P07191 (MAL1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable maltase D
EC=3.2.1.20

Alternative name(s):
Larval visceral protein D

Gene names

Name:	LvpD
ORF Names:	CG8694

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	567 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
Developmental stage	One of the proteins expressed by the 44D cuticle gene cluster. Expressed in first, second and early 3rd instar larvae and in adults, but not in embryos or pupae.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.
Sequence caution	The sequence CAA23492.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	cation binding Inferred from electronic annotation. Source: InterPro maltose alpha-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 567	544	Probable maltase D		PRO_0000001446
Sites
	Active site	226	1	Nucleophile By similarity
	Active site	298	1	Proton donor By similarity
	Site	364	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	30	1	N-linked (GlcNAc...) Potential
	Glycosylation	124	1	N-linked (GlcNAc...) Potential
	Glycosylation	198	1	N-linked (GlcNAc...) Potential
	Glycosylation	312	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	527	1	P → T in CAA23492. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P07191 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: 51242BA9F185213D	FASTA	567	64,542
	10 20 30 40 50 60 MPKWAHLGLA ALLLISTTQE GTADIDWWEN ASLYQIYPRS FQDSDGDGIG DLKGITSRLG 70 80 90 100 110 120 YLKEIGITAT WLSPIFTSPM SDFGYDISNF YDIDPIFGTL EDFDDLIVEA KSLGVKIILD 130 140 150 160 170 180 FVPNHSSDEN VWFEKSVNRE DGYDDFYVWD DGKLNEETGA RDPPSNWVSV FSGPMWTWNE 190 200 210 220 230 240 KRQQYFLHQF QVKQPDLNFT NPMVREHMLD VLKFWLDRGV DGFRIDAVPH IYEHRNADGS 250 260 270 280 290 300 YPDEPVSGWG SDPNAYDYHD HIYTKDQPAT VDLMYEWREF LDNYRAQNGG DSRVLLAEAY 310 320 330 340 350 360 SSVETLSAYF GNSTHQGTQL PMNFQLMYLS GYSTAKDVVG SIDYWMNTMW KEHQTANWVV 370 380 390 400 410 420 GNHDTNRVAD RMGAHKVDLL NVIVNALPGA SVTYYGEEIG MSNVDVECTG DSCEDRDGER 430 440 450 460 470 480 TPMQWTAGKN ADFSDGESTW LPLSPEYQRY NVQTERGVSR SSLNIFKGLQ ELKSSSAFLA 490 500 510 520 530 540 FKEDGGFSYE AVTEQVLQII RTNKISEEYR ILVNMGNGME ILDGLAPKTY EYVLATAYST 550 560 HYSGQKADLS QRIILMPYEA VVLRWLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two gene families clustered in a small region of the Drosophila genome." Snyder M., Davidson N. J. Mol. Biol. 166:101-118(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Detection of protein similarities using nucleotide sequence databases." Henikoff S., Wallace J.C. Nucleic Acids Res. 16:6191-6204(1988) [PubMed] [Europe PMC] [Abstract] Cited for: POSSIBLE FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	V00204 Genomic DNA. Translation: CAA23492.1. Sequence problems. AE013599 Genomic DNA. Translation: AAF59088.1. AY071566 mRNA. Translation: AAL49188.1.
PIR	S08597.
RefSeq	NP_476625.2. NM_057277.2.
UniGene	Dm.5267.
3D structure databases
ProteinModelPortal	P07191.
SMR	P07191. Positions 22-566.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-851985.
STRING	7227.FBpp0087826.
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Proteomic databases
PaxDb	P07191.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0088747; FBpp0087826; FBgn0002569.
GeneID	35825.
KEGG	dme:Dmel_CG8694.
Organism-specific databases
CTD	35825.
FlyBase	FBgn0002569. LvpD.
Phylogenomic databases
eggNOG	COG0366.
GeneTree	ENSGT00530000063127.
InParanoid	P07191.
KO	K01187.
OMA	SVTYYGE.
OrthoDB	EOG4GXD2V.
PhylomeDB	P07191.
Gene expression databases
Bgee	P07191.
GermOnline	CG8694. Drosophila melanogaster.
Family and domain databases
Gene3D	3.20.20.80. 2 hits.
InterPro	IPR015902. Glyco_hydro_13. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
PANTHER	PTHR10357. PTHR10357. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. [Graphical view]
SMART	SM00642. Aamy. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	35825.
NextBio	795392.

Entry information

Entry name

MAL1_DROME

Accession

Primary (citable) accession number: P07191
Secondary accession number(s): Q9V4T7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	July 5, 2005
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project