GUAD_HUMAN
ID GUAD_HUMAN Reviewed; 454 AA.
AC Q9Y2T3; B4DTY5; Q5SZC7; Q9H335; Q9ULG2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Guanine deaminase;
DE Short=Guanase;
DE Short=Guanine aminase;
DE EC=3.5.4.3 {ECO:0000269|PubMed:10075721, ECO:0000269|PubMed:22662200};
DE AltName: Full=Guanine aminohydrolase;
DE Short=GAH;
DE AltName: Full=p51-nedasin;
GN Name=GDA {ECO:0000312|HGNC:HGNC:4212};
GN Synonyms=KIAA1258 {ECO:0000303|PubMed:10574462};
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Brain;
RX PubMed=10075721; DOI=10.1074/jbc.274.12.8175;
RA Yuan G., Bin J.C., McKay D.J., Snyder F.F.;
RT "Cloning and characterization of human guanine deaminase. Purification and
RT partial amino acid sequence of the mouse protein.";
RL J. Biol. Chem. 274:8175-8180(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10542258; DOI=10.1074/jbc.274.45.32204;
RA Kuwahara H., Araki N., Makino K., Masuko N., Honda S., Kaibuchi K.,
RA Fukunaga K., Miyamoto E., Ogawa M., Saya H.;
RT "A novel NE-dlg/SAP102-associated protein, p51-nedasin, related to the
RT amidohydrolase superfamily, interferes with the association between NE-
RT dlg/SAP102 and N-methyl-D-aspartate receptor.";
RL J. Biol. Chem. 274:32204-32214(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Park K.H., Seong Y.S., Park J.B.;
RT "Molecular cloning of human guanine aminohydrolase.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [9]
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 [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP XANTHINE.
RG Structural genomics consortium (SGC);
RT "Human guanine deaminase (GUAD) in complex with zinc and its product
RT xanthine.";
RL Submitted (JAN-2008) to the PDB data bank.
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS).
RX PubMed=19470646; DOI=10.1073/pnas.0811070106;
RA Murphy P.M., Bolduc J.M., Gallaher J.L., Stoddard B.L., Baker D.;
RT "Alteration of enzyme specificity by computational loop remodeling and
RT design.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9215-9220(2009).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP SUBSTRATE ANALOG VALACICLOVIR, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22662200; DOI=10.1371/journal.pone.0037724;
RA Egeblad L., Welin M., Flodin S., Graslund S., Wang L., Balzarini J.,
RA Eriksson S., Nordlund P.;
RT "Pan-pathway based interaction profiling of FDA-approved nucleoside and
RT nucleobase analogs with enzymes of the human nucleotide metabolism.";
RL PLoS ONE 7:E37724-E37724(2012).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing
CC xanthine and ammonia. {ECO:0000269|PubMed:10075721,
CC ECO:0000269|PubMed:22662200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanine + H(+) + H2O = NH4(+) + xanthine;
CC Xref=Rhea:RHEA:14665, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16235, ChEBI:CHEBI:17712, ChEBI:CHEBI:28938; EC=3.5.4.3;
CC Evidence={ECO:0000269|PubMed:10075721, ECO:0000269|PubMed:22662200};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14666;
CC Evidence={ECO:0000269|PubMed:10075721, ECO:0000269|PubMed:22662200};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22662200};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22662200};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.5 uM for guanine {ECO:0000269|PubMed:10075721};
CC Note=kcat is 17.4 sec(-1) with guanine as substrate.
CC {ECO:0000269|PubMed:10075721};
CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC step 1/1. {ECO:0000269|PubMed:10075721}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.11}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y2T3-1; Sequence=Displayed;
CC Name=2; Synonyms=c;
CC IsoId=Q9Y2T3-2; Sequence=VSP_042075;
CC Name=3; Synonyms=a;
CC IsoId=Q9Y2T3-3; Sequence=VSP_042076;
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86572.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF095286; AAD25978.1; -; mRNA.
DR EMBL; AF019638; AAF13301.1; -; mRNA.
DR EMBL; AF144745; AAG40469.1; -; mRNA.
DR EMBL; AB033084; BAA86572.1; ALT_INIT; mRNA.
DR EMBL; AK300418; BAG62147.1; -; mRNA.
DR EMBL; AK315988; BAH14359.1; -; mRNA.
DR EMBL; AL583829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL135924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62529.1; -; Genomic_DNA.
DR EMBL; BC053584; AAH53584.1; -; mRNA.
DR CCDS; CCDS56576.1; -. [Q9Y2T3-3]
DR CCDS; CCDS56577.1; -. [Q9Y2T3-2]
DR CCDS; CCDS6641.1; -. [Q9Y2T3-1]
DR RefSeq; NP_001229434.1; NM_001242505.2. [Q9Y2T3-3]
DR RefSeq; NP_001229435.1; NM_001242506.2. [Q9Y2T3-2]
DR RefSeq; NP_001229436.1; NM_001242507.2. [Q9Y2T3-2]
DR RefSeq; NP_004284.1; NM_004293.4. [Q9Y2T3-1]
DR RefSeq; XP_005252374.1; XM_005252317.1. [Q9Y2T3-3]
DR RefSeq; XP_016870825.1; XM_017015336.1.
DR PDB; 2UZ9; X-ray; 2.30 A; A=1-454.
DR PDB; 3E0L; X-ray; 2.37 A; A/B=1-454.
DR PDB; 4AQL; X-ray; 1.99 A; A=1-454.
DR PDBsum; 2UZ9; -.
DR PDBsum; 3E0L; -.
DR PDBsum; 4AQL; -.
DR AlphaFoldDB; Q9Y2T3; -.
DR SMR; Q9Y2T3; -.
DR BioGRID; 114976; 61.
DR IntAct; Q9Y2T3; 4.
DR MINT; Q9Y2T3; -.
DR STRING; 9606.ENSP00000238018; -.
DR BindingDB; Q9Y2T3; -.
DR ChEMBL; CHEMBL3129; -.
DR DrugCentral; Q9Y2T3; -.
DR MEROPS; M38.981; -.
DR iPTMnet; Q9Y2T3; -.
DR PhosphoSitePlus; Q9Y2T3; -.
DR BioMuta; GDA; -.
DR DMDM; 9910736; -.
DR EPD; Q9Y2T3; -.
DR jPOST; Q9Y2T3; -.
DR MassIVE; Q9Y2T3; -.
DR MaxQB; Q9Y2T3; -.
DR PaxDb; Q9Y2T3; -.
DR PeptideAtlas; Q9Y2T3; -.
DR PRIDE; Q9Y2T3; -.
DR ProteomicsDB; 85890; -. [Q9Y2T3-1]
DR ProteomicsDB; 85891; -. [Q9Y2T3-2]
DR ProteomicsDB; 85892; -. [Q9Y2T3-3]
DR Antibodypedia; 12519; 266 antibodies from 24 providers.
DR DNASU; 9615; -.
DR Ensembl; ENST00000238018.8; ENSP00000238018.4; ENSG00000119125.17. [Q9Y2T3-3]
DR Ensembl; ENST00000358399.8; ENSP00000351170.4; ENSG00000119125.17. [Q9Y2T3-1]
DR Ensembl; ENST00000475764.5; ENSP00000436619.1; ENSG00000119125.17. [Q9Y2T3-1]
DR Ensembl; ENST00000545168.5; ENSP00000437972.1; ENSG00000119125.17. [Q9Y2T3-2]
DR GeneID; 9615; -.
DR KEGG; hsa:9615; -.
DR MANE-Select; ENST00000358399.8; ENSP00000351170.4; NM_004293.5; NP_004284.1.
DR UCSC; uc004aiq.4; human. [Q9Y2T3-1]
DR CTD; 9615; -.
DR DisGeNET; 9615; -.
DR GeneCards; GDA; -.
DR HGNC; HGNC:4212; GDA.
DR HPA; ENSG00000119125; Tissue enhanced (brain, intestine, kidney, liver).
DR MIM; 139260; gene.
DR neXtProt; NX_Q9Y2T3; -.
DR OpenTargets; ENSG00000119125; -.
DR PharmGKB; PA28625; -.
DR VEuPathDB; HostDB:ENSG00000119125; -.
DR eggNOG; KOG3968; Eukaryota.
DR GeneTree; ENSGT00390000017130; -.
DR HOGENOM; CLU_012358_0_1_1; -.
DR InParanoid; Q9Y2T3; -.
DR OMA; ALIGKVC; -.
DR OrthoDB; 612054at2759; -.
DR PhylomeDB; Q9Y2T3; -.
DR TreeFam; TF324539; -.
DR BioCyc; MetaCyc:HS04276-MON; -.
DR BRENDA; 3.5.4.3; 2681.
DR PathwayCommons; Q9Y2T3; -.
DR Reactome; R-HSA-74259; Purine catabolism.
DR SABIO-RK; Q9Y2T3; -.
DR SignaLink; Q9Y2T3; -.
DR UniPathway; UPA00603; UER00660.
DR BioGRID-ORCS; 9615; 18 hits in 1075 CRISPR screens.
DR ChiTaRS; GDA; human.
DR EvolutionaryTrace; Q9Y2T3; -.
DR GenomeRNAi; 9615; -.
DR Pharos; Q9Y2T3; Tbio.
DR PRO; PR:Q9Y2T3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y2T3; protein.
DR Bgee; ENSG00000119125; Expressed in ileal mucosa and 139 other tissues.
DR ExpressionAtlas; Q9Y2T3; baseline and differential.
DR Genevisible; Q9Y2T3; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR GO; GO:0008892; F:guanine deaminase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0000255; P:allantoin metabolic process; IEA:Ensembl.
DR GO; GO:0006161; P:deoxyguanosine catabolic process; IEA:Ensembl.
DR GO; GO:0046055; P:dGMP catabolic process; IEA:Ensembl.
DR GO; GO:0046038; P:GMP catabolic process; IEA:Ensembl.
DR GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046098; P:guanine metabolic process; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR CDD; cd01303; GDEase; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR014311; Guanine_deaminase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11271:SF6; PTHR11271:SF6; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02967; guan_deamin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..454
FT /note="Guanine deaminase"
FT /id="PRO_0000122298"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22662200,
FT ECO:0007744|PDB:2UZ9"
FT BINDING 84..87
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:22662200,
FT ECO:0007744|PDB:2UZ9"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22662200,
FT ECO:0007744|PDB:2UZ9"
FT BINDING 213..214
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:22662200,
FT ECO:0007744|PDB:2UZ9"
FT BINDING 240..243
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:22662200,
FT ECO:0007744|PDB:2UZ9"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22662200,
FT ECO:0007744|PDB:2UZ9"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:22662200,
FT ECO:0007744|PDB:2UZ9"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22662200,
FT ECO:0007744|PDB:2UZ9"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTT6"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10542258,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_042075"
FT VAR_SEQ 454
FT /note="V -> VKETIHLPASSPHPPPFP (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_042076"
FT CONFLICT 316..318
FT /note="LEV -> ARI (in Ref. 3; AAG40469)"
FT /evidence="ECO:0000305"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2UZ9"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2UZ9"
FT HELIX 184..201
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4AQL"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:4AQL"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 315..320
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:4AQL"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 339..355
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 365..372
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 374..379
FT /evidence="ECO:0007829|PDB:4AQL"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 423..431
FT /evidence="ECO:0007829|PDB:4AQL"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:4AQL"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:4AQL"
SQ SEQUENCE 454 AA; 51003 MW; A45C868E6EEA7380 CRC64;
MCAAQMPPLA HIFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEEASQ QEKLAKEWCF
KPCEIRELSH HEFFMPGLVD THIHASQYSF AGSSIDLPLL EWLTKYTFPA EHRFQNIDFA
EEVYTRVVRR TLKNGTTTAC YFATIHTDSS LLLADITDKF GQRAFVGKVC MDLNDTFPEY
KETTEESIKE TERFVSEMLQ KNYSRVKPIV TPRFSLSCSE TLMGELGNIA KTRDLHIQSH
ISENRDEVEA VKNLYPSYKN YTSVYDKNNL LTNKTVMAHG CYLSAEELNV FHERGASIAH
CPNSNLSLSS GFLNVLEVLK HEVKIGLGTD VAGGYSYSML DAIRRAVMVS NILLINKVNE
KSLTLKEVFR LATLGGSQAL GLDGEIGNFE VGKEFDAILI NPKASDSPID LFYGDFFGDI
SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSV
