ID A0A2I2UMQ8_FELCA Unreviewed; 2061 AA.
AC A0A2I2UMQ8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 33.
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=PIKFYVE {ECO:0000313|Ensembl:ENSFCAP00000033804.3};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000033804.3, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000033804.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000033804.3,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000033804.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000033804.3,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000033804.3}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000033804.3};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; AANG04002752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSFCAT00000045192.3; ENSFCAP00000033804.3; ENSFCAG00000003977.6.
DR GeneTree; ENSGT00940000156307; -.
DR Proteomes; UP000011712; Chromosome C1.
DR Bgee; ENSFCAG00000003977; Expressed in embryonic head and 10 other cell types or tissues.
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; 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:UP000011712};
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 1746..2061
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 60..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1787
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 66..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 455..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1706..1732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2061 AA; 232997 MW; D4E41B792C9B2AC3 CRC64;
MATDDKTSPT LDSANDLPRS PTSPSHLTHF KPLTPDQDEP PFKSAYSSFV NLFRFNKERV
EGGQGEQPSL SGSWTSPQLP SRTQSVRSPT PYKKQLNEEL QRRSSAVLEE NSLQHPQENT
DTRRKAEPAF GGHDPRTAVQ LRSLSTVLKR LKEIMEGKSQ DSDLKQYWMP DSQCKECYDC
SEKFTTFRRR HHCRLCGQIF CSRCCNQEIP GKFMGYTGDL RACTYCRKIA LSYAHSTDSN
SIGEDLNALS DSASSVSVLD PNEPRTPVGS RKASRNIFLE DDFAWQSLIH PDSSNTPLST
RLVSVQEDAG KSPARNRSAS ITNLSLDRSG SPMVSSYETS VSPQANRTYV RTETTEDERK
ILLDSVQLKD LWKKICHHSS GMEFQDHRYW LRTHPNCIVG KELVNWLIRN GHIATRAQAI
AIGQAMVDGR WLDCVSHHDQ LFRDEYALYR PLQSTEFSET PSPDSDSVNS VEGHSEPSWF
KDIKFDDSDT EQIAEEGDDN LTNSASPSKR TSVSSFQSTV DSDSAASISL NVELDNVNFH
IKKPSKYPHV PPHPADQKEY LISDNGGQQL SISDAFIKES LFNRRVEEKS KELPFTPLGW
HHNNLELLRE ENGEKQAMER LLSANHNHMM ALLQQLLHNE SLSPSWRDII VSLVCQVVQT
VRPDVKNRDD DMDIRQFVHI KKMNSCIKNP KILLLKCSIE YLYREETKFT CIDPIVLQER
EFLKNYVQRI VDVRPTLVLV EKTVSRIAQD MLLEHGITLV INVKSQVLER ISRMTQGDLV
MSMDQLLTKP HLGTCHKFYM QIFQLPNEQT KTLMFFEGCP QHLGCTIKLR GGSDYELARV
KEILIFMICV AYHSQLEISF LMDEFAMPPT LTQNPSFHSL IEGREDEGTA QEPFSGSPLP
REPDFPPEFL PSDDSSLLES RIVFEKGDQE NRSIPQDVAC LKHQEYATAA CPAGIPCALF
PSVPESLLPL HVDDQQDAVG LEQPEALQHP DELQDPKSQM RAFRDPLQDD TGLYVTEEVT
SSEDKRKTYS LAFKQELKDV ILCISPVITF REPFLLTEKG MRCSTRDYFA EQVYWSPLLN
KEFKEVESRR KKQLLRDLSG LQGMNGSVQA KAIQVLPSHE LVSTRIAEHL GDSQSLGRML
ADYRARGGRI QQKNADPFAH SKDVPGTSSG RSGSKTDGDE EKGLIPSDAV WSTKVDCLNP
VNHQRLCVLF SSSSAQSSNA PSACVSPWIV TMEFYGKNDL TLGIFLERYC FRPSYQCPSM
FCDTPMVHHI RRFVHGQGCV QIILKELDSP VPGYQHTILT YSWCRICKQV TPVVALSNES
WSMSFAKYLE LRFYGHQYTR RANAEPCGHS IHHDYHQYFS YNQMVASFSY SPIRLLEVCV
PLPKIFIKRQ APLKVSLLQD LKDFFQKVSQ VYLAVDERLA SLKTDTFSKT REEKMEDIFA
QKEMEEGEFK NWVEKMQARL MSSSADAPQQ LQSIFESLIA KKQSLCEVLQ AWNNRLQDLF
QQEKGRKRPS VPPSPGRLRQ GEESKISAMD AAPRNISPGL QNGEKEDRFL TTLSSQSPAS
SAHLQLPTPP EALPEQLAGA PPELDTASSS EDVFDGHLLG STDSQVKEKS TMKAIFANLL
PGNSYNPIPF PFDPDKHYLM YEHERVPIAV CEKEPSSIIA FALSCKEYRN ALEELSKATQ
RNSAEEGLPT NSTLDSRPKS SSPIRLPEVS GGQTNRTAEA EPQPTKKTSG MLSFFRGTAG
KSPDLSSQKR ETLRGADSAY YQVGQTGKEG TENQGAESQD EVDGGDTQKK QLINPHVELQ
FSDANAKFYC RLYYAGEFHK MREVILGSSE EDFIRSLSHS SPWQARGGKS GAAFYATEDD
RFILKQMPRL EVQSFLDFAP HYFNYITNAV QQKRPTALAK ILGVYRIGYK NSQNNTEKKL
DLLVMENLFY GRKMAQVFDL KGSLRNRNVK TDTGKESCDV VLLDENLLKM VRDNPLYIRS
HSKAVLRASI RSDSHFLSSH LIIDYSLLVG RDDTSNELVV GIIGKMPTVV SPELYRTRFC
EAMDKYFLMV PDHWTGLGLN C
//
