ID F6XJV0_CIOIN Unreviewed; 1915 AA.
AC F6XJV0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000021673.2, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000021673.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; EAAA01000846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCINT00000021919.2; ENSCINP00000021673.2; ENSCING00000006215.3.
DR GeneTree; ENSGT00940000156307; -.
DR HOGENOM; CLU_000480_2_1_1; -.
DR Proteomes; UP000008144; Chromosome 12.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04448; DEP_PIKfyve; 1.
DR CDD; cd15725; FYVE_PIKfyve_Fab1; 1.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR043548; PIKfyve.
DR InterPro; IPR037378; PIKfyve_DEP.
DR InterPro; IPR044769; PIKfyve_PIPKc.
DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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 PANTHER; PTHR46715; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE; 1.
DR PANTHER; PTHR46715:SF1; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 9..71
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 215..289
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 1565..1901
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 745..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1602..1623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1077
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1915 AA; 218089 MW; 63608D34CDFBB3A8 CRC64;
DLKQYWMPDK HCHECYECGD RFTTFRRRHH CRICGHIFCS RCCYQFIPRE VIAQAGVGML
RSCTYCYSLL TSYTKPTVTN TTAKNLQILN EYDGLIDVRI NICLLEIVYS TVSLEAMLLP
KNLIFFKVLK FIQASHESNT SLNLQLDPFN TSFSRHPKGR SRSLVSGRGS PIEDGVMSPM
QTEATRPPFN NQHEQVTFAK GSVQLHELWA KISDDKDGLE FRDHRYRLRK FTQSVTGTEL
VDWLITRGIT ETRPQGCAIA QALLDAEWIK SVVDDRVFHD EYCLYQHGTP IKQSRRPSRQ
SRVLSHEYGT TLDNEPNWVK EISNEEEKDS DDGLHFWSPV IHNPSLLSFR DLYRHDSVNP
SQSGGSLSSY VEIDNEHKII KYKRPSSPPP LESGLKQPKF VDENVTSISA DYIRSKFGFG
LLCLCLNMLP VSCVGWREKE VQTSHLPSHV KHAFYRLKKL YFRHSMKFLH QLFVREKLHT
SWSDVVVPLA KQICDTVTPN AEVNMEICHY VHVKKLLDNE PQDSRLLWGV VFSHNVVHNK
MMNRIDNPTI MLLATPLEYQ RVQYKLSSLD PIVQQEPEFL KHLISRIVSR KPDIVMSQCS
VSHEGRRLLL DAGITLIINV KQPVMERLSR CTNADVAYSI DQLKTVRLGS CDYHTDPTHS
LRSESSTNAY KTLIYVDGCD PTKGCSVILR DLPHYLRRQD TDHVIQDRLS RVKRVLLFLI
RIMYHGKLEI SYLLDQQDVA SSFPSSRKKK RCRRSKPTVA PPPIKGFSSE TSGRSLYLFI
WNVIFVWGRY FMTCPWFLTP TMRCMKPPFC SSKNYIGCRF PVFNKSQTII ILESEVHSAE
ESVVASGGFV SSVSDDNTIT PDFLSANDRT PDSCPDSPLF NAAHKGATFT LPNVDKPNIE
VSTELEQSKH GKVLEEKSKV FQDFLKTSLL STSPLIQPVV PFLLTNKGPS SPLRKYLPER
LFWSDSFCSN PESVKHEWVG KNEMILSVEV EAGSSVKQWQ GVKHDRMTSH VRMPSQVSTR
ALSKPASSTQ MKDLLASFRA RGSNLTPATR TTPSSWGHPL LPPPPSPPTP PEDLTEPTLP
PLDCLEPHNH QHIFVLFSSY SLQSPNAPYP CVIPWAVDID YYHGNDITIG GFLERYCFRP
SYHCPSPTCK RPMVEHVRSF VHGNTAMNIV LKELSKPIPV PHILSWCWDP TTKTSTDIRP
LSEDGWSMSF AKFLELRLQT HPTVKQDGEV PAFGAFQYFL FKDIVAAFKC YHVQVHDVAL
PSSKMALSSH GTTQVGYEAM DSIQDMILDA KSSNPYDLLD VGDVGFDVGT LQQTRGNHFD
ELLSMYQDER CHLRDTADNI HLTLLSIKKR NSNNRQSTEE SVIVMRPCEK LVLTWNNRIS
KVFQQDKNSR RGSKSVPSYP NPPLPLDAVL TSENLKPKRS PVLPSLFETT EAEPASASLL
QMLRLYYRFN DVSMFNELFF PQDSADSIGS SYDDSALFSE KSPLTSSQSV PRVSMRSILT
HLRTTTPINM VEPPFPPDEH YLLPDTLNLG HVVRDTEPSS IIAYSLATSL YQKSSDAVSS
VARCSVARSS DARSSDARFS DAKSSDARSS DARSCYAKSS VASSTNISPT QAPTQPPHNP
PEHLEIQFSD STTKFYCKIY FASKFKDLRE KFLDIPESTY ITSLSRCVRW DARGGKSGLS
FHKTLDDRLV LKQMSKFELQ SFLDVAPSYL DHVSDAIREN TPTALSKILG VYRVSFRNMT
TNRSFKQDLL IMENLFYKRN IQQVFDLKGS VRNRHVKTGN DPNQNDLVLL DENLLSIMKD
HPLYVHQHTK VIIKKALHHD SSFLARHLII DYSLLVGIDD EKKEIVVGII DYMRTFTWDK
KLEMVVKSYG MIGRQGTRSM PTVVSPELYK TRFCDAMERY FQVVPDRWYG LQAYE
//
