ID W5QCJ0_SHEEP Unreviewed; 2105 AA.
AC W5QCJ0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:ENSOARP00000020437.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000020437.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000020437.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000020437.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000020437.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AMGL01055587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01055588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01055589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSOART00000020719.1; ENSOARP00000020437.1; ENSOARG00000019028.1.
DR HOGENOM; CLU_000480_2_1_1; -.
DR Proteomes; UP000002356; Chromosome 2.
DR Bgee; ENSOARG00000019028; Expressed in thymus and 55 other cell types or tissues.
DR ExpressionAtlas; W5QCJ0; baseline.
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; 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; 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:UP000002356};
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 163..223
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 370..445
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 1765..2091
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1808
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..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1568..1586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2105 AA; 237683 MW; 0CF7F780BFCAD983 CRC64;
MATDDKTSPT LDSANDLPRS PTSPSHLTHF KPLTPDQDEP PFKSAYSSFV NLFRFNKERG
EGGQGEQQSL SGSWTSPQLP SRTQSVRSPT PYKKRLNEEF QRRSSVLGNP NSDTRRKAEP
TFGGHDPRTA VQLRSLSTVL KRLKEIMEGK SQDSDLKQYW MPDSQCKECY DCNEKFTTFR
RRHHCRLCGQ IFCSRCCNQE IPGKFMGYTG DLRACTYCRK IALSYAHSTD SNSIGEDLNA
LSDSASSVSV LDPSEPRTPV GSRKASRNIF LEDDFAWQSL IHPDSSNTAL STRLVSVQED
AGKSPARNRS ASITNLSLDR SGSPMVPSYE TSVSPQANRT YVRTETTEDE RKILLDSVQL
KDLWKKICHH SSGMEFQDHR YWLRTHPNCI VGKELVNWLI RNGHIATRAQ AIAIGQAMVD
GRWLDCVSHH DQLFRDEYAL YRPLQSTEFS ETPSPDSDSV NSVEGHSEPS WFKDIKFDDS
DTEQIAEEGD DNLTNSASPS KRTSVSSFQS TVDSDSAASI SLNVELDNVN FHIKKPSKYP
HVPPHPADQK EYLISDNGGQ QLSISDAFIK ESLFNRRVEE KSKELPFTPL GWHHNNLELL
REENGEKQAM ERLLSANHNH MMALLQQLLH SESLSTSWRD IIVSLVCQVV QTVRPDVKNR
DDDMDIRQFV HIKKIPGGKK FDSVVVNGFV CTKNIAHKKM NSSIKNPKIL LLKCSIEYLY
REETKFTCID PIVLQEREFL KNYVQRIVDV RPTLVLVEKT VSRIAQDMLL EHGITLVINV
KSQVLERVSR MTQGDLVMSM DQLLTKPHLG TCHKFYMQMF QLPNEQTKTL MFFEGCPQHL
GCTIKLRGGS DYELARVKEI LIFMICVAYH SQLEISFLMD EFAMPPTLTQ NPSFHSLIEG
QEDEGAAQEP FSGSPLPREP DFPPDFLPSD DGSLLESRIL FEKGDQENKS VPQDVASLKP
QEHAPAVCPM GAPCALFPSV PESLLPLHVD DQEDAIGSEQ PEALQQIEEL PDPTSQMRAF
RDPLQDDTGL YVTEEVTSSE DKRKTDSLTF KQELKDVILC ISPVITFREP FLLTDKGMRC
STRDYFAEQV YWSPLLNKEF KEMESRRKKQ MLRDLSGVQG MNGSVQAKSI QVLPSHELVS
TRIAEHLGDS QSLGRMLADY RARGGRIQQK NSDPFAYSKE ASGTSSGKSG SRTEGDEEKG
LITSDAVWST KVDCLNPVNH QRLCVLFSSS SAQSSNAPSA CVSPWIVTME FYGKNDLTLG
IFLERYCFRQ RPSYQCPSMF CDTPMVHHIR RFVHGQGCVQ IILKELDSPV PGYQHTILTY
SWCRICKQVT PVVALSNESW SMSFAKYLEL RFYGHQYTRR ANAEPCGHSI HHDYHQYFSY
NQMVASFSYS PIRLLEVCVP LPKIFIKRQV PLKVSLLQDL KDFFQKVSQV YLAVDERLAS
LKTDTFSKSR EEKMEDIFAQ KEMEESEFKS WTEKMQARLL SSSMETPQQL QSVFESLIAK
KQSLCEVLQA WNNRLQDLFQ QEKGRKRPSV PPSPGRLRQG EESKISAVDA SPRNASPGLP
NGEKEDRFLA TLSSQSSTSS PHLQLPTSPE GVPEQAMGGP PELDTASSSE DVFDGHLLGS
TDSQVKEKST MKAIFANLLP GNSYNPIPFP FDPDKHYLMY EHERVPIAVC EKEPSSIIAF
ALSCKEYRNA LEELSKATQR NSAEEGLPTN STLDSRPKSS SPIRLPEISG GQTNRAVEAE
PQPTKKASGM LSFFRGTAGK SPDLSSQKRE TLRGADSAYY QVGQTGKEGT ENQGIEPQDE
VDGGDTQKKQ LTNPHVELQF SDANAKFYCR LYYAGEFHKM REVILGSSEE 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
//
