ID A0A2Y9JFM2_ENHLU Unreviewed; 2055 AA.
AC A0A2Y9JFM2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
GN Name=LOC111145703 {ECO:0000313|RefSeq:XP_022356570.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022356570.1};
RN [1] {ECO:0000313|RefSeq:XP_022356570.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022356570.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_022356570.1; XM_022500862.1.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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; cd03334; Fab1_TCP; 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; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
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; 2.
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; SSF54849; GroEL-intermediate 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:UP000248482};
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 171..231
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 378..453
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 1715..2041
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1646..1756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1646..1669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2055 AA; 232400 MW; D8CF8666725BEC6D CRC64;
MATDDKASPT LDSANDLPRS PTSPSHLTHF KPLTPDQDEP PFKSAYSSFV NLFRFNKERA
EGGQGEQQSL AGSWASPQLP SRTQSVRSPT PYKKQLNEEL QRRSSAVLEE NSLQHPQENT
DTRRKAEPTF GGHDPRTAVQ LRSLSTVLKR LKEIMEGKSQ DSDLKQYWMP DSQCKECYDC
SEKFTTFRRR HHCRLCGQIF CSRCCNQEIP GKFMGYTGDL RACTYCRKIA LSYAHSTDSN
SIGEDLNALS DSASSVSVLD PSEPRTPVGS RKASRNIFLE DDFAWQSLIH PDSSNTPLST
RLVSVQEDAG KSPARNRSAS VTNLSLDRSG SPMVSSYETS VSPQANRTYV RTETTEDERK
ILLDSVQLKD LWKKICHHSS GMEFQDHRYW LRTHPNCIVG KELVNWLIRN GHIATRAQAI
AIGQAMVDGR WLDCVSHHDQ LFRDEYALYR PLQSTEFSET PSPDSDSVNS VEGHSEPSWF
KDIKFDDSDT EQIAEEGDDN LTKYLISDNG GQQLSISDAF IKESLFNRRV EEKSKELPFT
PLGWHHNNLE LLREENGEKQ AMERLLSANH NHMMALLQQL LHNESLSPSW RDIIVSLVCQ
VVQTVRPDVK NRDDDMDIRQ FVHIKKIPGG KKFDSVVVNG FVCTKNIAHK KMNSCIKNPK
ILLLKCSIEY LYREETKFTC IDPIVLQERE FLKNYVQRIV DVRPTLVLVE KTVSRIAQDM
LLEHGITLVI NVKSQVLERI SRMTQGDLVM SMDQLLTKPH LGTCHKFYMQ MFQLPSEQTK
TLMFFEGCPQ HLGCTIKLRG GSDYELARVK EILIFMICVA YHSQLEISFL MDEFAMPPTL
TQNPSFHSLI EGREDEGTAQ EPFSGSPLTR EPDFPAEILP SEDGSLLEPR TVFEKGDQEN
KSVTPDAASL KHQEYATTAC AAGIPCALFP SVPESLLPLH VDDPQDALGM EQPEPLQHAD
ELQDPKSPMR TFRDPLQDDT GLYVTEEVTS SEDKRKTYSL AFKQELKDVI LCISPVITFR
EPFLLTEKGM RCSTRDYFAE QVYWSPLLNK EFKEMESRRK KQLLRDLSGL QGMNGSVQAK
SIQVLPSHEL VSTRIAEHLG DSQSLGRMLA DYRARGGRIQ QKNADPFAYS KEVPGTASGR
SGSKIEGDEE KGLIPNDAVW STKVDCLNPV NHQRLCVLFS SSSAQSSNAP SACVSPWIVT
MEFYGKNDLT LGIFLERYCF RPSYQCPSMF CDTPMVHHIR RFVHGQGCVQ IILKELDSPV
PGYQHTILTY SWCRICKQVT PVVALSNESW SMSFAKYLEL RFYGHQYTRR ANAEPCGHSI
HHDYHQYFSY NQMVASFSYS PIRLLEVCVP LPKIFIKRQA PLKVSLLQDL KDFFQKVSQV
YLAVDERLAS LKTDTFSKTR EEKMEDIFAQ KEMEEGEFKN WIEKMQARLM SSSVDAPQQL
QSVFESLIAK KQSLCEVLQA WNNRLQDLFQ QEKGRKRPSV PPSPGRLRQG EESKISAMDA
APRNISPGLQ NGEKEDRFLT TLSSQSSTSS THLQLPTPPE VMPEQLGAGP PDLDTASSSE
DVFDGHLLGS TDSQVKEKST MKAIFANLLP GNSYNPIPFP FDPDKHYLMY EHERVPIAVC
EREPSSIIAF ALSCKEYRNA LEELSKATQR SSAEEGLPTN STLDSRPKSS SPIRLPEVSG
GQTNRAAEAE PQPTKKASGM LSFFRGTAGK SPDLSSQKRE TLRGADSAYY QVGQTGKEGT
ESQGIEPQDE VDGGDTQKKQ LINPHVELQF SDANAKFYCR LYYAGEFHKM REVILGSSED
DFIRSLSHSS PWQARGGKSG AAFYATEDDR FILKQMPRLE VQSFLDFAPH YFNYITNAVQ
QKRPTALAKI LGVYRIGYKN SQNNTEKKLD LLVMENLFYG RKMAQVFDLK GSLRNRNVKT
DTGKESCDVV LLDENLLKMV RDNPLYIRSH SKAVLRASIR SDSHFLSSHL IIDYSLLVGR
DDTSNELVVG IIDYIRTFTW DKKLEMVVKS TGILGGQGKM PTVVSPELYR TRFCEAMDKY
FLMVPDHWTG LGLNC
//