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O18408 (AMYR_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-amylase-related protein
EC=3.2.1.1
Gene names
Name:Amyrel
ORF Names:CG8221
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Binds 1 chloride ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Secreted Probable.

Tissue specificity

Midgut and fat body.

Developmental stage

Expressed during second and third larval instars, but not in the adult.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Chloride
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 493474Alpha-amylase-related protein
PRO_0000001382

Sites

Active site2071Nucleophile By similarity
Active site2441Proton donor By similarity
Metal binding1171Calcium By similarity
Metal binding1681Calcium; via carbonyl oxygen By similarity
Metal binding1771Calcium By similarity
Metal binding2111Calcium; via carbonyl oxygen By similarity
Binding site2051Chloride By similarity
Binding site3071Chloride By similarity
Binding site3421Chloride By similarity
Site3091Transition state stabilizer By similarity

Amino acid modifications

Modified residue201Pyrrolidone carboxylic acid By similarity
Disulfide bond47 ↔ 103 By similarity
Disulfide bond156 ↔ 170 By similarity
Disulfide bond375 ↔ 381 By similarity
Disulfide bond417 ↔ 440 Potential
Disulfide bond447 ↔ 459 By similarity

Experimental info

Sequence conflict21F → S in AAD08845. Ref.2
Sequence conflict21F → S in AAD09147. Ref.3
Sequence conflict71T → A in AAD08845. Ref.2
Sequence conflict181L → V in AAD08845. Ref.2
Sequence conflict181L → V in AAD09147. Ref.3
Sequence conflict691L → I in AAD08845. Ref.2
Sequence conflict691L → I in AAD09147. Ref.3
Sequence conflict1271A → V in AAD08845. Ref.2
Sequence conflict1271A → V in AAD09147. Ref.3
Sequence conflict1571E → V in AAD08845. Ref.2
Sequence conflict1571E → V in AAD09147. Ref.3
Sequence conflict2531V → D in AAD08845. Ref.2
Sequence conflict3401I → T in AAD08845. Ref.2
Sequence conflict3581Q → R in AAD08845. Ref.2
Sequence conflict466 – 4672VN → MS in AAD08845. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O18408 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 3223298DAF7E634C

FASTA49355,451
        10         20         30         40         50         60 
MFKFALTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ 

        70         80         90        100        110        120 
VSPVNENILS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS 

       130        140        150        160        170        180 
GDFDGVAVGT AGTEAEPSKK SFPGVPYTAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ 

       190        200        210        220        230        240 
SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF 

       250        260        270        280        290        300 
IFQEVIDHGH ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TDWGFLPSGQ 

       310        320        330        340        350        360 
ALTFVDNHDN QRDAGAVLNY KSPRQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA 

       370        380        390        400        410        420 
QERIISPEFD ADGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQISFCRGN 

       430        440        450        460        470        480 
KGFLAINNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTVNENG YGYIHIGSDD 

       490 
FDGVLALHVD AKV

« Hide

References

« Hide 'large scale' references
[1]"Amyrel, a paralogous gene of the amylase gene family in Drosophila melanogaster and the Sophophora subgenus."
Da Lage J.-L., Renard E., Chartois F., Lemeunier F., Cariou M.-L.
Proc. Natl. Acad. Sci. U.S.A. 95:6848-6853(1998) [PubMed: 9618501] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Canton-S.
[2]Da Lage J.-L.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION AT 310.
[3]Da Lage J.-L.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Canton-S.
[4]"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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[5]"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. expand/collapse author list , 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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[6]"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: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Larva and Pupae.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U69607 Genomic DNA. Translation: AAD08845.1.
AF022713 Genomic DNA. Translation: AAD09147.2.
AE013599 Genomic DNA. Translation: AAF57971.1.
AY052055 mRNA. Translation: AAK93479.1.
RefSeqNP_477262.1. NM_057914.3.
UniGeneDm.4395.

3D structure databases

ProteinModelPortalO18408.
SMRO18408. Positions 20-493.
ModBaseSearch...

Protein-protein interaction databases

STRINGO18408.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0087117; FBpp0086263; FBgn0020506.
GeneID36863.
KEGGdme:Dmel_CG8221.
UCSCCG8221-RA. d. melanogaster.

Organism-specific databases

CTD36863.
FlyBaseFBgn0020506. Amyrel.

Phylogenomic databases

eggNOGinNOG06322.
InParanoidO18408.
OMAGNRNTIV.
OrthoDBEOG4XD26M.
PhylomeDBO18408.

Gene expression databases

BgeeO18408.
GermOnlineCG8221. Drosophila melanogaster.

Family and domain databases

InterProIPR006048. A-amylase_b_C.
IPR015902. Alpha_amylase.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KOK01176.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Other

NextBio800776.

Entry information

Entry nameAMYR_DROME
AccessionPrimary (citable) accession number: O18408
Secondary accession number(s): Q9V7S3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 11, 2011
Last modified: January 25, 2012
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents