohydrolase; DE Short=ATIC; DE Includes: DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase; DE EC=2.1.2.3 {ECO:0000269|PubMed:29072452}; DE AltName: Full=5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase; DE Short=AICAR formyltransferase; DE AltName: Full=AICAR transformylase; DE Includes: DE RecName: Full=Inosine 5'-monophosphate cyclohydrolase {ECO:0000305}; DE Short=IMP cyclohydrolase {ECO:0000305}; DE EC=3.5.4.10 {ECO:0000250|UniProtKB:P31939}; DE AltName: Full=IMP synthase; DE AltName: Full=Inosinicase; GN Name=Atic; Synonyms=Purh; 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 MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Cerebellum, Corpora quadrigemina, and Embryonic stem cell; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=129; TISSUE=Mammary tumor; 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 98-108; 178-194 AND 531-545, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Friebe K., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; 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 [5] RP FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=29072452; DOI=10.1021/acs.jmedchem.7b01046; RA Fales K.R., Njoroge F.G., Brooks H.B., Thibodeaux S., Torrado A., Si C., RA Toth J.L., Mc Cowan J.R., Roth K.D., Thrasher K.J., Frimpong K., Lee M.R., RA Dally R.D., Shepherd T.A., Durham T.B., Margolis B.J., Wu Z., Wang Y., RA Atwell S., Wang J., Hui Y.H., Meier T.I., Konicek S.A., Geeganage S.; RT "Discovery of LSN 3213128, a Potent and Selective Nonclassical Antifolate RT Aminoimidazole-4-carboxamide Ribonucleotide Formyltransferase (AICARFT) RT Inhibitor Effective at Tumor Suppression in a Cancer Xenograft Model."; RL J. Med. Chem. 60:9599-9616(2017). CC -!- FUNCTION: Bifunctional enzyme that catalyzes the last two steps of CC purine biosynthesis (PubMed:29072452). Acts as a transformylase that CC incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5- CC phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the CC intermediate formyl-AICAR (FAICAR) (PubMed:29072452). Also displays CC cyclohydrolase activity involving the cyclization of FAICAR to IMP. Can CC use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the CC formyl donor in this reaction. Also catalyzes the cyclization of FAICAR CC to IMP. Promotes insulin receptor/INSR autophosphorylation and is CC involved in INSR internalization (By similarity). CC {ECO:0000250|UniProtKB:P31939, ECO:0000269|PubMed:29072452}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D- CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467, CC ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.1.2.3; CC Evidence={ECO:0000269|PubMed:29072452}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22193; CC Evidence={ECO:0000269|PubMed:29072452}; CC -!- CATALYTIC ACTIVITY: CC Reaction=10-formyldihydrofolate + 5-amino-1-(5-phospho-beta-D- CC ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamide + 7,8-dihydrofolate; CC Xref=Rhea:RHEA:59144, ChEBI:CHEBI:57451, ChEBI:CHEBI:57452, CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; CC Evidence={ECO:0000250|UniProtKB:P31939}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59145; CC Evidence={ECO:0000250|UniProtKB:P31939}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10; CC Evidence={ECO:0000250|UniProtKB:P31939}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18447; CC Evidence={ECO:0000250|UniProtKB:P31939}; CC -!- ACTIVITY REGULATION: AMP and XMP inhibit AICAR formyltransferase CC activity (By similarity). AICAR formyltransferase activity is inhibited CC by N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5- [(3R)-3- CC hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide (LSN 3213128), which CC acts as a tumor suppression in cancer cell lines (PubMed:29072452). CC {ECO:0000250|UniProtKB:P31939, ECO:0000269|PubMed:29072452}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino- CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): CC step 1/1. {ECO:0000269|PubMed:29072452}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step CC 1/1. {ECO:0000250|UniProtKB:P31939}. CC -!- SUBUNIT: Homodimer. Associates with internalized INSR complexes on CC Golgi/endosomal membranes. Interacts with INSR; ATIC together with CC PRKAA2/AMPK2 and HACD3/PTPLAD1 is proposed to be part of a signaling CC network regulating INSR autophosphorylation and endocytosis. CC {ECO:0000250|UniProtKB:P31939}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P54113}. CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal CC region. {ECO:0000250|UniProtKB:P31939}. CC -!- MISCELLANEOUS: The de novo purine synthesis pathway includes 10 CC sequential steps, beginning with phosphoribosyl pyrophosphate and CC ending with inositol monophosphate (IMP), the first purin compound of CC the pathway. {ECO:0000250|UniProtKB:P31939}. CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB28011.1; Type=Frameshift; Evidence={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; AK010449; BAB26949.3; -; mRNA. DR EMBL; AK010611; BAB27060.1; -; mRNA. DR EMBL; AK012074; BAB28011.1; ALT_FRAME; mRNA. DR EMBL; AK046353; BAC32688.1; -; mRNA. DR EMBL; AK076091; BAC36175.1; -; mRNA. DR EMBL; AK139235; BAE23927.1; -; mRNA. DR EMBL; BC039925; AAH39925.2; -; mRNA. DR CCDS; CCDS15030.1; -. DR RefSeq; NP_080471.2; NM_026195.3. DR AlphaFoldDB; Q9CWJ9; -. DR SMR; Q9CWJ9; -. DR BioGRID; 223864; 19. DR IntAct; Q9CWJ9; 1. DR STRING; 10090.ENSMUSP00000027384; -. DR BindingDB; Q9CWJ9; -. DR ChEMBL; CHEMBL2277; -. DR iPTMnet; Q9CWJ9; -. DR PhosphoSitePlus; Q9CWJ9; -. DR SwissPalm; Q9CWJ9; -. DR REPRODUCTION-2DPAGE; Q9CWJ9; -. DR CPTAC; non-CPTAC-3870; -. DR CPTAC; non-CPTAC-3941; -. DR EPD; Q9CWJ9; -. DR jPOST; Q9CWJ9; -. DR MaxQB; Q9CWJ9; -. DR PaxDb; 10090-ENSMUSP00000027384; -. DR PeptideAtlas; Q9CWJ9; -. DR ProteomicsDB; 301954; -. DR Pumba; Q9CWJ9; -. DR Antibodypedia; 4601; 480 antibodies from 36 providers. DR DNASU; 108147; -. DR Ensembl; ENSMUST00000027384.6; ENSMUSP00000027384.6; ENSMUSG00000026192.14. DR GeneID; 108147; -. DR KEGG; mmu:108147; -. DR UCSC; uc007bjs.2; mouse. DR AGR; MGI:1351352; -. DR CTD; 471; -. DR MGI; MGI:1351352; Atic. DR VEuPathDB; HostDB:ENSMUSG00000026192; -. DR eggNOG; KOG2555; Eukaryota. DR GeneTree; ENSGT00390000004553; -. DR HOGENOM; CLU_016316_3_2_1; -. DR InParanoid; Q9CWJ9; -. DR OMA; IKHNNPC; -. DR OrthoDB; 275312at2759; -. DR PhylomeDB; Q9CWJ9; -. DR TreeFam; TF105642; -. DR Reactome; R-MMU-73817; Purine ribonucleoside monophosphate biosynthesis. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR BioGRID-ORCS; 108147; 23 hits in 79 CRISPR screens. DR ChiTaRS; Atic; mouse. DR PRO; PR:Q9CWJ9; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q9CWJ9; Protein. DR Bgee; ENSMUSG00000026192; Expressed in manus and 231 other cell types or tissues. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IMP:MGI. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IMP:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IMP:MGI. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IMP:MGI. DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; IMP:MGI. DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl. DR GO; GO:0003360; P:brainstem development; IEA:Ensembl. DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl. DR GO; GO:0046452; P:dihydrofolate metabolic process; ISO:MGI. DR GO; GO:0006177; P:GMP biosynthetic process; IMP:MGI. DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; ISO:MGI. DR CDD; cd01421; IMPCH; 1. DR Gene3D; 1.10.287.440; -; 1. DR Gene3D; 3.40.140.20; -; 2. DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1. DR HAMAP; MF_00139; PurH; 1. DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf. DR InterPro; IPR024050; AICAR_Tfase_insert_dom_sf. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR036914; MGS-like_dom_sf. DR InterPro; IPR002695; PurH-like. DR NCBIfam; TIGR00355; purH; 1. DR PANTHER; PTHR11692:SF0; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC; 1. DR PANTHER; PTHR11692; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH; 1. DR Pfam; PF01808; AICARFT_IMPCHas; 1. DR Pfam; PF02142; MGS; 1. DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1. DR SMART; SM00798; AICARFT_IMPCHas; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF53927; Cytidine deaminase-like; 1. DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1. DR PROSITE; PS51855; MGS; 1. DR Genevisible; Q9CWJ9; MM. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; KW Multifunctional enzyme; Purine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1..592 FT /note="Bifunctional purine biosynthesis protein ATIC" FT /id="PRO_0000192157" FT DOMAIN 1..146 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" FT REGION 1..198 FT /note="IMP cyclohydrolase" FT /evidence="ECO:0000250|UniProtKB:P31335" FT REGION 199..592 FT /note="AICAR formyltransferase" FT /evidence="ECO:0000250|UniProtKB:P31335" FT ACT_SITE 137 FT /note="Proton donor/acceptor; for FAICAR cyclization FT activity" FT /evidence="ECO:0000250|UniProtKB:P31939" FT ACT_SITE 267 FT /note="Proton acceptor; for AICAR formyltransferase FT activity" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 12..14 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 34..37 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 64..67 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 101..102 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 125..126 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 207..208 FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- FT carboxamide" FT /ligand_id="ChEBI:CHEBI:58475" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 267 FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- FT carboxamide" FT /ligand_id="ChEBI:CHEBI:58475" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 316 FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- FT carboxamide" FT /ligand_id="ChEBI:CHEBI:58475" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 339 FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- FT carboxamide" FT /ligand_id="ChEBI:CHEBI:58475" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 431 FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- FT carboxamide" FT /ligand_id="ChEBI:CHEBI:58475" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 451 FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- FT carboxamide" FT /ligand_id="ChEBI:CHEBI:58475" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 452 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000250|UniProtKB:P31335" FT BINDING 541 FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- FT carboxamide" FT /ligand_id="ChEBI:CHEBI:58475" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P31939" FT BINDING 546 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000250|UniProtKB:P31335" FT BINDING 565..566 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000250|UniProtKB:P31335" FT BINDING 588 FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- FT carboxamide" FT /ligand_id="ChEBI:CHEBI:58475" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P31939" FT SITE 266 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P31939" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P31939" FT MOD_RES 199 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P31939" FT CONFLICT 22 FT /note="R -> K (in Ref. 1; BAB26949)" FT /evidence="ECO:0000305" FT CONFLICT 183 FT /note="A -> T (in Ref. 1; BAE23927)" FT /evidence="ECO:0000305" FT CONFLICT 219 FT /note="L -> S (in Ref. 2; AAH39925)" FT /evidence="ECO:0000305" FT CONFLICT 371 FT /note="Y -> C (in Ref. 1; BAB27060)" FT /evidence="ECO:0000305" SQ SEQUENCE 592 AA; 64217 MW; 8C5278040059FB5D CRC64; MAPSQLALFS VSDKTGLVEF ARSLASLGLS LVASGGTAKA IRDAGLAVRD VSELTGFPEM LGGRVKTLHP AVHAGILARN IPEDAADMAR LDFNLVRVVV CNLYPFVKTV ASPDVTVEAA VEQIDIGGVT LLRAAAKNHA RVTVVCEPED YAGVAAEMHG SDSKDTSLET RRHLALKAFT HTAQYDEAIS DYFRKQYSKG ISQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL CDALNAWQLV TELRGAVDIP AAASFKHVSP AGAAVGVPLS EDEARVCMVY DLYPTLTPLA VAYARARGAD RMSSFGDFVA LSDICDVPTA KIISREVSDG IVAPGYEEEA LKILSKKKNG NYCVLQMDQS YKPDENEVRT LFGLRLSQKR NNGVVDKSLF SNIVTKNKDL PESALRDLIV ATVAVKYTQS NSVCYAKDGQ VIGIGAGQQS RIHCTRLAGD KANSWWLRHH PRVLSMKFKA GVKRAEISNA IDQYVTGTIG EGEDLVKWEA LFEEVPELLT EAEKKEWVDK LSGVSVSSDA FFPFRDNVDR AKRSGVAYIV APSGSTADKV VIEACDELGI VLAHTDLRLF HH //