O96838 (FYV1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative 1-phosphatidylinositol-3-phosphate 5-kinase
Short name=Phosphatidylinositol-3-phosphate 5-kinase
EC=2.7.1.150

Alternative name(s):
Type III PIP kinase
Short name=PIPkin-III

Gene names

Name:	fab1
ORF Names:	CG6355

Organism

Drosophila melanogaster (Fruit fly)

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	1809 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol-3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol-3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. Has a role at a late stage in endosome-related membrane trafficking, at a point when signal termination has occurred. Is not required for receptor silencing. Ref.5
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.
Cofactor	Zinc By similarity.
Subcellular location	Endosome membrane. Note: Mainly associated with membranes of the late endocytic pathway. Ref.5
Disruption phenotype	Flies contain undetectable phosphatidylinositol 3,5-bisphosphate levels, show profound increases in cell and organ size, and die at the pupal stage. Mutant larvae contain highly enlarged multivesicular bodies and late endosomes that are inefficiently acidified. Even though endocytic receptor trafficking is impaired in fab1 mutants, Notch, Wingless, and Dpp signaling is unaffected. Ref.5
Sequence similarities	Contains 1 DEP domain. Contains 1 FYVE-type zinc finger. Contains 1 PIPK domain.
Sequence caution	The sequence AAL25475.1 differs from that shown. Reason: Erroneous initiation. The sequence AAL39881.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA22949.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Endosome Membrane
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular protein metabolic process Inferred from electronic annotation. Source: InterPro endosome to lysosome transport Inferred from mutant phenotype Ref.5. Source: FlyBase intracellular signal transduction Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell vesicle membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	1-phosphatidylinositol-3-phosphate 5-kinase activity Inferred from mutant phenotype Ref.5. Source: FlyBase 1-phosphatidylinositol-4-phosphate 5-kinase activity Inferred from sequence or structural similarity. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1809	1809	Putative 1-phosphatidylinositol-3-phosphate 5-kinase		PRO_0000185454
Regions
	Domain	323 – 399	77	DEP
	Domain	1473 – 1796	324	PIPK
	Zinc finger	186 – 246	61	FYVE-type
	Region	1552 – 1809	258	Catalytic
Amino acid modifications
	Modified residue	755	1	Phosphoserine Ref.6
	Modified residue	760	1	Phosphothreonine Ref.6
	Modified residue	1530	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	1403	1	A → ASSASA in CAA22949. Ref.3
	Sequence conflict	1420	1	V → I in CAA22949. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O96838 [UniParc]. Last modified May 10, 2004. Version 2. Checksum: B5A111FAD317B05F	FASTA	1,809	204,635
	10 20 30 40 50 60 MTSNNQNNSS SHQHLHSPSK LTEFARNFED KPESLFGRVV NKIQNVYNQS YNTVNDISSG 70 80 90 100 110 120 SSSSSSTQPV QVVGKSQFFS DSQTSTAEIA DVETSSQSSV RPQPPTTLSI RTNSETRGTS 130 140 150 160 170 180 TSSNTAAEDS ETSDRVETLP LPTSEANQGR TVSNVLKHIS NIVATKNNND LRNYKDTELQ 190 200 210 220 230 240 RFWMPDSKAK ECYDCSQKFS TFRRKHHCRL CGQIFCSKCC NQVVPGMIIR CDGDLKVCNY 250 260 270 280 290 300 CSKIVLTFLK SSSSEMGQDM QELQQHLSNK LEVQDSGSSL AKHPQMQRAP LPRKTSVGYQ 310 320 330 340 350 360 EERFSSHPTY TTLSIDDRKN ILQQSNSLIT LHEEMQRDLP AQNCGQRLIE FLNSNNKSAN 370 380 390 400 410 420 EVQAVAILNA MLAAGFLEPI VPDPEQMDFD SSLHYKFSKS SSSDTSRTMS PQFEANPHAE 430 440 450 460 470 480 PQPPKSMDQS AEEKEKELEN ELENDRCYTT ATSKLLASYC EHEEQLLAQM LRAHNLDQEW 490 500 510 520 530 540 DKVLQMLCST AANHFKPEHC SNDLMDIRNY VNFKKVPGGR RKDSKIVHGV AFSKNVAHKD 550 560 570 580 590 600 MATHVPFPRI LLLQCPIVYE RIEGKFVTIE TVLLQEKEYL RNVCARIMSF KPNVVLVHKN 610 620 630 640 650 660 VAGIAQDLLR SYEVTLVLDV KLSVMERLSR TLQCDIVSSI ESNITMPKLG YCNDFYIRNY 670 680 690 700 710 720 NGKTLMFFEK LTNPRGYTCL LRGGSNAELT RVKRVASALL FARYNWRLEM SFLLNEFAQP 730 740 750 760 770 780 LSPKPSIFDS KETSPKTETE AELRSKRPII LERKSEDKIT TIVSENVSDF TDPLRASQAE 790 800 810 820 830 840 ALSTSPCAPP VVEALAVEPR YDNRFRTALS STLLSVSPFL TFPLPYLETE QGRKCKLRKL 850 860 870 880 890 900 FPAELYFSKQ WSRTGLERPD SMGDGEAGKS EPGNKENQMQ LLPAHDFVLM KITAPASSRD 910 920 930 940 950 960 IQSKLAEFRS FGGRLPKGKA PMLRPKKKNA EVIQRPQKVS EEQLYKDALD PQNHQRLPVL 970 980 990 1000 1010 1020 FCSFHYNPKG VSSFCKLPML LDMKFYGQYD IMLEQFLQRY CCLFNSMCPS CNLPMLGHVR 1030 1040 1050 1060 1070 1080 RYVHSLGCVH VYLTEDLTRS DPTRIYFTSW CSICNATTPT IPLSDAAKCL SLAKYLEMRF 1090 1100 1110 1120 1130 1140 HGHAYKRRPP STDAEQGGTV CEHSLHRDYV HHFSFRGVGA KFQYTPVEVW ETDLPSLTVQ 1150 1160 1170 1180 1190 1200 LDLPQPFQSA QVQEEIKNFS IKGHEVYNRI HERIADLATE EENSPLVQHL KTMLTHDQFI 1210 1220 1230 1240 1250 1260 FKQKIEIVHT LLTDNRATAY DTSDALAMAR RALAESIELW GPRLQEIEKL TAKQAHHIDS 1270 1280 1290 1300 1310 1320 GTICTEELRP EQVQTADSSK VTTSSLPKEN DPLECPSEDT ETGASNSQTV LDKNFSIDQM 1330 1340 1350 1360 1370 1380 LASTVNVYSD KKSIRKILTQ LLPSGNQVNP LQSPFPAQDH LTLPLGSIPI HVRETDLSSV 1390 1400 1410 1420 1430 1440 IAYSLTSMDY QKAIDEAEAN SNAAHSSPQL KRKIPLAESV SDAEDSPSLS RTSSNTSAAP 1450 1460 1470 1480 1490 1500 NASVPSPATA ASESEEKSKE RIKQPPSPHI TLAFQDHSCQ FQCKIYFARE FDAMRSKSLK 1510 1520 1530 1540 1550 1560 PPKLDKSLYR RLEKSKMREE LRISQSRTGS EMELVRKPSD VGAPRTTEDD SNQEEDARIA 1570 1580 1590 1600 1610 1620 LARSLCKSVQ WEARGGKSGS RFCKTLDDRF VLKEMNSRDM TIFEPFAPKY FEYIDRCQQQ 1630 1640 1650 1660 1670 1680 QQPTLLAKIF GVFRVSVKKK DSFVERSVMV MENLFYGCNI ENKFDLKGSE RNRLVDPSNQ 1690 1700 1710 1720 1730 1740 QGEIVLLDEN LVQMSWSKPL YVLSHSKTVL RDAIQRDSSF LEKNLVMDYS LLVGLDKKNG 1750 1760 1770 1780 1790 1800 VLVLGIIDYI RTFTLDKRVE SIIKGSGILG GKGKDPTVVN PERYKQRFID AMDRYFLTVP DRWEGLSKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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. Strain: Berkeley.
[3]	"From sequence to chromosome: the tip of the X chromosome of D. melanogaster." Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M. Science 287:2220-2222(2000) [PubMed: 10731137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Oregon-R.
[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] OF 979-1809. Strain: Berkeley. Tissue: Embryo, Larva and Pupae.
[5]	"Fab1 phosphatidylinositol 3-phosphate 5-kinase controls trafficking but not silencing of endocytosed receptors." Rusten T.E., Rodahl L.M.W., Pattni K., Englund C., Samakovlis C., Dove S., Brech A., Stenmark H. Mol. Biol. Cell 17:3989-4001(2006) [PubMed: 16837550] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[6]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755; THR-760 AND SER-1530, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013599 Genomic DNA. Translation: AAF57789.1. AE013599 Genomic DNA. Translation: AAS64818.1. AL035311 Genomic DNA. Translation: CAA22949.1. Sequence problems. AY060436 mRNA. Translation: AAL25475.1. Different initiation. AY069736 mRNA. Translation: AAL39881.1. Different initiation.
PIR	T13576.
RefSeq	NP_611269.1. NM_137425.3. NP_995880.1. NM_206158.1.
UniGene	Dm.7091.
3D structure databases
ProteinModelPortal	O96838.
SMR	O96838. Positions 180-247, 475-719, 1526-1796.
ModBase	Search...
Protein-protein interaction databases
STRING	O96838.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0089554; FBpp0088523; FBgn0028741. FBtr0089555; FBpp0088952; FBgn0028741.
GeneID	37033.
KEGG	dme:Dmel_CG6355.
Organism-specific databases
CTD	37033.
FlyBase	FBgn0028741. fab1.
Phylogenomic databases
eggNOG	inNOG06375.
GeneTree	EMGT00050000006689.
InParanoid	O96838.
OMA	GHATSGH.
OrthoDB	EOG4WM38G.
PhylomeDB	O96838.
Gene expression databases
GermOnline	CG6355. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002423. Cpn60/TCP-1. IPR000591. DEP_dom. IPR002498. PInositol-4-P-5-kinase_core. IPR016034. PInositol-4P-5-kinase_core_sub. IPR011991. WHTH_trsnscrt_rep_DNA-bd. IPR000306. Znf_FYVE. IPR017455. Znf_FYVE-rel. IPR011011. Znf_FYVE_PHD. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit. G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
KO	K00921.
PANTHER	PTHR11353. Cpn60/TCP-1. 1 hit.
Pfam	PF00118. Cpn60_TCP1. 1 hit. PF01363. FYVE. 1 hit. PF01504. PIP5K. 1 hit. [Graphical view]
SMART	SM00049. DEP. 1 hit. SM00064. FYVE. 1 hit. SM00330. PIPKc. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS50186. DEP. 1 hit. PS51455. PIPK. 1 hit. PS50178. ZF_FYVE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	801599.

Entry information

Entry name

FYV1_DROME

Accession

Primary (citable) accession number: O96838
Secondary accession number(s): A4UZM3 , Q8SZX0, Q95SX9, Q9V886

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 10, 2004
Last modified:	January 25, 2012
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project