FYV1_DICDI
ID FYV1_DICDI Reviewed; 2656 AA.
AC B0G126;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=1-phosphatidylinositol 3-phosphate 5-kinase;
DE Short=Phosphatidylinositol 3-phosphate 5-kinase;
DE EC=2.7.1.150;
DE AltName: Full=FYVE finger-containing phosphoinositide kinase;
DE AltName: Full=PIKfyve;
DE AltName: Full=Phosphatidylinositol 3-phosphate 5-kinase type III;
DE Short=PIPkin-III;
DE Short=Type III PIP kinase;
DE AltName: Full=Serine-protein kinase PIKFYVE;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9Y2I7};
GN Name=pip5k3; ORFNames=DDB_G0279149;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Dual specificity kinase part of the PI(3,5)P2 regulatory
CC complex which regulates both the synthesis and turnover of
CC phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the
CC phosphorylation of phosphatidylinositol 3-phosphate on the fifth
CC hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-
CC bisphosphate. {ECO:0000250|UniProtKB:Q9Y2I7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:13609,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57923,
CC ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.150;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2I7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13610;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2I7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:44680, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57795, ChEBI:CHEBI:57880, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2I7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44681;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2I7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2I7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2I7};
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9Y2I7};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z1T6}. Early
CC endosome membrane {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q9Y2I7}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Y2I7}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Z1T6}.
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DR EMBL; AAFI02000027; EDR41082.1; -; Genomic_DNA.
DR RefSeq; XP_001732989.1; XM_001732937.1.
DR AlphaFoldDB; B0G126; -.
DR SMR; B0G126; -.
DR STRING; 44689.DDB0234209; -.
DR PaxDb; B0G126; -.
DR PRIDE; B0G126; -.
DR EnsemblProtists; EDR41082; EDR41082; DDB_G0279149.
DR GeneID; 8621895; -.
DR KEGG; ddi:DDB_G0279149; -.
DR dictyBase; DDB_G0279149; pip5k3.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_227573_0_0_1; -.
DR InParanoid; B0G126; -.
DR OMA; HRQYVHG; -.
DR PRO; PR:B0G126; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; ISS:dictyBase.
DR GO; GO:0052810; F:1-phosphatidylinositol-5-kinase activity; IEA:RHEA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:dictyBase.
DR GO; GO:0090383; P:phagosome acidification; IMP:dictyBase.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:dictyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1905161; P:protein localization to phagocytic vesicle; IMP:dictyBase.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.800.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR044769; PIKfyve_PIPKc.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasmic vesicle; Endosome; Kinase; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..2656
FT /note="1-phosphatidylinositol 3-phosphate 5-kinase"
FT /id="PRO_0000387998"
FT DOMAIN 2275..2596
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT ZN_FING 198..255
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 24..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1710..1844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2031..2127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2179..2208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2246..2304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2615..2656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1741..1823
FT /evidence="ECO:0000255"
FT COILED 2019..2061
FT /evidence="ECO:0000255"
FT COMPBIAS 54..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1752..1800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2192..2208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2247..2304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 2656 AA; 299097 MW; 75FD652210C4CF25 CRC64;
MAESFQQLGV GSKSNERSFF SKFFGTDDSQ KDFGPLPEIE YSDEQRFNPY PAIYEKKNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNSN GNGNRSNSSL NNSNNNNQVR RTHSPSVSNK
SDESNTTNTN TNITTNTNIT TNTNTNTNTN STNNDTSSNV TQQQLLTNLG QSKIISALKT
KFQRPLPPVD DKKFWMPDHS SAVCYECSEE FTTFKRRHHC RLCGQIFCWK CSQKTLTDGK
GERVRVCNFC YRRYMAPDDL DMEGYHYDPI TGTVISLITN NDDGTNLNNG NGLIKLDGST
HNMNVSLGNS GDNSSFVQSP NNNFSQSPTF SQQQQQQQQQ QQQQQQQQQQ QQQQQTTGVM
SGLNPFSNST LLFGRNNNNN NQQQQQPIIE EDKQYYGDIN TSYNNSYFNN NGFNNFNNEH
YNNTNFNATS LNLNSQLHSN LLANTNGELF YDNSQHSISN YGNLDHHQQQ QQSNSHGSLS
ATPSNTPSGL ISPIVGAPSI LDPNKMIFYS DQEGNYDNLD DYETSSSDGS DNDNEDNHLK
SSHSSANDLG TSNTVSTGES NSESKLSSSS NDISIHHHHY HHHHHHSHGN LLKSNSLTPL
NLNNNNIIIN NNNINNNNNN DNGNDDNNNN NNDNNNNTTI EVDPRHSMPS KTSNTSFSMA
SLPSIFKLPT IGRNNNNNNN SGSGNSQYLS ANSNASNSIS PPNSARGSSS NPNSMTPTPT
LSSSFSNLPN AETSPPSLVK AKQQQQQQQQ QQQQPQPVLQ PTIHHPLKTS LPMFSTQSPP
PPTNQLAQST SMAPPPSIFS PLGKLQALSH PSSSSNNQQQ QQPQIVKPII IAPNSLFFSD
PSIVSLKSHP KTTNKTKFLE KYPLPKKYYE STENIIDTFG FKRTPSTEGN LLSQMLATSK
QKEFDEKERL KISNNPQMSV YIQHINNLVS EQLEKNNIDL SWRSIIIDLT KKATDNVKIF
VRKGDKMSTN EYIKIKKIPG GNKSECNYVD GVVMTKILTH KKMKDKFINP KILLLSCSVE
FQRVENKFLY FDQLLQQEKE YLRILVSKIA ERKPDLVLVE KTVSRHAQDF LLDAGISLAL
NVKPKLLERL GRCLGGEVLP TLDIIYNNNS NNNNSNSIQL QQQQNSNSPA SLQNSTTTTN
NNNNNNNNST TLGSCGQFKV ITYSEIGLKE KEILGKKTLM YFEKCPVELG ATIIIRGEDL
AVLKIIKKIL KLSIFSMHNA YLELKYLNDQ SSTSNLLFVN NNGQNLSCSP QIKFPLPKTY
PTIPWKYQFT SQHIPVKKAL LTSFYKPHSD FGQQQSVIQW TSDDEVLGIG TSDAFKHCDM
KFPIENESIY DHQSIVFSHS IFCNSNQCIP FEIHAIDYYT DNDLTLGEFL SKFCFSLHIC
NIKECNRPLI EHERTFMNST TRINICVQKT QTIQDRPTNS SPAQQRNQPV QRAGINVINL
CKICNKFSPE SPMSEEAWEM SFGKFLELCF FGFLPIKTGI SPECSHNNAK DHISYFYYQD
LAAIFSYEPL PSLELSLPPK NLKATYTEKQ RQSVRAKELE IMNQCANQVY SAIHERLYEI
GQENQGDRVQ ELIPSLVQEK QLICSKIESL LLLPESAHKS NDQIINLTKL LYANFMTWNS
QLTGLIDSTS YQRSKRNVQQ QQQQQQHQQS QQPQPQILIG GDVYSDSHLH TDSVKKINSK
QHSHNTILLQ SIQSNQEQQL EQQEEFEINV NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNTIDN KSENENENKN ENKNENENEN ENKNENKNEN ENENKKENEN QLEIKNENND
SGEEITNNNN NNNNNNNNNN NNNNNNNNNI DNNNNKDENI SSTPLLSPSS VLGVSNSGIN
QAFLNAPNNT YNSVEQDLTL PLNHQSLNFA VGGLVSPGSS SGGLPVGSVP NSSSMPSIHN
GGSGNIPSNL VGSASGLSTN YSPNALKDPK KLKIIDTIAG IVSSISQTRI LGPTMPYLLL
ESTDNVALFE NEPSTTIAYT LSSSDFKIAL NSLLDEEWKR ISEIEKQYEL QQQQQQDSQD
LESSSQQQQQ QQQQQQEQQE QPSLPTPSHP LSQSMNFSPS SLLKISSSSL PKDNNNSSEN
KPNSETNDIV RSRGSVKLSG SPISISPLSN AFEKRKSTSL SSSANNSPIS SILEKEKKLK
QQSPSLSNSL SGQTIINNNQ QQQQQQQPSP IIIDEKDDRN TEKSSIIETD SIIEDLNINQ
DESNITNEDG GKIGDYESEL LYDHHQQGDS ENNNNNNNNN NNNNNNNNNN NNNNNNNNTN
NNNEQQINNS DTEGDSDSIK SSNSNIYSEK NIKLSKLMVS TQRKEIRSRF KFEKNGYELN
IFCSSYYPVQ FHALREYMCG DQEFIQSLTR SKIWNAKGGK SGSSWNKTLD DRFILKQVSR
IELESFLDFA PLYFEYICKS FLNQIPTALC KILGVFTVRW KDSNGKALKK DLIVMENLFH
SKCISKTYDL KGSLRGRLVK NESEVLLDEN LLQASFASPI CLGEYDKTRV ALAVWNDTAF
LSSLNVMDYS LLSGIDNQSN QLVVGIIDYM RKFTWDKALE MKVKQSGIMG GGGKVPTVIS
PKQYKLRFRD AMWLYFTLSP DKFTKVKHLM PYEKKKNNNN NYNYNNFNNN NFNNNNNISN
NGNGNINQRQ VQQINK
