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Q24238 (APH4_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alkaline phosphatase 4

EC=3.1.3.1
Gene names
Name:Aph-4
ORF Names:CG1462
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length596 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Important role in neural and renal epithelial function. Ref.1

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactor

Binds 1 magnesium ion By similarity.

Binds 2 zinc ions By similarity.

Subunit structure

Homodimer By similarity. UniProtKB P05187

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor By similarity.

Tissue specificity

Ellipsoid body ring neurons in the adult brain and in the lower Malpighian tubule and ureter. Ref.1

Developmental stage

Highest abundance during larval stage (prior to the secretion of pupal cuticle) and adult stage. Ref.1

Sequence similarities

Belongs to the alkaline phosphatase family. UniProtKB P05187

Sequence caution

The sequence CAA67052.1 differs from that shown. Reason: Frameshift at position 538.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A Ref.2 (identifier: Q24238-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B Ref.2 (identifier: Q24238-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 570550Alkaline phosphatase 4
PRO_0000024049
Propeptide571 – 59626Removed in mature form
PRO_0000024050

Regions

Transmembrane571 – 59121Helical; Potential

Sites

Active site1441Phosphoserine intermediate By similarity UniProtKB P05187
Metal binding931Magnesium By similarity
Metal binding931Zinc 2 By similarity
Metal binding2021Magnesium By similarity
Metal binding2041Magnesium By similarity
Metal binding3691Magnesium By similarity
Metal binding3741Zinc 1 By similarity
Metal binding3781Zinc 1 By similarity
Metal binding4151Zinc 2 By similarity
Metal binding4161Zinc 2 By similarity
Metal binding5041Zinc 1 By similarity

Amino acid modifications

Lipidation5701GPI-anchor amidated asparagine Potential
Glycosylation2621N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Glycosylation4641N-linked (GlcNAc...) Potential
Glycosylation4701N-linked (GlcNAc...) Potential
Disulfide bond539 ↔ 550 By similarity UniProtKB P05187

Natural variations

Alternative sequence1 – 9494Missing in isoform B. Ref.2
VSP_007002

Experimental info

Sequence conflict2001I → N in AAL68351. Ref.4
Sequence conflict2801T → S in ABA81845. Ref.5
Sequence conflict3581G → D in CAA67052. Ref.1
Sequence conflict3751Q → H in CAA67052. Ref.1
Sequence conflict495 – 4962AT → EP in CAA67052. Ref.1
Sequence conflict5701N → S in CAA67052. Ref.1
Sequence conflict5731T → S in CAA67052. Ref.1
Sequence conflict593 – 5942GR → CH in CAA67052. Ref.1
Sequence conflict593 – 5942GR → CH in ABA81845. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified March 28, 2003. Version 3.
Checksum: 333F3345BEFBAEFB

FASTA59665,262
        10         20         30         40         50         60 
MHCLVILGFL LGSLVAFSWA GVTTQPPPLI RTLSAGGDIG PQFDVGKTKE PEDAEFWHNV 

        70         80         90        100        110        120 
GLRQLEKTIK QAQRVKEDSY QKKARNIIIF IGDGMGISTI SAGRIYKGQY LKHGYGEEET 

       130        140        150        160        170        180 
LVFDDFPNTG MAKTYNVDKQ VPDSAGTATA IFSGSKTHYG AIGMDATRSK KNGQQGRVQS 

       190        200        210        220        230        240 
VMEWAQKEGK RTGVVTTTRI THATPAATYA HIYDRDWECD TEVPAESVGF HVDIARQLVE 

       250        260        270        280        290        300 
NAPGNRFNVI LGGGMSPMGI LNASEVKTTI FEGPTETICT RGDNRNLPAE WLAHHANDTV 

       310        320        330        340        350        360 
PPALVHNRKD LLNVNVKKVD HLMGLFRNNH ITYSIAREAG EPSLQEMTET ALGILERGDE 

       370        380        390        400        410        420 
SNGFVLLVEG GRIDQGHHMN YARAALHELY EFDLAIQAAV NNTDPDETLI LVTADHSHAV 

       430        440        450        460        470        480 
TFNGYALRGA DILGTANSHE KNDPMFYETI SYANGPGYWD HLANDSRPQN SSNMWMPLKH 

       490        500        510        520        530        540 
FTAEERAAPT YRHLATVPRK DETHGGEDVA VFAYGPGSSL IRGVFEQNYL AYVMSYAGCL 

       550        560        570        580        590 
GPAKDFDDSC EDHKDGQKDR PLDKPNPKRN GATVVGASLI PILTAATAAI LRGRGL 

« Hide

Isoform B [UniParc].

Checksum: A9E70E72FDAC8AAF
Show »

FASTA50254,887

References

« Hide 'large scale' references
[1]"A novel Drosophila alkaline phosphatase specific to the ellipsoid body of the adult brain and the lower Malpighian (renal) tubule."
Yang M.Y., Wang Z., MacPherson M., Dow J.A.T., Kaiser K.
Genetics 154:285-297(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Head.
[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. 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] [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. 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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
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] (ISOFORM A).
Strain: Berkeley.
Tissue: Head.
[5]Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
Strain: Berkeley.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98402 mRNA. Translation: CAA67052.1. Frameshift.
AE014297 Genomic DNA. Translation: AAF57106.1.
AE014297 Genomic DNA. Translation: AAN14265.1.
AY075544 mRNA. Translation: AAL68351.1.
BT023911 mRNA. Translation: ABA81845.1.
BT057987 mRNA. Translation: ACM16697.1.
RefSeqNP_524601.2. NM_079862.3.
NP_733413.1. NM_170534.2.
UniGeneDm.5439.

3D structure databases

ProteinModelPortalQ24238.
SMRQ24238. Positions 50-545.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ24238.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085733; FBpp0085095; FBgn0016123. [Q24238-1]
GeneID43671.
KEGGdme:Dmel_CG1462.

Organism-specific databases

CTD43671.
FlyBaseFBgn0016123. Aph-4.

Phylogenomic databases

eggNOGCOG1785.
GeneTreeENSGT00390000008704.
HOGENOMHOG000028185.
InParanoidQ24238.
KOK01077.
OMARNNHITY.
OrthoDBEOG7SN8CH.
PhylomeDBQ24238.

Gene expression databases

BgeeQ24238.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
PfamPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00113. ALKPHPHTASE.
SMARTSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi43671.
NextBio835185.

Entry information

Entry nameAPH4_DROME
AccessionPrimary (citable) accession number: Q24238
Secondary accession number(s): B9EQR2 expand/collapse secondary AC list , Q3KN28, Q8IMH0, Q8SXW6, Q9VA19
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: April 16, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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