Reviewed, UniProtKB/Swiss-Prot Q24238 (APH4_DROME)

Names and origin

Protein names

Recommended name:
    Alkaline phosphatase 4
    EC=3.1.3.1

Gene names

Name:	Aph-4
ORF Names:	CG1462

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	596 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)

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-anchor › GPI-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.
Sequence caution	The sequence CAA67052.1 differs from that shown. Reason: Frameshift at position 538.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane
Ligand	Magnesium Metal-binding Zinc
Molecular function	Hydrolase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	epithelial fluid transport Ref.1 Inferred from mutant phenotype. Source: UniProtKB metabolic process Inferred from electronic annotation. Source: InterPro nervous system development Ref.1 Inferred from expression pattern. Source: UniProtKB
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alkaline phosphatase activity Non-traceable author statement. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 570	550	Alkaline phosphatase 4		PRO_0000024049
	Propeptide	571 – 596	26	Removed in mature form		PRO_0000024050
Regions
	Transmembrane	571 – 591	21	Potential
Sites
	Active site	144	1	Phosphoserine intermediate By similarity UniProtKB P05187
	Metal binding	93	1	Magnesium By similarity
	Metal binding	93	1	Zinc 2 By similarity
	Metal binding	202	1	Magnesium By similarity
	Metal binding	204	1	Magnesium By similarity
	Metal binding	369	1	Magnesium By similarity
	Metal binding	374	1	Zinc 1 By similarity
	Metal binding	378	1	Zinc 1 By similarity
	Metal binding	415	1	Zinc 2 By similarity
	Metal binding	416	1	Zinc 2 By similarity
	Metal binding	504	1	Zinc 1 By similarity
Amino acid modifications
	Lipidation	570	1	GPI-anchor amidated asparagine Potential
	Glycosylation	262	1	N-linked (GlcNAc...) Potential
	Glycosylation	297	1	N-linked (GlcNAc...) Potential
	Glycosylation	401	1	N-linked (GlcNAc...) Potential
	Glycosylation	464	1	N-linked (GlcNAc...) Potential
	Glycosylation	470	1	N-linked (GlcNAc...) Potential
	Disulfide bond	539 ↔ 550		By similarity UniProtKB P05187
Natural variations
	Alternative sequence	1 – 94	94	Missing in isoform B. Ref.2		VSP_007002
Experimental info
	Sequence conflict	200	1	I → N in AAL68351. Ref.4
	Sequence conflict	280	1	T → S in ABA81845. Ref.5
	Sequence conflict	358	1	G → D in CAA67052. Ref.1
	Sequence conflict	375	1	Q → H in CAA67052. Ref.1
	Sequence conflict	495 – 496	2	AT → EP in CAA67052. Ref.1
	Sequence conflict	570	1	N → S in CAA67052. Ref.1
	Sequence conflict	573	1	T → S in CAA67052. Ref.1
	Sequence conflict	593 – 594	2	GR → CH in CAA67052. Ref.1
	Sequence conflict	593 – 594	2	GR → CH in ABA81845. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified March 28, 2003. Version 3. Checksum: 333F3345BEFBAEFB	FASTA	596	65,262
	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
	Isoform B. Checksum: A9E70E72FDAC8AAF	FASTA	502	54,887
	10 20 30 40 50 60 MGISTISAGR IYKGQYLKHG YGEEETLVFD DFPNTGMAKT YNVDKQVPDS AGTATAIFSG 70 80 90 100 110 120 SKTHYGAIGM DATRSKKNGQ QGRVQSVMEW AQKEGKRTGV VTTTRITHAT PAATYAHIYD 130 140 150 160 170 180 RDWECDTEVP AESVGFHVDI ARQLVENAPG NRFNVILGGG MSPMGILNAS EVKTTIFEGP 190 200 210 220 230 240 TETICTRGDN RNLPAEWLAH HANDTVPPAL VHNRKDLLNV NVKKVDHLMG LFRNNHITYS 250 260 270 280 290 300 IAREAGEPSL QEMTETALGI LERGDESNGF VLLVEGGRID QGHHMNYARA ALHELYEFDL 310 320 330 340 350 360 AIQAAVNNTD PDETLILVTA DHSHAVTFNG YALRGADILG TANSHEKNDP MFYETISYAN 370 380 390 400 410 420 GPGYWDHLAN DSRPQNSSNM WMPLKHFTAE ERAAPTYRHL ATVPRKDETH GGEDVAVFAY 430 440 450 460 470 480 GPGSSLIRGV FEQNYLAYVM SYAGCLGPAK DFDDSCEDHK DGQKDRPLDK PNPKRNGATV 490 500 VGASLIPILT AATAAILRGR GL

References

	« Hide 'large scale' referencesShow '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: 10628988] [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. , 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.
[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: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[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: 12537569] [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.
RefSeq	NP_524601.2. NP_733413.1.
UniGene	Dm.5439
3D structure databases
SMR	Q24238. Positions 48-547.
ModBase	Search...
Protein-protein interaction databases
STRING	Q24238.
Genome annotation databases
Ensembl	FBtr0085733; FBpp0085095; FBgn0016123; Drosophila melanogaster. [Genome view] FBtr0085734; FBpp0085096; FBgn0016123; Drosophila melanogaster. [Genome view]
GeneID	43671.
KEGG	dme:Dmel_CG1462.
Organism-specific databases
CTD	43671.
FlyBase	FBgn0016123. Aph-4.
Phylogenomic databases
eggNOG	inNOG05826.
InParanoid	Q24238.
OMA	ETISYAN.
OrthoDB	EOG91C72W.
PhylomeDB	Q24238.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-014263-MONOMER.
BRENDA	3.1.3.1. 48.
Gene expression databases
GermOnline	CG1462. Drosophila melanogaster.
Family and domain databases
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR001952. Alkaline_phosphatase. IPR018299. Alkaline_phosphatase_AS. IPR017850. Alkaline_phosphatase_core. [Graphical view]
Gene3D	G3DSA:3.40.720.10. Alk_phosphtse. 1 hit.
Pfam	PF00245. Alk_phosphatase. 1 hit. [Graphical view]
PRINTS	PR00113. ALKPHPHTASE.
SMART	SM00098. alkPPc. 1 hit. [Graphical view]
PROSITE	PS00123. ALKALINE_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	835185.

Entry information

Entry name

APH4_DROME

Accession

Primary (citable) accession number: Q24238
Secondary accession number(s): B9EQR2 , Q3KN28, Q8IMH0, Q8SXW6, Q9VA19

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	March 28, 2003
Last modified:	January 19, 2010
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project