ACHE_MAIZE
ID ACHE_MAIZE Reviewed; 396 AA.
AC B4FZ87; A0A3L6E326; Q5FC14;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=GDSL esterase/lipase ACHE {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:15980188};
DE AltName: Full=Acetylcholinesterase {ECO:0000303|PubMed:15980188};
DE Short=AChE {ECO:0000303|PubMed:15980188};
DE Flags: Precursor;
GN Name=ACHE {ECO:0000303|PubMed:15980188};
GN ORFNames=ZEAMMB73_Zm00001d021961 {ECO:0000312|EMBL:ONM59167.1},
GN Zm00014a_018493 {ECO:0000312|EMBL:PWZ15334.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-51, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15980188; DOI=10.1104/pp.105.062927;
RA Sagane Y., Nakagawa T., Yamamoto K., Michikawa S., Oguri S., Momonoki Y.S.;
RT "Molecular characterization of maize acetylcholinesterase: a novel enzyme
RT family in the plant kingdom.";
RL Plant Physiol. 138:1359-1371(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Missouri 17; TISSUE=Seedling;
RX PubMed=30061735; DOI=10.1038/s41588-018-0182-0;
RA Sun S., Zhou Y., Chen J., Shi J., Zhao H., Zhao H., Song W., Zhang M.,
RA Cui Y., Dong X., Liu H., Ma X., Jiao Y., Wang B., Wei X., Stein J.C.,
RA Glaubitz J.C., Lu F., Yu G., Liang C., Fengler K., Li B., Rafalski A.,
RA Schnable P.S., Ware D.H., Buckler E.S., Lai J.;
RT "Extensive intraspecific gene order and gene structural variations between
RT Mo17 and other maize genomes.";
RL Nat. Genet. 50:1289-1295(2018).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
CC -!- FUNCTION: Esterase that can hydrolyze acetylthiocholine and
CC propionylthiocholine in vitro (PubMed:15980188). Substrate preference
CC is propionylthiocholine > acetylthiocholine (PubMed:15980188).
CC Possesses extremely low activity against butyrylthiocholine
CC (PubMed:15980188). {ECO:0000269|PubMed:15980188}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.7 mM for acetylthiocholine {ECO:0000269|PubMed:15980188};
CC KM=3.1 mM for propionylthiocholine {ECO:0000269|PubMed:15980188};
CC Vmax=1.7 umol/min/mg enzyme with acetylthiocholine as substrate
CC {ECO:0000269|PubMed:15980188};
CC Vmax=1.7 umol/min/mg enzyme with propionylthiocholine as substrate
CC {ECO:0000269|PubMed:15980188};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AB093208; BAD89850.1; -; mRNA.
DR EMBL; CM007650; ONM59167.1; -; Genomic_DNA.
DR EMBL; NCVQ01000008; PWZ15334.1; -; Genomic_DNA.
DR EMBL; EU964721; ACG36839.1; -; mRNA.
DR EMBL; BT042425; ACF87430.1; -; mRNA.
DR RefSeq; NP_001105800.2; NM_001112330.2.
DR AlphaFoldDB; B4FZ87; -.
DR SMR; B4FZ87; -.
DR PRIDE; B4FZ87; -.
DR EnsemblPlants; Zm00001eb325910_T001; Zm00001eb325910_P001; Zm00001eb325910.
DR GeneID; 606473; -.
DR Gramene; Zm00001eb325910_T001; Zm00001eb325910_P001; Zm00001eb325910.
DR KEGG; zma:606473; -.
DR OMA; NRYIFER; -.
DR OrthoDB; 704138at2759; -.
DR Proteomes; UP000007305; Chromosome 7.
DR Proteomes; UP000251960; Chromosome 7.
DR ExpressionAtlas; B4FZ87; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006581; P:acetylcholine catabolic process; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd01837; SGNH_plant_lipase_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR035669; SGNH_plant_lipase-like.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Serine esterase; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:15980188"
FT CHAIN 32..396
FT /note="GDSL esterase/lipase ACHE"
FT /id="PRO_5011203678"
FT ACT_SITE 49
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0ADA1"
FT ACT_SITE 359
FT /evidence="ECO:0000250|UniProtKB:P0ADA1"
FT ACT_SITE 362
FT /evidence="ECO:0000250|UniProtKB:P0ADA1"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 26..31
FT /note="ALRPSD -> RASG (in Ref. 1; BAD89850)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="I -> T (in Ref. 1; BAD89850)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="A -> P (in Ref. 1; BAD89850)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="N -> K (in Ref. 1; BAD89850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 42680 MW; 0989645D434D6585 CRC64;
MATAATATAG SRAAVLLLLS LALALALRPS DAGAGGDCHF PAVFNFGDSN SDTGGLSSLF
GAAPPPNGRT FFGMPAGRYC DGRLVIDFIA ESLGLTHLSA YLNSIGSNFT QGANFATAGS
SIRRQNTSLF LSGFSPISLD VQFWEFEQFI NRSQLVYNNK GGIYREILPR AEYFSQALYT
FDIGQNDITS SYFVNNTTEE VEAIIPDLME RLTSIIQSVY SRGGRYFWIH NTGPLGCLPY
ALLHRPDLAI PADGTGCSVT YNKVAQLFNL RLKETVASLR KTHPDAAFTY VDVYTAKYKL
ISQANKLGFD DPLLTCCGYG GGRYNLDLSV GCGGKKQVNG TSVVVGKSCE NPSKRVSWDG
VHFTEAANKF VFDQIVAGAL SDPPVALRQA CHSRGQ
