1433I_PLAF7
ID 1433I_PLAF7 Reviewed; 262 AA.
AC C0H4V6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=14-3-3 protein I {ECO:0000305};
DE AltName: Full=Pf14-3-3I {ECO:0000303|PubMed:23308157};
GN Name=14-3-3I {ECO:0000303|PubMed:23308157};
GN ORFNames=PF3D7_0818200 {ECO:0000312|EMBL:CAX64133.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH H3, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=23308157; DOI=10.1371/journal.pone.0053179;
RA Dastidar E.G., Dzeyk K., Krijgsveld J., Malmquist N.A., Doerig C.,
RA Scherf A., Lopez-Rubio J.J.;
RT "Comprehensive histone phosphorylation analysis and identification of Pf14-
RT 3-3 protein as a histone H3 phosphorylation reader in malaria parasites.";
RL PLoS ONE 8:e53179-e53179(2013).
RN [4] {ECO:0000305}
RP FUNCTION, SUBUNIT, INTERACTION WITH CDPK1, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=32484216; DOI=10.1042/bcj20200145;
RA Jain R., Dey P., Gupta S., Pati S., Bhattacherjee A., Munde M., Singh S.;
RT "Molecular dynamics simulations and biochemical characterization of Pf14-3-
RT 3 and PfCDPK1 interaction towards its role in growth of human malaria
RT parasite.";
RL Biochem. J. 477:2153-2177(2020).
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH PKAR AND CDPK1, INTERACTION WITH
RP CDPK1 AND 14-3-3I, DEVELOPMENTAL STAGE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=32817103; DOI=10.1128/mbio.01287-20;
RA More K.R., Kaur I., Giai Gianetto Q., Invergo B.M., Chaze T., Jain R.,
RA Huon C., Gutenbrunner P., Weisser H., Matondo M., Choudhary J.S.,
RA Langsley G., Singh S., Chitnis C.E.;
RT "Phosphorylation-Dependent Assembly of a 14-3-3 Mediated Signaling Complex
RT during Red Blood Cell Invasion by Plasmodium falciparum Merozoites.";
RL MBio 11:0-0(2020).
CC -!- FUNCTION: Adapter protein which binds to its partners, usually via a
CC phosphoserine or phosphothreonine motif (PubMed:23308157,
CC PubMed:32484216, PubMed:32817103). Binding generally results in the
CC modulation of the activity and/or cellular localization of the binding
CC partner (Probable). Via its interaction with CDPK1 and PKAr, involved
CC in merozoite microneme secretion and thus in merozoite invasion of host
CC erythrocytes (PubMed:32817103). {ECO:0000269|PubMed:23308157,
CC ECO:0000269|PubMed:32484216, ECO:0000269|PubMed:32817103,
CC ECO:0000305|PubMed:32817103}.
CC -!- SUBUNIT: Homodimer (Probable). Forms a complex composed of CDPK1, PKA
CC regulatory subunit PKAr and 14-3-3I; the complex is formed in
CC merozoites in response to low extracellular level of K(+) and may play
CC a role in microneme secretion (PubMed:32817103). Interacts with CDPK1
CC (when phosphorylated) in a Ca(2+)-independent manner; the interaction
CC does not regulate CDPK1 catalytic activity but is required for
CC merozoite invasion of host erythrocytes (PubMed:32484216,
CC PubMed:32817103). Interacts with PKA regulatory subunit PKAr (when
CC phosphorylated) in a Ca(2+)-dependent manner (PubMed:32817103).
CC Interacts with histone H3 (when phosphorylated at 'Ser-28' or when
CC phosphorylated at 'Ser-28' and 'Ser-32') (PubMed:23308157).
CC {ECO:0000269|PubMed:23308157, ECO:0000269|PubMed:32484216,
CC ECO:0000269|PubMed:32817103, ECO:0000305|PubMed:32484216}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32484216};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000269|PubMed:32484216}. Cytoplasm {ECO:0000269|PubMed:23308157,
CC ECO:0000269|PubMed:32484216}. Nucleus {ECO:0000269|PubMed:23308157}.
CC -!- DEVELOPMENTAL STAGE: Expressed during parasite asexual blood stages, at
CC the ring, trophozoite and schizont stages and in free merozoites (at
CC protein level). {ECO:0000269|PubMed:23308157,
CC ECO:0000269|PubMed:32484216, ECO:0000269|PubMed:32817103}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
CC {ECO:0000255|RuleBase:RU003466}.
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DR EMBL; AL844507; CAX64133.1; -; Genomic_DNA.
DR RefSeq; XP_002808856.1; XM_002808810.1.
DR AlphaFoldDB; C0H4V6; -.
DR SMR; C0H4V6; -.
DR IntAct; C0H4V6; 1.
DR STRING; 5833.MAL8P1.69; -.
DR DrugBank; DB11638; Artenimol.
DR TCDB; 8.A.98.1.3; the 14-3-3 protein (14-3-3) family.
DR PRIDE; C0H4V6; -.
DR EnsemblProtists; CAX64133; CAX64133; PF3D7_0818200.
DR GeneID; 2655418; -.
DR KEGG; pfa:PF3D7_0818200; -.
DR VEuPathDB; PlasmoDB:PF3D7_0818200; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; C0H4V6; -.
DR OMA; IPCATTG; -.
DR PhylomeDB; C0H4V6; -.
DR Proteomes; UP000001450; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:GeneDB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:GeneDB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Nucleus; Reference proteome.
FT CHAIN 1..262
FT /note="14-3-3 protein I"
FT /id="PRO_0000453004"
SQ SEQUENCE 262 AA; 30193 MW; 78CF3EE38425D91A CRC64;
MATSEELKQL RCDCTYRSKL AEQAERYDEM ADAMRTLVEQ CVNNDKDELT VEERNLLSVA
YKNAVGARRA SWRIISSVEQ KEMSKANVHN KNVAATYRKK VEEELNNICQ DILNLLTKKL
IPNTSESESK VFYYKMKGDY YRYISEFSCD EGKKEASNCA QEAYQKATDI AENELPSTHP
IRLGLALNYS VFFYEILNQP HQACEMAKRA FDDAITEFDN VSEDSYKDST LIMQLLRDNL
TLWTSDLQGD QTEEKSKDEG LE
