AMYR_DROME
ID AMYR_DROME Reviewed; 493 AA.
AC O18408; Q9V7S3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Alpha-amylase-related protein;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE Flags: Precursor;
GN Name=Amyrel; ORFNames=CG8221;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=9618501; DOI=10.1073/pnas.95.12.6848;
RA Da Lage J.-L., Renard E., Chartois F., Lemeunier F., Cariou M.-L.;
RT "Amyrel, a paralogous gene of the amylase gene family in Drosophila
RT melanogaster and the Sophophora subgenus.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6848-6853(1998).
RN [2]
RP SEQUENCE REVISION AT 310.
RA Da Lage J.-L.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RA Da Lage J.-L.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P56634};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P56634};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Midgut and fat body.
CC -!- DEVELOPMENTAL STAGE: Expressed during second and third larval instars,
CC but not in the adult.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; U69607; AAD08845.1; -; Genomic_DNA.
DR EMBL; AF022713; AAD09147.2; -; Genomic_DNA.
DR EMBL; AE013599; AAF57971.1; -; Genomic_DNA.
DR EMBL; AY052055; AAK93479.1; -; mRNA.
DR RefSeq; NP_477262.1; NM_057914.4.
DR AlphaFoldDB; O18408; -.
DR SMR; O18408; -.
DR BioGRID; 62575; 5.
DR IntAct; O18408; 3.
DR STRING; 7227.FBpp0086263; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; O18408; -.
DR DNASU; 36863; -.
DR EnsemblMetazoa; FBtr0087117; FBpp0086263; FBgn0020506.
DR GeneID; 36863; -.
DR KEGG; dme:Dmel_CG8221; -.
DR UCSC; CG8221-RA; d. melanogaster.
DR CTD; 36863; -.
DR FlyBase; FBgn0020506; Amyrel.
DR VEuPathDB; VectorBase:FBgn0020506; -.
DR eggNOG; KOG2212; Eukaryota.
DR GeneTree; ENSGT00940000167534; -.
DR HOGENOM; CLU_013336_2_1_1; -.
DR InParanoid; O18408; -.
DR OMA; QSWGTDW; -.
DR OrthoDB; 665362at2759; -.
DR PhylomeDB; O18408; -.
DR Reactome; R-DME-189085; Digestion of dietary carbohydrate.
DR SignaLink; O18408; -.
DR BioGRID-ORCS; 36863; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36863; -.
DR PRO; PR:O18408; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0020506; Expressed in midgut and 7 other tissues.
DR ExpressionAtlas; O18408; differential.
DR Genevisible; O18408; DM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IDA:FlyBase.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:FlyBase.
DR GO; GO:0016160; F:amylase activity; ISS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Calcium; Carbohydrate metabolism; Chloride; Disulfide bond; Glycosidase;
KW Hydrolase; Metal-binding; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..493
FT /note="Alpha-amylase-related protein"
FT /id="PRO_0000001382"
FT ACT_SITE 207
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 205
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 307
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 342
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 309
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 47..103
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 156..170
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 375..381
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 417..440
FT /evidence="ECO:0000255"
FT DISULFID 447..459
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT CONFLICT 2
FT /note="F -> S (in Ref. 2; AAD08845 and 3; AAD09147)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="T -> A (in Ref. 2; AAD08845)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="L -> V (in Ref. 2; AAD08845 and 3; AAD09147)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="L -> I (in Ref. 2; AAD08845 and 3; AAD09147)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="A -> V (in Ref. 2; AAD08845 and 3; AAD09147)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="E -> V (in Ref. 2; AAD08845 and 3; AAD09147)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="V -> D (in Ref. 2; AAD08845)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="I -> T (in Ref. 2; AAD08845)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="Q -> R (in Ref. 2; AAD08845)"
FT /evidence="ECO:0000305"
FT CONFLICT 466..467
FT /note="VN -> MS (in Ref. 2; AAD08845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 55451 MW; 3223298DAF7E634C CRC64;
MFKFALTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ
VSPVNENILS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS
GDFDGVAVGT AGTEAEPSKK SFPGVPYTAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ
SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF
IFQEVIDHGH ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TDWGFLPSGQ
ALTFVDNHDN QRDAGAVLNY KSPRQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA
QERIISPEFD ADGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQISFCRGN
KGFLAINNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTVNENG YGYIHIGSDD
FDGVLALHVD AKV
