STT4_SCHPO
ID STT4_SCHPO Reviewed; 1877 AA.
AC Q9USR3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Phosphatidylinositol 4-kinase stt4;
DE Short=PI4-kinase;
DE Short=PtdIns-4-kinase;
DE EC=2.7.1.67;
GN Name=stt4; ORFNames=SPBC577.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Acts on phosphatidylinositol (PI) in the first committed step
CC in the production of the second messenger inositol 1,4,5,-
CC trisphosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAB54814.1; -; Genomic_DNA.
DR PIR; T40550; T40550.
DR RefSeq; NP_595304.1; NM_001021211.2.
DR AlphaFoldDB; Q9USR3; -.
DR SMR; Q9USR3; -.
DR BioGRID; 277400; 11.
DR STRING; 4896.SPBC577.06c.1; -.
DR iPTMnet; Q9USR3; -.
DR MaxQB; Q9USR3; -.
DR PaxDb; Q9USR3; -.
DR PRIDE; Q9USR3; -.
DR EnsemblFungi; SPBC577.06c.1; SPBC577.06c.1:pep; SPBC577.06c.
DR GeneID; 2540883; -.
DR KEGG; spo:SPBC577.06c; -.
DR PomBase; SPBC577.06c; stt4.
DR VEuPathDB; FungiDB:SPBC577.06c; -.
DR eggNOG; KOG0902; Eukaryota.
DR HOGENOM; CLU_000893_3_0_1; -.
DR InParanoid; Q9USR3; -.
DR OMA; HNYLESD; -.
DR PhylomeDB; Q9USR3; -.
DR Reactome; R-SPO-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-SPO-1660514; Synthesis of PIPs at the Golgi membrane.
DR PRO; PR:Q9USR3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISO:PomBase.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:PomBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR045495; PI4K_N.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF19274; PI4K_N; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..1877
FT /note="Phosphatidylinositol 4-kinase stt4"
FT /id="PRO_0000314092"
FT DOMAIN 1305..1491
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 1593..1861
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1492..1625
FT /note="Pleckstrin homology (PH) domain conferring
FT phosphoinositide binding specificity"
FT /evidence="ECO:0000250"
FT REGION 1599..1605
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1728..1736
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1747..1771
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 1877 AA; 213963 MW; AD4577CC2D4EC5BD CRC64;
MDCIDKSIRR ESLRKLGCLP DHGWNLFVQS SNRYSKLLEA DSKLFKAQRI EDTVLSICEV
TLENKASENA LTLFQQLRFY LLNYLFLEDT SEYKSVLCSL DESVYPNLLP LTANICPCIL
KALLALVRQH RELSSDIVKF LNSIFLALTR ILNTPHSSNN NPTHTKTTIF EKVFYASHLG
FFFEEIADAC ISALPQDACL WAMEVCNTIL VSDLPCKLID LHNDSFLHHS NYYAGFGLSY
YLYLSSMKAY INSSGCLWYE DATSFWDIVK HRPSSPEEKP FLTQFQSILN LSDKFLSKTG
TLRLQEKLGT SCNLFFVLVL KLALLSSSYI GFVPYTYSDW INVLLGSISE DPELLPHLIE
LMASLACVFP THFQFAMKRL RLIAIYAPRF DDGNVTYAQL ASRKLAQLFN YSSRDTAITS
IYQFANLLSP ADTPDSYLAA PKERLSISDN MSSSSSQTAT VNTISNYLNV IDSVREIALT
VNDEKIYGLA ISLLIQKFSR KFDSRVSTEL VRTLADISTK ANDRDFSILV QFYSIQNKML
VKNGDEALTI AICDSRCLIA RGTESNSFKR SDLLKSLLEE IIHIGIVRDT PAPELKGYYF
GMSKAVQALV ECVAGTDWSS LPKEEMYPAL FRDMWFTLVI NRFRYSVDLG ETLEVDLENI
AKNSPLLVFE DFGSNFESNL ELNTVLRTHI EHSVISQIKS ELLVRVPNID LKPLSTSEIC
FLSAVLLLES LRCKSNKLSA LVEYLLDPSL RDSQLPQSIR AIALYNLTSF VESLSKERRV
ASSTIDEFQK LLCLCCNRVD CVRQLALECM NYIMETLPHL LGIKEILFSV LELSSLLWKA
RTEECTDQYV PQLLYKSNKL NLSVILSDIY SCREEVLFQF NRHARSWIQN SSKAIPYQVK
NLLESYLADF VDFDDLEVVE LGRSLAVELG TRIVSSDRDN FVLPAFGNWT PDTSSEFMAE
YTIRQRYSHV DNSILNIEGD MSTDRIDLIL NEKSKLFETH LAALKSLEDD ILQGNTVSPQ
RLRNEVRKAA AHAVQEPIFQ FSVLARKIVR IPFLDFSPSS FKLGITLWNW MMNQVPSFSS
FLISNIIRNW KNEIVTEKRG YFSTAKSKSP LALPMTYSPT ERASFLSYKN KVMSQMIPHL
LLLQLIAGNF EGFWYGDRQT AKLIVHFMKF VLKKITSMEV NLNVLTRELH FKFVSFGLRI
AENLLNSPLG SRFYNLCVDA GLCWFSGMPN WTYGADKLHV AAEISVMRSL RDKLDSFLLR
YPLKVSTTLK QKLLIILLNN EMYMLYTWLT PVLHGRNVRM VEPIPDSDAA SSPITLEMLQ
VAWNVSPNIV LYAPKRFQNA PLKQMALNFV IANPFTSVKH EVALEYLFEH YPSGEFPIDR
KFILYWEPMY PVSGPVMFMP NVKWNPQLLQ YTMRSMESYP VSVTFFYVPQ IVQSLRYDSM
GYAESFILET SGTSQLFAHQ ILWNMKANLY KDEAATVPDS IKPILDRVMD KMINSLSGED
KQFYEREFTF FNEVTSISGK LKPFIRKSKP EKKAKIDEEM KKIKLDVGVY LPSNPDGVIV
GIDRKSGKPL QSHAKAPFMA TFKIRKEKLV DADPEELAVN GTEEEAGDSA KKQTYEVWQS
AIFKVGDDCR QDVLTLQLIA MFKNIFNSVG LDVYLFPYRV TATNPGCGVI DVLPNCISRD
MLGREAVNGL YDYFRTKFGD EDSIAFQKAR SNFVQSMAAY SVITYLLQFK DRHNGNIMID
DQGHILHIDF GFIFDIAPGG ITFESAPFKL TTEMIAVMGG SNKSQPFQWF QELCVKAFLA
CRPYAHYICQ AVEVMLDSGL PCFKGQLTIT HCLERFALNL NERQASTFML HLIEQSYANK
RTLMYDQFQK ATNGIPY
