ID   MAL1_DROME              Reviewed;         577 AA.
AC   P07190; Q9V4T6;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 2.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Maltase A1;
DE            EC=3.2.1.20;
DE   AltName: Full=Larval visceral protein H;
DE   Flags: Precursor;
GN   Name=Mal-A1; Synonyms=LvpH; ORFNames=CG8696;
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], AND DEVELOPMENTAL STAGE.
RX   PubMed=6854639; DOI=10.1016/s0022-2836(83)80001-1;
RA   Snyder M., Davidson N.;
RT   "Two gene families clustered in a small region of the Drosophila genome.";
RL   J. Mol. Biol. 166:101-118(1983).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
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).
RN   [5]
RP   SEQUENCE REVISION.
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC   -!- DEVELOPMENTAL STAGE: One of the proteins expressed by the 44D cuticle
CC       gene cluster. Expressed in first, second and early 3rd instar larvae
CC       and in adults, but not in embryos or pupae.
CC       {ECO:0000269|PubMed:6854639}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL48097.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; V00204; CAA23491.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE013599; AAF59089.3; -; Genomic_DNA.
DR   EMBL; AY070626; AAL48097.2; ALT_INIT; mRNA.
DR   PIR; S07253; S07253.
DR   RefSeq; NP_476627.3; NM_057279.5.
DR   AlphaFoldDB; P07190; -.
DR   SMR; P07190; -.
DR   BioGRID; 61676; 5.
DR   IntAct; P07190; 1.
DR   STRING; 7227.FBpp0087838; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GlyCosmos; P07190; 5 sites, No reported glycans.
DR   GlyGen; P07190; 5 sites.
DR   PaxDb; 7227-FBpp0087838; -.
DR   DNASU; 35824; -.
DR   EnsemblMetazoa; FBtr0088759; FBpp0087838; FBgn0002570.
DR   GeneID; 35824; -.
DR   KEGG; dme:Dmel_CG8696; -.
DR   AGR; FB:FBgn0002570; -.
DR   CTD; 35824; -.
DR   FlyBase; FBgn0002570; Mal-A1.
DR   VEuPathDB; VectorBase:FBgn0002570; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_8_3_1; -.
DR   InParanoid; P07190; -.
DR   OMA; FYQIHPE; -.
DR   OrthoDB; 3680211at2759; -.
DR   PhylomeDB; P07190; -.
DR   SignaLink; P07190; -.
DR   BioGRID-ORCS; 35824; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 35824; -.
DR   PRO; PR:P07190; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0002570; Expressed in adult midgut (Drosophila) and 15 other cell types or tissues.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; ISS:FlyBase.
DR   CDD; cd11328; AmyAc_maltase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF233; MALTASE A1; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   Genevisible; P07190; DM.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..577
FT                   /note="Maltase A1"
FT                   /id="PRO_0000001447"
FT   ACT_SITE        221
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        297
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            363
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   577 AA;  66386 MW;  E005AE05F98ABE0F CRC64;
     MRPQSAACLL LAIVGFVGAT EWWESGNYYQ IYPRSFRDSD GDGIGDLNGV TEKLQYLKDI
     GFTGTWLSPI FKSPMVDFGY DISDFYQIHP EYGTMEDFER MIAKAKEVGI KIILDFVPNH
     SSTENEWFTK SVDSDPVYKD FYIWHDGKIN NETGEREPPS NWNSEFRYSA WEWNEVRQQY
     YLHQFAIQQA DLNYRNPAVV NEMKNVIRFW LGKGVSGFRI DAVPYLFEVD LDRYNQYPDE
     PLTNDSVNCP DPDDHCYTQH IYTQDMPETI DMVYQWRELV DEFHVENGGD KRLLMTEAYT
     SFENIMTYYG NGVRNGSHIP FNFDFLTSIN NASKAGEYVE HIKKWMDAMP EGVYANWVLG
     NHDNKRVASR FGVQRTDLIN ILLQTLPGHA VTYNGEELGM TDVWISWEDT VDPNACNSDP
     DNYYARSRDP ARSPYQWDAS SKAGFTSADH TWLPVADDYK TNNALQQLRA PRSHLQIFKK
     LVRVRKEPSF RQGELNIQAI DDDVIIYSRQ KTGSDLYVIV LNLGSTSKTL DLTKYYELGT
     QAEVITTSLS SQYIDGDVIK STEFVANPYV GTVLVAV
//