PUR2_HUMAN
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 03-AUG-2022, entry version 233.
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-dideazaacyclic-
RT 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=(6S)-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:57454, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286;
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,
CC ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-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}.
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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 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 AlphaFoldDB; P22102; -.
DR SMR; P22102; -.
DR BioGRID; 108888; 147.
DR IntAct; P22102; 48.
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; P22102; -.
DR PeptideAtlas; P22102; -.
DR PRIDE; P22102; -.
DR ProteomicsDB; 53961; -. [P22102-1]
DR ProteomicsDB; 53962; -. [P22102-2]
DR Antibodypedia; 1063; 214 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 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; 105366at2759; -.
DR PhylomeDB; P22102; -.
DR TreeFam; TF106368; -.
DR BioCyc; MetaCyc:HS08358-MON; -.
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; 176 hits in 1080 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 180 other tissues.
DR ExpressionAtlas; P22102; baseline and differential.
DR Genevisible; P22102; HS.
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; 3.30.1330.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.90.600.10; -; 1.
DR Gene3D; 3.90.650.10; -; 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 PANTHER; PTHR10520; PTHR10520; 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; SM01210; GARS_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00877; purD; 1.
DR TIGRFAMs; TIGR00878; purM; 1.
DR TIGRFAMs; TIGR00639; PurN; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
DR PROSITE; PS00373; GART; 1.
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="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000305|PubMed:12755606,
FT ECO:0007744|PDB:1NJS"
FT BINDING 896..899
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
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="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000305|PubMed:12755606,
FT ECO:0007744|PDB:1NJS"
FT BINDING 947..951
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
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
