(data stored in SCRATCH zone)

SWISSPROT: Q8IAR3_PLAF7

ID   Q8IAR3_PLAF7            Unreviewed;       260 AA.
AC   Q8IAR3;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 2.
DT   11-DEC-2019, entry version 117.
DE   RecName: Full=Proteasome endopeptidase complex {ECO:0000256|PROSITE-ProRule:PRU00808};
DE            EC=3.4.25.1 {ECO:0000256|PROSITE-ProRule:PRU00808};
GN   ORFNames=PF3D7_0807500 {ECO:0000313|EMBL:CAD51297.2};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CAD51297.2, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|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:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|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:0000213|PDB:5FMG}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS).
RX   PubMed=26863983; DOI=10.1038/NATURE16936;
RA   Li H., O'Donoghue A.J., van der Linden W.A., Xie S.C., Yoo E., Foe I.T.,
RA   Tilley L., Craik C.S., da Fonseca P.C., Bogyo M.;
RT   "Structure- and function-based design of Plasmodium-selective proteasome
RT   inhibitors.";
RL   Nature 530:233-236(2016).
RN   [4] {ECO:0000213|PDB:6MUV, ECO:0000213|PDB:6MUW, ECO:0000213|PDB:6MUX}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS).
RX   PubMed=31384003; DOI=10.1038/s41564-019-0524-4;
RA   Xie S.C., Metcalfe R.D., Hanssen E., Yang T., Gillett D.L., Leis A.P.,
RA   Morton C.J., Kuiper M.J., Parker M.W., Spillman N.J., Wong W., Tsu C.,
RA   Dick L.R., Griffin M.D.W., Tilley L.;
RT   "The structure of the PA28-20S proteasome complex from Plasmodium
RT   falciparum and implications for proteostasis.";
RL   Nat. Microbiol. 0:0-0(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1; Evidence={ECO:0000256|PROSITE-ProRule:PRU00808};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00594407}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; AL844507; CAD51297.2; -; Genomic_DNA.
DR   RefSeq; XP_001349448.2; XM_001349412.2.
DR   PDB; 5FMG; EM; 3.60 A; A/O=1-260.
DR   PDB; 6MUV; EM; 3.80 A; A/O=1-260.
DR   PDB; 6MUW; EM; 3.60 A; A/O=1-260.
DR   PDB; 6MUX; EM; 3.90 A; A/O=1-260.
DR   PDBsum; 5FMG; -.
DR   PDBsum; 6MUV; -.
DR   PDBsum; 6MUW; -.
DR   PDBsum; 6MUX; -.
DR   SMR; Q8IAR3; -.
DR   DIP; DIP-43027N; -.
DR   IntAct; Q8IAR3; 2.
DR   PRIDE; Q8IAR3; -.
DR   EnsemblProtists; CAD51297; CAD51297; PF3D7_0807500.
DR   GeneDB; PF3D7_0807500.1:pep; -.
DR   GeneID; 2655251; -.
DR   KEGG; pfa:PF3D7_0807500; -.
DR   EuPathDB; PlasmoDB:PF3D7_0807500; -.
DR   HOGENOM; HOG000091084; -.
DR   InParanoid; Q8IAR3; -.
DR   KO; K02730; -.
DR   OMA; YGYDMPV; -.
DR   PhylomeDB; Q8IAR3; -.
DR   Reactome; R-PFA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-PFA-382556; ABC-family proteins mediated transport.
DR   Reactome; R-PFA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-PFA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-PFA-5689603; UCH proteinases.
DR   Reactome; R-PFA-5689880; Ub-specific processing proteases.
DR   Reactome; R-PFA-68949; Orc1 removal from chromatin.
DR   Reactome; R-PFA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-PFA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Proteomes; UP000001450; Chromosome 8.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005839; C:proteasome core complex; ISS:GeneDB.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; ISS:GeneDB.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:GeneDB.
DR   CDD; cd03754; proteasome_alpha_type_6; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR034642; Proteasome_subunit_alpha6.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q8IAR3.
DR   SWISS-2DPAGE; Q8IAR3.
KW   3D-structure {ECO:0000213|PDB:5FMG, ECO:0000213|PDB:6MUV,
KW   ECO:0000213|PDB:6MUW, ECO:0000213|PDB:6MUX};
KW   Cytoplasm {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000313|EMBL:CAD51297.2}; Nucleus {ECO:0000256|SAAS:SAAS00136223};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Proteasome {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000313|EMBL:CAD51297.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Threonine protease {ECO:0000256|PROSITE-ProRule:PRU00808}.
FT   DOMAIN          9..31
FT                   /note="PROTEASOME_ALPHA_1"
FT                   /evidence="ECO:0000259|SMART:SM00948"
SQ   SEQUENCE   260 AA;  29500 MW;  7236D13D35BCBC14 CRC64;
     MVRPSQSMYD RHLTIFSPDG NLYQIEYAIK AVKNTNITSV GVKGENCAVI ISQKKMATQY
     ISQDKLLDYN NITNIYNITD EIGCSMVGMP GDCLSMVYKA RSEASEFLYS NGYNVNAETL
     CRNICDKIQV YTQHAYMRLH ACSGMIIGID ENNKPELFKF DPSGFCAGYR ACVIGNKEQE
     SISVLERLLE KRKKKIQQET IDEDIRNTTI LAIEALQTIL AFDLKASEIE VAIVSTKNRN
     FTQISEKEID NYLTYIAERD
//

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