位置:首页 > 蛋白库 > PI3K_ARATH
PI3K_ARATH
ID   PI3K_ARATH              Reviewed;         814 AA.
AC   P42339; O22695;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Phosphatidylinositol 3-kinase VPS34 {ECO:0000303|PubMed:7972072};
DE            EC=2.7.1.137;
DE   AltName: Full=PI3-kinase VPS34 {ECO:0000303|PubMed:7972072};
DE            Short=AtVPS34 {ECO:0000303|PubMed:7972072};
DE            Short=PI3K VPS34 {ECO:0000303|PubMed:7972072};
DE   AltName: Full=PtdIns-3-kinase VSP34 {ECO:0000303|PubMed:7972072};
GN   Name=VPS34 {ECO:0000303|PubMed:7972072};
GN   OrderedLocusNames=At1g60490 {ECO:0000312|Araport:AT1G60490};
GN   ORFNames=F8A5.4 {ECO:0000312|EMBL:AAB71971.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seedling;
RX   PubMed=7972072; DOI=10.1073/pnas.91.24.11398;
RA   Welters P., Takegawa K., Emr S.D., Chrispeels M.J.;
RT   "AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an
RT   essential protein with homology to a calcium-dependent lipid binding
RT   domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:11398-11402(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   INTERACTION WITH VPS15.
RC   STRAIN=cv. Columbia;
RX   PubMed=22361507; DOI=10.1016/j.jgg.2012.01.002;
RA   Wang W.-Y., Zhang L., Xing S., Ma Z., Liu J., Gu H., Qin G., Qu L.-J.;
RT   "Arabidopsis AtVPS15 plays essential roles in pollen germination possibly
RT   by interacting with AtVPS34.";
RL   J. Genet. Genomics 39:81-92(2012).
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-3-phosphate) + ADP +
CC         H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC         EC=2.7.1.137;
CC   -!- SUBUNIT: Interacts with VPS15. {ECO:0000269|PubMed:22361507}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00880}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U10669; AAA83427.1; -; mRNA.
DR   EMBL; AC002292; AAB71971.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33693.1; -; Genomic_DNA.
DR   EMBL; BT000878; AAN41278.1; -; mRNA.
DR   PIR; B96630; B96630.
DR   RefSeq; NP_176251.1; NM_104735.4.
DR   AlphaFoldDB; P42339; -.
DR   SMR; P42339; -.
DR   BioGRID; 27568; 1.
DR   IntAct; P42339; 2.
DR   STRING; 3702.AT1G60490.1; -.
DR   PaxDb; P42339; -.
DR   PRIDE; P42339; -.
DR   ProteomicsDB; 226176; -.
DR   EnsemblPlants; AT1G60490.1; AT1G60490.1; AT1G60490.
DR   GeneID; 842344; -.
DR   Gramene; AT1G60490.1; AT1G60490.1; AT1G60490.
DR   KEGG; ath:AT1G60490; -.
DR   Araport; AT1G60490; -.
DR   TAIR; locus:2036546; AT1G60490.
DR   eggNOG; KOG0906; Eukaryota.
DR   HOGENOM; CLU_004869_0_0_1; -.
DR   InParanoid; P42339; -.
DR   OMA; GRQKCKI; -.
DR   OrthoDB; 204282at2759; -.
DR   PhylomeDB; P42339; -.
DR   BioCyc; ARA:AT1G60490-MON; -.
DR   BRENDA; 2.7.1.137; 399.
DR   PRO; PR:P42339; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P42339; baseline and differential.
DR   Genevisible; P42339; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IBA:GO_Central.
DR   GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IBA:GO_Central.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IDA:TAIR.
DR   GO; GO:0055046; P:microgametogenesis; IMP:TAIR.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   Gene3D; 1.25.40.70; -; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR035892; C2_domain_sf.
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; IPR002420; PI3K-type_C2_dom.
DR   InterPro; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR008290; PI3K_Vps34.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048; PTHR10048; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   PIRSF; PIRSF000587; PI3K_Vps34; 1.
DR   SMART; SM00142; PI3K_C2; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51547; C2_PI3K; 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   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..814
FT                   /note="Phosphatidylinositol 3-kinase VPS34"
FT                   /id="PRO_0000088819"
FT   DOMAIN          25..177
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT   DOMAIN          274..449
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT   DOMAIN          532..799
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          538..544
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..708
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   CONFLICT        37
FT                   /note="S -> A (in Ref. 1; AAA83427)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        452..453
FT                   /note="KL -> NW (in Ref. 1; AAA83427)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        557
FT                   /note="G -> R (in Ref. 1; AAA83427)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   814 AA;  93328 MW;  0A09926196E08D3E CRC64;
     MGANEFRFFL SCDINSPVTF RIEKLDGNLP VKKSSDSGVV SIAEEKKPEL YIECALYIDG
     APFGLPMRTR LKTTGPPYCW NELITLSSKY RDLTAHSQLA ITVWDVSCGK TEGLIGGATV
     LLFNSKMQMK SGKQKLRLWQ GKEADGSFPT STPGKVPRHE RGELERLEKL MNKYERGQIQ
     SIDWLDRLML KSLDTIKEQE STKHGSSHLF VVIDFCSFEH RVVFQESGAN LFITAPIGST
     NEFVTVWDTE LGKTNPSENK QLKLARSLDR GIIDRDLKPS NIERKSIQRV LKYPPTRTLS
     GDERQLLWKF RFSLMSEKRA LTKFLRCVEW SDVQEAKQAI QLMYKWEMID VCDALELLSP
     LFESEEVRAY AVSVLERADD EELQCYLLQL VQALRFERSD RSCLSQFLVQ RALQNIELAS
     FLRWYVAVEL HDHVYAKRFY STYELLEENI IKLPPGVNGE DGYQLWQSLV RQTELTAQLC
     SITREVRNVR GNTQKKIEKL RQLLGGLLSE LTYFEEPIRS PLTPNVLIKG IVAGESSLFK
     SALHPLRLTF RTPEEGGSCK LIFKKGDDLR QDQLVVQMVW LMDRLLKLEN LDLCLTPYKV
     LATGHDEGML EFIPSRSLAQ ILSEHRSITS YLQKFHPDEH APFGITATCL DTFIKSCAGY
     SVITYILGIG DRHLDNLLLT DDGRLFHVDF AFILGRDPKP FPPPMKLCKE MVEAMGGAES
     QYYTRFKSYC CEAYNILRKS SNLILNLFHL MAGSTIPDIA SDPEKGILKL QEKFRLDMDD
     EACIHFFQDL INESVSALFP QMVETIHRWA QYWR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024