ID PUR2_HUMAN Reviewed; 1010 AA. AC P22102; A8K945; A8KA32; D3DSF3; D3DSF4; O14659; Q52M77; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 27-MAR-2024, entry version 242. DE RecName: Full=Trifunctional purine biosynthetic protein adenosine-3 {ECO:0000305|PubMed:2183217}; DE Includes: DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000305|PubMed:2183217}; DE EC=6.3.4.13 {ECO:0000305|PubMed:20631005, ECO:0000305|PubMed:2183217}; DE AltName: Full=Glycinamide ribonucleotide synthetase; DE Short=GARS {ECO:0000303|PubMed:2183217}; DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000303|PubMed:2183217}; DE Includes: DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000305|PubMed:2183217}; DE EC=6.3.3.1 {ECO:0000305|PubMed:20631005, ECO:0000305|PubMed:2183217}; DE AltName: Full=AIR synthase; DE Short=AIRS {ECO:0000303|PubMed:2183217}; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase; DE Includes: DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000303|PubMed:2183217}; DE EC=2.1.2.2 {ECO:0000269|PubMed:12450384, ECO:0000269|PubMed:12755606, ECO:0000305|PubMed:20631005, ECO:0000305|PubMed:2183217}; DE AltName: Full=5'-phosphoribosylglycinamide transformylase; DE AltName: Full=GAR transformylase {ECO:0000303|PubMed:12450384}; DE Short=GART {ECO:0000303|PubMed:2183217}; GN Name=GART; Synonyms=PGFT, PRGS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RX PubMed=2147474; DOI=10.1093/nar/18.22.6665; RA Aimi J., Qiu H., Williams J., Zalkin H., Dixon J.E.; RT "De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs RT encoding the trifunctional glycinamide ribonucleotide synthetase- RT aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide RT transformylase by functional complementation in E. coli."; RL Nucleic Acids Res. 18:6665-6672(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANT ILE-421. RC TISSUE=Testis, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). RC TISSUE=Brain, and Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-432, AND VARIANT ILE-421. RX PubMed=9224613; DOI=10.1093/nar/25.15.3118; RA Kan J.L.C., Moran R.G.; RT "Intronic polyadenylation in the human glycinamide ribonucleotide RT formyltransferase gene."; RL Nucleic Acids Res. 25:3118-3123(1997). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 709-1010, FUNCTION, CATALYTIC ACTIVITY, RP PATHWAY, AND DOMAIN. RX PubMed=2183217; DOI=10.1073/pnas.87.8.2916; RA Schild D., Brake A.J., Kiefer M.C., Young D., Barr P.J.; RT "Cloning of three human multifunctional de novo purine biosynthetic genes RT by functional complementation of yeast mutations."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2916-2920(1990). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-350, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-440; THR-682; SER-796 RP AND SER-802, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] {ECO:0007744|PDB:1MEJ, ECO:0007744|PDB:1MEN, ECO:0007744|PDB:1MEO} RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 808-1010 IN COMPLEX WITH RP N(1)-(5-PHOSPHO-BETA-D-RIBOSYL)GLYCINAMIDE, FUNCTION, CATALYTIC ACTIVITY, RP PATHWAY, DOMAIN, AND REGION. RX PubMed=12450384; DOI=10.1021/bi020522m; RA Zhang Y., Desharnais J., Greasley S.E., Beardsley G.P., Boger D.L., RA Wilson I.A.; RT "Crystal structures of human GAR Tfase at low and high pH and with RT substrate beta-GAR."; RL Biochemistry 41:14206-14215(2002). RN [15] {ECO:0007744|PDB:1NJS} RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 808-1010 IN COMPLEX WITH RP FORMYLTETRAHYDROFOLATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND RP REGION. RX PubMed=12755606; DOI=10.1021/bi034219c; RA Zhang Y., Desharnais J., Marsilje T.H., Li C., Hedrick M.P., RA Gooljarsingh L.T., Tavassoli A., Benkovic S.J., Olson A.J., Boger D.L., RA Wilson I.A.; RT "Rational design, synthesis, evaluation, and crystal structure of a potent RT inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10- RT dideazaacyclic-5,6,7,8-tetrahydrofolic acid."; RL Biochemistry 42:6043-6056(2003). RN [16] {ECO:0007744|PDB:1ZLX, ECO:0007744|PDB:1ZLY} RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 808-1010 IN COMPLEX WITH RP SUBSTRATE ANALOGS, AND REGION. RX PubMed=16026156; DOI=10.1021/bi050307g; RA Dahms T.E., Sainz G., Giroux E.L., Caperelli C.A., Smith J.L.; RT "The apo and ternary complex structures of a chemotherapeutic target: human RT glycinamide ribonucleotide transformylase."; RL Biochemistry 44:9841-9850(2005). RN [17] {ECO:0007744|PDB:2QK4, ECO:0007744|PDB:2V9Y} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-430 AND 467-794 IN COMPLEX WITH RP ATP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, AND REGION. RX PubMed=20631005; DOI=10.1093/nar/gkq595; RA Welin M., Grossmann J.G., Flodin S., Nyman T., Stenmark P., Tresaugues L., RA Kotenyova T., Johansson I., Nordlund P., Lehtio L.; RT "Structural studies of tri-functional human GART."; RL Nucleic Acids Res. 38:7308-7319(2010). CC -!- FUNCTION: Trifunctional enzyme that catalyzes three distinct reactions CC as part of the 'de novo' inosine monophosphate biosynthetic pathway. CC {ECO:0000305|PubMed:12450384, ECO:0000305|PubMed:12755606, CC ECO:0000305|PubMed:20631005, ECO:0000305|PubMed:2183217}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + CC N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; CC Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, CC ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; CC Evidence={ECO:0000305|PubMed:20631005, ECO:0000305|PubMed:2183217}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17454; CC Evidence={ECO:0000305|PubMed:2183217}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D- CC ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)- CC formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide; CC Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, CC ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366; CC EC=2.1.2.2; Evidence={ECO:0000269|PubMed:12450384, CC ECO:0000269|PubMed:12755606}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15054; CC Evidence={ECO:0000305|PubMed:12450384}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; CC Evidence={ECO:0000305|PubMed:20631005, ECO:0000305|PubMed:2183217}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23033; CC Evidence={ECO:0000305|PubMed:2183217}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P15640, ECO:0000255|PROSITE- CC ProRule:PRU00409}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00409}; CC Note=Binds 1 magnesium or manganese ion per subunit. CC {ECO:0000255|PROSITE-ProRule:PRU00409}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 2/2. {ECO:0000305|PubMed:12450384}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)- CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1- CC diphosphate: step 2/2. {ECO:0000305|PubMed:2183217}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)- CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D- CC ribosyl)glycinamide (10-formyl THF route): step 1/1. CC {ECO:0000305|PubMed:2183217}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20631005}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P22102-1; Sequence=Displayed; CC Name=Short; CC IsoId=P22102-2; Sequence=VSP_005517; CC -!- DOMAIN: The N-terminal ATP-grasp domain carries the CC phosphoribosylamine--glycine ligase activity. CC {ECO:0000305|PubMed:20631005, ECO:0000305|PubMed:2183217}. CC -!- DOMAIN: The central AIRS domain carries the CC phosphoribosylformylglycinamidine cyclo-ligase activity. CC {ECO:0000305|PubMed:20631005, ECO:0000305|PubMed:2183217}. CC -!- DOMAIN: The C-terminal GART domain carries the CC phosphoribosylglycinamide formyltransferase activity. CC {ECO:0000269|PubMed:12450384, ECO:0000269|PubMed:12755606, CC ECO:0000269|PubMed:20631005}. CC -!- SIMILARITY: In the N-terminal section; belongs to the GARS family. CC {ECO:0000305}. CC -!- SIMILARITY: In the central section; belongs to the AIR synthase family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GART family. CC {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; X54199; CAA38119.1; -; mRNA. DR EMBL; AK292560; BAF85249.1; -; mRNA. DR EMBL; AK292897; BAF85586.1; -; mRNA. DR EMBL; CH471079; EAX09826.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09827.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09828.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09829.1; -; Genomic_DNA. DR EMBL; BC038958; AAH38958.1; -; mRNA. DR EMBL; BC093641; AAH93641.1; -; mRNA. DR EMBL; BC101565; AAI01566.1; -; mRNA. DR EMBL; AF008653; AAB70812.1; -; Genomic_DNA. DR EMBL; M32082; AAA60077.1; -; mRNA. DR CCDS; CCDS13627.1; -. [P22102-1] DR CCDS; CCDS13628.1; -. [P22102-2] DR PIR; S12616; AJHUPR. DR RefSeq; NP_000810.1; NM_000819.4. [P22102-1] DR RefSeq; NP_001129477.1; NM_001136005.1. [P22102-1] DR RefSeq; NP_001129478.1; NM_001136006.1. [P22102-1] DR RefSeq; NP_780294.1; NM_175085.2. [P22102-2] DR RefSeq; XP_005260998.1; XM_005260941.1. [P22102-1] DR RefSeq; XP_006724052.1; XM_006723989.1. [P22102-1] DR RefSeq; XP_006724053.1; XM_006723990.1. [P22102-1] DR RefSeq; XP_011527828.1; XM_011529526.1. [P22102-1] DR PDB; 1MEJ; X-ray; 2.00 A; A/B/C=810-1010. DR PDB; 1MEN; X-ray; 2.23 A; A/B/C=810-1010. DR PDB; 1MEO; X-ray; 1.72 A; A=808-1010. DR PDB; 1NJS; X-ray; 1.98 A; A/B=808-1010. DR PDB; 1RBM; X-ray; 2.30 A; A/B=808-1010. DR PDB; 1RBQ; X-ray; 2.10 A; A/B/C/D=808-1010. DR PDB; 1RBY; X-ray; 2.10 A; A/B/C/D=808-1010. DR PDB; 1RBZ; X-ray; 2.10 A; A/B=808-1010. DR PDB; 1RC0; X-ray; 2.05 A; A/B=808-1010. DR PDB; 1RC1; X-ray; 2.25 A; A/B=808-1010. DR PDB; 1ZLX; X-ray; 2.20 A; A=808-1010. DR PDB; 1ZLY; X-ray; 2.07 A; A=808-1010. DR PDB; 2QK4; X-ray; 2.45 A; A/B=1-430. DR PDB; 2V9Y; X-ray; 2.10 A; A/B=467-794. DR PDB; 4EW1; X-ray; 1.52 A; A=810-1010. DR PDB; 4EW2; X-ray; 1.60 A; A=808-1010. DR PDB; 4EW3; X-ray; 1.70 A; A=808-1010. DR PDB; 4ZYT; X-ray; 1.70 A; A=808-1010. DR PDB; 4ZYU; X-ray; 1.95 A; A=808-1010. DR PDB; 4ZYV; X-ray; 2.05 A; A=808-1010. DR PDB; 4ZYW; X-ray; 2.05 A; A=808-1010. DR PDB; 4ZYX; X-ray; 1.65 A; A=808-1010. DR PDB; 4ZYY; X-ray; 1.85 A; A=808-1010. DR PDB; 4ZYZ; X-ray; 1.60 A; A=808-1010. DR PDB; 4ZZ0; X-ray; 1.65 A; A=808-1010. DR PDB; 4ZZ1; X-ray; 1.35 A; A=808-1010. DR PDB; 4ZZ2; X-ray; 1.45 A; A=808-1010. DR PDB; 4ZZ3; X-ray; 2.50 A; A=808-1010. DR PDB; 5J9F; X-ray; 2.10 A; A=808-1010. DR PDB; 7JG0; X-ray; 1.98 A; A=808-1010. DR PDB; 7JG3; X-ray; 2.09 A; A=808-1010. DR PDB; 7JG4; X-ray; 2.46 A; A=808-1010. DR PDB; 8FDX; X-ray; 2.07 A; A=808-1010. DR PDB; 8FDY; X-ray; 2.06 A; A=808-1010. DR PDB; 8FDZ; X-ray; 2.48 A; A=808-1010. DR PDB; 8FE0; X-ray; 2.22 A; A=808-1010. DR PDB; 8FJV; X-ray; 2.69 A; A=808-1010. DR PDB; 8FJW; X-ray; 2.08 A; A=808-1010. DR PDB; 8FJX; X-ray; 2.17 A; A=808-1010. DR PDB; 8FJY; X-ray; 2.98 A; A=808-1010. DR PDBsum; 1MEJ; -. DR PDBsum; 1MEN; -. DR PDBsum; 1MEO; -. DR PDBsum; 1NJS; -. DR PDBsum; 1RBM; -. DR PDBsum; 1RBQ; -. DR PDBsum; 1RBY; -. DR PDBsum; 1RBZ; -. DR PDBsum; 1RC0; -. DR PDBsum; 1RC1; -. DR PDBsum; 1ZLX; -. DR PDBsum; 1ZLY; -. DR PDBsum; 2QK4; -. DR PDBsum; 2V9Y; -. DR PDBsum; 4EW1; -. DR PDBsum; 4EW2; -. DR PDBsum; 4EW3; -. DR PDBsum; 4ZYT; -. DR PDBsum; 4ZYU; -. DR PDBsum; 4ZYV; -. DR PDBsum; 4ZYW; -. DR PDBsum; 4ZYX; -. DR PDBsum; 4ZYY; -. DR PDBsum; 4ZYZ; -. DR PDBsum; 4ZZ0; -. DR PDBsum; 4ZZ1; -. DR PDBsum; 4ZZ2; -. DR PDBsum; 4ZZ3; -. DR PDBsum; 5J9F; -. DR PDBsum; 7JG0; -. DR PDBsum; 7JG3; -. DR PDBsum; 7JG4; -. DR PDBsum; 8FDX; -. DR PDBsum; 8FDY; -. DR PDBsum; 8FDZ; -. DR PDBsum; 8FE0; -. DR PDBsum; 8FJV; -. DR PDBsum; 8FJW; -. DR PDBsum; 8FJX; -. DR PDBsum; 8FJY; -. DR AlphaFoldDB; P22102; -. DR SMR; P22102; -. DR BioGRID; 108888; 221. DR IntAct; P22102; 52. DR MINT; P22102; -. DR STRING; 9606.ENSP00000371253; -. DR BindingDB; P22102; -. DR ChEMBL; CHEMBL3972; -. DR DrugBank; DB02236; Glycinamide Ribonucleotide. DR DrugBank; DB03546; N-({4-[(1R)-4-[(2R,4S,5S)-2,4-diamino-6-oxohexahydropyrimidin-5-yl]-1-(2,2,2-trifluoro-1,1-dihydroxyethyl)butyl]phenyl}carbonyl)-L-glutamic acid. DR DrugBank; DB00642; Pemetrexed. DR DrugCentral; P22102; -. DR GlyGen; P22102; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P22102; -. DR MetOSite; P22102; -. DR PhosphoSitePlus; P22102; -. DR SwissPalm; P22102; -. DR BioMuta; GART; -. DR DMDM; 131616; -. DR EPD; P22102; -. DR jPOST; P22102; -. DR MassIVE; P22102; -. DR MaxQB; P22102; -. DR PaxDb; 9606-ENSP00000371253; -. DR PeptideAtlas; P22102; -. DR ProteomicsDB; 53961; -. [P22102-1] DR ProteomicsDB; 53962; -. [P22102-2] DR Pumba; P22102; -. DR Antibodypedia; 1063; 250 antibodies from 31 providers. DR DNASU; 2618; -. DR Ensembl; ENST00000361093.9; ENSP00000354388.5; ENSG00000159131.17. [P22102-2] DR Ensembl; ENST00000381815.9; ENSP00000371236.4; ENSG00000159131.17. [P22102-1] DR Ensembl; ENST00000381831.7; ENSP00000371253.3; ENSG00000159131.17. [P22102-1] DR Ensembl; ENST00000381839.7; ENSP00000371261.3; ENSG00000159131.17. [P22102-1] DR Ensembl; ENST00000571089.2; ENSP00000459532.2; ENSG00000262473.5. DR Ensembl; ENST00000573055.5; ENSP00000459391.2; ENSG00000262473.5. DR Ensembl; ENST00000575273.5; ENSP00000461700.2; ENSG00000262473.5. DR GeneID; 2618; -. DR KEGG; hsa:2618; -. DR MANE-Select; ENST00000381815.9; ENSP00000371236.4; NM_000819.5; NP_000810.1. DR UCSC; uc002yrx.4; human. [P22102-1] DR AGR; HGNC:4163; -. DR CTD; 2618; -. DR DisGeNET; 2618; -. DR GeneCards; GART; -. DR HGNC; HGNC:4163; GART. DR HPA; ENSG00000159131; Low tissue specificity. DR MIM; 138440; gene. DR neXtProt; NX_P22102; -. DR OpenTargets; ENSG00000159131; -. DR PharmGKB; PA28576; -. DR VEuPathDB; HostDB:ENSG00000159131; -. DR eggNOG; KOG0237; Eukaryota. DR eggNOG; KOG3076; Eukaryota. DR GeneTree; ENSGT00390000000292; -. DR HOGENOM; CLU_005361_0_2_1; -. DR InParanoid; P22102; -. DR OMA; EVMQACC; -. DR OrthoDB; 729at2759; -. DR PhylomeDB; P22102; -. DR TreeFam; TF106368; -. DR BioCyc; MetaCyc:HS08358-MONOMER; -. DR BRENDA; 2.1.2.2; 2681. DR BRENDA; 6.3.4.13; 2681. DR PathwayCommons; P22102; -. DR Reactome; R-HSA-73817; Purine ribonucleoside monophosphate biosynthesis. DR SignaLink; P22102; -. DR SIGNOR; P22102; -. DR UniPathway; UPA00074; UER00125. DR UniPathway; UPA00074; UER00126. DR UniPathway; UPA00074; UER00129. DR BioGRID-ORCS; 2618; 201 hits in 1178 CRISPR screens. DR ChiTaRS; GART; human. DR EvolutionaryTrace; P22102; -. DR GenomeRNAi; 2618; -. DR Pharos; P22102; Tclin. DR PRO; PR:P22102; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P22102; Protein. DR Bgee; ENSG00000159131; Expressed in ventricular zone and 182 other cell types or tissues. DR ExpressionAtlas; P22102; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IBA:GO_Central. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IDA:MGI. DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IDA:MGI. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IDA:MGI. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IDA:MGI. DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; IDA:MGI. DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central. DR GO; GO:0003360; P:brainstem development; IEA:Ensembl. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl. DR GO; GO:0006544; P:glycine metabolic process; IEA:Ensembl. DR GO; GO:0006177; P:GMP biosynthetic process; IDA:MGI. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome. DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl. DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:Ensembl. DR CDD; cd08645; FMT_core_GART; 1. DR CDD; cd02196; PurM; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1. DR Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 1. DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1. DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1. DR HAMAP; MF_00741; AIRS; 1. DR HAMAP; MF_00138; GARS; 1. DR HAMAP; MF_01930; PurN; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR036477; Formyl_transf_N_sf. DR InterPro; IPR004607; GART. DR InterPro; IPR001555; GART_AS. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp. DR InterPro; IPR000115; PRibGlycinamide_synth. DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom. DR InterPro; IPR037123; PRibGlycinamide_synth_C_sf. DR InterPro; IPR020559; PRibGlycinamide_synth_CS. DR InterPro; IPR020562; PRibGlycinamide_synth_N. DR InterPro; IPR010918; PurM-like_C_dom. DR InterPro; IPR036676; PurM-like_C_sf. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR036921; PurM-like_N_sf. DR InterPro; IPR004733; PurM_cligase. DR InterPro; IPR011054; Rudment_hybrid_motif. DR NCBIfam; TIGR00877; purD; 1. DR NCBIfam; TIGR00878; purM; 1. DR NCBIfam; TIGR00639; PurN; 1. DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1. DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR Pfam; PF01071; GARS_A; 1. DR Pfam; PF02843; GARS_C; 1. DR Pfam; PF02844; GARS_N; 1. DR SMART; SM01209; GARS_A; 1. DR SMART; SM01210; GARS_C; 1. DR SUPFAM; SSF53328; Formyltransferase; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1. DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1. DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00184; GARS; 1. DR PROSITE; PS00373; GART; 1. DR Genevisible; P22102; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Ligase; KW Magnesium; Manganese; Metal-binding; Multifunctional enzyme; KW Nucleotide-binding; Phosphoprotein; Purine biosynthesis; KW Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..1010 FT /note="Trifunctional purine biosynthetic protein adenosine- FT 3" FT /id="PRO_0000074937" FT DOMAIN 111..318 FT /note="ATP-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT REGION 434..809 FT /note="AIRS domain" FT /evidence="ECO:0000250|UniProtKB:P21872" FT REGION 810..1010 FT /note="GART domain" FT /evidence="ECO:0000269|PubMed:12450384, FT ECO:0000269|PubMed:12755606, ECO:0007744|PDB:1MEN, FT ECO:0007744|PDB:1NJS" FT ACT_SITE 915 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P08179" FT BINDING 190..193 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:20631005, FT ECO:0007744|PDB:2QK4" FT BINDING 197 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:20631005, FT ECO:0007744|PDB:2QK4" FT BINDING 220 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:20631005, FT ECO:0007744|PDB:2QK4" FT BINDING 229 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:20631005, FT ECO:0007744|PDB:2QK4" FT BINDING 288 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 290 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 818..820 FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide" FT /ligand_id="ChEBI:CHEBI:143788" FT /evidence="ECO:0000269|PubMed:12450384, FT ECO:0000269|PubMed:16026156, ECO:0007744|PDB:1MEN, FT ECO:0007744|PDB:1ZLY" FT BINDING 871 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000305|PubMed:12755606, FT ECO:0007744|PDB:1NJS" FT BINDING 896..899 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000305|PubMed:12755606, FT ECO:0000305|PubMed:16026156, ECO:0007744|PDB:1NJS, FT ECO:0007744|PDB:1ZLY" FT BINDING 913 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000305|PubMed:12755606, FT ECO:0007744|PDB:1NJS" FT BINDING 947..951 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000305|PubMed:12755606, FT ECO:0000305|PubMed:16026156, ECO:0007744|PDB:1NJS, FT ECO:0007744|PDB:1ZLY" FT BINDING 977..980 FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide" FT /ligand_id="ChEBI:CHEBI:143788" FT /evidence="ECO:0000269|PubMed:12450384, FT ECO:0000269|PubMed:16026156, ECO:0007744|PDB:1MEN, FT ECO:0007744|PDB:1ZLY" FT SITE 951 FT /note="Raises pKa of active site His" FT /evidence="ECO:0000250|UniProtKB:P08179" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 350 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 440 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 682 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 796 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 802 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 434..1010 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_005517" FT VARIANT 21 FT /note="L -> F (in dbSNP:rs1804387)" FT /id="VAR_011817" FT VARIANT 421 FT /note="V -> I (in dbSNP:rs8788)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9224613" FT /id="VAR_011818" FT VARIANT 510 FT /note="D -> G (in dbSNP:rs35927582)" FT /id="VAR_051882" FT VARIANT 641 FT /note="P -> A (in dbSNP:rs34588874)" FT /id="VAR_051883" FT VARIANT 752 FT /note="D -> G (in dbSNP:rs8971)" FT /id="VAR_011819" FT STRAND 2..9 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 12..21 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 27..34 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 40..47 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 55..65 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 69..72 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 76..79 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 82..88 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:2QK4" FT TURN 98..101 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 102..105 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 107..116 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 124..129 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 130..139 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 144..151 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 164..174 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 187..191 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 195..204 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 215..222 FT /evidence="ECO:0007829|PDB:2QK4" FT TURN 223..225 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 226..238 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 244..253 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 255..264 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 271..280 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 283..292 FT /evidence="ECO:0007829|PDB:2QK4" FT TURN 295..297 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 298..301 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 309..317 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 321..324 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 333..340 FT /evidence="ECO:0007829|PDB:2QK4" FT TURN 342..345 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 357..362 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 366..375 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 378..381 FT /evidence="ECO:0007829|PDB:2QK4" FT STRAND 383..395 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 396..409 FT /evidence="ECO:0007829|PDB:2QK4" FT HELIX 423..428 FT /evidence="ECO:0007829|PDB:2QK4" FT TURN 479..483 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 485..494 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 499..506 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 512..525 FT /evidence="ECO:0007829|PDB:2V9Y" FT TURN 526..528 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 530..542 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 545..562 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 565..573 FT /evidence="ECO:0007829|PDB:2V9Y" FT TURN 575..577 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 583..594 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 595..597 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 602..604 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 610..615 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 617..619 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 624..633 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 648..650 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 651..655 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 663..671 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 677..680 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 685..689 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 691..693 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 698..703 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 704..706 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 711..720 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 724..730 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 735..741 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 743..745 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 746..755 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 760..768 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 776..779 FT /evidence="ECO:0007829|PDB:2V9Y" FT HELIX 781..785 FT /evidence="ECO:0007829|PDB:2V9Y" FT STRAND 809..816 FT /evidence="ECO:0007829|PDB:4ZZ1" FT HELIX 819..828 FT /evidence="ECO:0007829|PDB:4ZZ1" FT STRAND 836..844 FT /evidence="ECO:0007829|PDB:4ZZ1" FT HELIX 848..855 FT /evidence="ECO:0007829|PDB:4ZZ1" FT STRAND 860..862 FT /evidence="ECO:0007829|PDB:4ZZ1" FT HELIX 865..867 FT /evidence="ECO:0007829|PDB:4ZZ1" FT STRAND 868..870 FT /evidence="ECO:0007829|PDB:4ZZ1" FT HELIX 871..884 FT /evidence="ECO:0007829|PDB:4ZZ1" FT STRAND 888..894 FT /evidence="ECO:0007829|PDB:4ZZ1" FT HELIX 901..906 FT /evidence="ECO:0007829|PDB:4ZZ1" FT TURN 907..909 FT /evidence="ECO:0007829|PDB:4ZZ1" FT STRAND 910..917 FT /evidence="ECO:0007829|PDB:4ZZ1" FT TURN 919..922 FT /evidence="ECO:0007829|PDB:4ZZ1" FT HELIX 927..934 FT /evidence="ECO:0007829|PDB:4ZZ1" FT STRAND 937..945 FT /evidence="ECO:0007829|PDB:4ZZ1" FT STRAND 955..962 FT /evidence="ECO:0007829|PDB:4ZZ1" FT HELIX 969..992 FT /evidence="ECO:0007829|PDB:4ZZ1" FT STRAND 995..998 FT /evidence="ECO:0007829|PDB:4ZZ1" FT STRAND 1002..1006 FT /evidence="ECO:0007829|PDB:4ZZ1" SQ SEQUENCE 1010 AA; 107767 MW; 9A4213F746EB17A2 CRC64; MAARVLIIGS GGREHTLAWK LAQSHHVKQV LVAPGNAGTA CSEKISNTAI SISDHTALAQ FCKEKKIEFV VVGPEAPLAA GIVGNLRSAG VQCFGPTAEA AQLESSKRFA KEFMDRHGIP TAQWKAFTKP EEACSFILSA DFPALVVKAS GLAAGKGVIV AKSKEEACKA VQEIMQEKAF GAAGETIVIE ELLDGEEVSC LCFTDGKTVA PMPPAQDHKR LLEGDGGPNT GGMGAYCPAP QVSNDLLLKI KDTVLQRTVD GMQQEGTPYT GILYAGIMLT KNGPKVLEFN CRFGDPECQV ILPLLKSDLY EVIQSTLDGL LCTSLPVWLE NHTALTVVMA SKGYPGDYTK GVEITGFPEA QALGLEVFHA GTALKNGKVV THGGRVLAVT AIRENLISAL EEAKKGLAAI KFEGAIYRKD VGFRAIAFLQ QPRSLTYKES GVDIAAGNML VKKIQPLAKA TSRSGCKVDL GGFAGLFDLK AAGFKDPLLA SGTDGVGTKL KIAQLCNKHD TIGQDLVAMC VNDILAQGAE PLFFLDYFSC GKLDLSVTEA VVAGIAKACG KAGCALLGGE TAEMPDMYPP GEYDLAGFAV GAMERDQKLP HLERITEGDV VVGIASSGLH SNGFSLVRKI VAKSSLQYSS PAPDGCGDQT LGDLLLTPTR IYSHSLLPVL RSGHVKAFAH ITGGGLLENI PRVLPEKLGV DLDAQTWRIP RVFSWLQQEG HLSEEEMART FNCGVGAVLV VSKEQTEQIL RDIQQHKEEA WVIGSVVARA EGSPRVKVKN LIESMQINGS VLKNGSLTNH FSFEKKKARV AVLISGTGSN LQALIDSTRE PNSSAQIDIV ISNKAAVAGL DKAERAGIPT RVINHKLYKN RVEFDSAIDL VLEEFSIDIV CLAGFMRILS GPFVQKWNGK MLNIHPSLLP SFKGSNAHEQ ALETGVTVTG CTVHFVAEDV DAGQIILQEA VPVKRGDTVA TLSERVKLAE HKIFPAALQL VASGTVQLGE NGKICWVKEE //