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PI4KB_CALJA
ID   PI4KB_CALJA             Reviewed;         816 AA.
AC   B0KWC1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Phosphatidylinositol 4-kinase beta;
DE            Short=PI4K-beta;
DE            Short=PI4Kbeta;
DE            Short=PtdIns 4-kinase beta;
DE            EC=2.7.1.67 {ECO:0000250|UniProtKB:Q9UBF8};
GN   Name=PI4KB; Synonyms=PIK4CB;
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA   Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA   Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA   Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA   Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA   Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA   Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA   Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA   Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA   Tsipouri V., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first
CC       committed step in the production of the second messenger inositol-
CC       1,4,5,-trisphosphate (PIP). May regulate Golgi
CC       disintegration/reorganization during mitosis, possibly via its
CC       phosphorylation (By similarity). Involved in Golgi-to-plasma membrane
CC       trafficking (By similarity). {ECO:0000250|UniProtKB:O08561,
CC       ECO:0000250|UniProtKB:Q9UBF8}.
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; Evidence={ECO:0000250|UniProtKB:Q9UBF8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC         Evidence={ECO:0000250|UniProtKB:Q9UBF8};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9UBF8};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q9UBF8};
CC   -!- ACTIVITY REGULATION: Inhibited by wortmannin. Increased kinase activity
CC       upon interaction with NCS1/FREQ. {ECO:0000250|UniProtKB:O02810}.
CC   -!- SUBUNIT: Interacts with ARF1 and ARF3 in the Golgi complex, but not
CC       with ARF4, ARF5 or ARF6 (By similarity). Interacts with NCS1/FREQ in a
CC       calcium-independent manner. Interacts with CALN1/CABP8 and CALN2/CABP7;
CC       in a calcium-dependent manner; this interaction competes with NCS1/FREQ
CC       binding (By similarity). Interacts with ACBD3. Interacts with ARMH3,
CC       YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ, YWHAZ and SFN (By similarity).
CC       Interacts with GGA2 (via VHS domain); the interaction is important for
CC       PI4KB location at the Golgi apparatus membrane (By similarity).
CC       Interacts with ATG9A. {ECO:0000250|UniProtKB:O08561,
CC       ECO:0000250|UniProtKB:Q9UBF8}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Mitochondrion
CC       outer membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Golgi apparatus
CC       {ECO:0000250}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UBF8}.
CC       Note=Found in the outer membrane of mitochondria and membranes of the
CC       rough endoplasmic reticulum. Recruited to the Golgi complex by the
CC       small GTPase ARF to stimulate the synthesis of phosphatidylinositol
CC       4,5-bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi
CC       apparatus membrane by ACBD3, GGA2 is also involved in the recruitment.
CC       {ECO:0000250|UniProtKB:Q9UBF8}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DP000572; ABY82093.1; -; Genomic_DNA.
DR   RefSeq; XP_017821753.1; XM_017966264.1.
DR   AlphaFoldDB; B0KWC1; -.
DR   SMR; B0KWC1; -.
DR   STRING; 9483.ENSCJAP00000046570; -.
DR   Ensembl; ENSCJAT00000052949; ENSCJAP00000049607; ENSCJAG00000007455.
DR   Ensembl; ENSCJAT00000129704; ENSCJAP00000091206; ENSCJAG00000007455.
DR   GeneID; 100386139; -.
DR   KEGG; cjc:100386139; -.
DR   CTD; 5298; -.
DR   eggNOG; KOG0903; Eukaryota.
DR   GeneTree; ENSGT00550000074892; -.
DR   InParanoid; B0KWC1; -.
DR   OrthoDB; 1147978at2759; -.
DR   Proteomes; UP000008225; Chromosome 18.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; ISS:UniProtKB.
DR   GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1070.11; -; 1.
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; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048; PTHR10048; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM00146; PI3Kc; 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   Acetylation; ATP-binding; Endoplasmic reticulum; Golgi apparatus; Kinase;
KW   Lipid metabolism; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   CHAIN           2..816
FT                   /note="Phosphatidylinositol 4-kinase beta"
FT                   /id="PRO_0000365163"
FT   DOMAIN          52..242
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT   DOMAIN          535..801
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..68
FT                   /note="Interaction with ACBD3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   REGION          99..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..547
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          668..676
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          687..711
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   COMPBIAS        277..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   MOD_RES         263
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   MOD_RES         266
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BKC8"
FT   MOD_RES         277
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BKC8"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   MOD_RES         428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   MOD_RES         438
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   MOD_RES         517
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT   MOD_RES         519
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBF8"
SQ   SEQUENCE   816 AA;  91377 MW;  599BA628F99126C0 CRC64;
     MGDTVVEPAP LKPTSEPTSG PPGNNGGSLL SVITEGVGEL SVIDPEVAQK ACQDVLEKVK
     LLHGGVAVSS RGAPLELVNG DGVDSEIRCL DDPPAQIREE EDEMGASVAS GTAKGARRRR
     QNNSAKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL
     NMYIHMDEDV GDAIKPYIVY RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI
     LSDELKPAHR KRELPSLSPA PDTGLSPSKR THQRSKSDAT ASISLSSNLK RTASNPKVEN
     EDEELSSSTE SIDNSFSSPV RLAPEREFIK SLMAIGKRLA TLPTKEQKTQ RLISELSLLN
     HKLPARVWLP TAGFDHHVVR VPHTQAVVLN SKDKAPYLIY VEVLECENFD TTSVPARIPE
     NRIRSTRSVE NLPECGITHE QRAGSFSTVP NYDNDDEAWS VDDIGELQVE LPEVHTNSCD
     NISQFSVDSI TSQESKEPVF IAAGDIRRRL SEQLAHTPTA FKRDPEDPSA VALKEPWQEK
     VRRIREGSPY GHLPNWRLLS VIVKCGDDLR QELLAFQVLK QLQSIWEQER VPLWIKPYKI
     LVISADSGMI EPVVNAVSIH QVKKQSQLSL LDYFLQEHGS YTTEAFLSAQ RNFVQSCAGY
     CLVCYLLQVK DRHNGNILLD AEGHIIHIDF GFILSSSPRN LGFETSAFKL TTEFVDVMGG
     LDGDMFNYYK MLMLQGLIAA RKHMDKVVQI VEIMQQGSQL PCFHGSSTIR NLKERFHMSM
     TEEQLQLLVE QMVDGSMRSI TTKLYDGFQY LTNGIM
 
 
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