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Database: UniProt
Entry: A0A2Y9JFM2_ENHLU
LinkDB: A0A2Y9JFM2_ENHLU
Original site: A0A2Y9JFM2_ENHLU 
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
//
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