PLP1_PLAFO
ID PLP1_PLAFO Reviewed; 679 AA.
AC W7K139;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Patatin-like phospholipase 1 {ECO:0000305};
DE EC=3.1.1.4 {ECO:0000269|PubMed:31413195};
DE AltName: Full=PfPATPL1 {ECO:0000303|PubMed:31413195};
GN Name=PATPL1 {ECO:0000303|PubMed:31413195};
GN Synonyms=PNPLA1 {ECO:0000303|PubMed:31734953};
GN ORFNames=CK202_3157 {ECO:0000312|EMBL:PKC46375.1},
GN PFNF54_00248 {ECO:0000312|EMBL:EWC91003.1};
OS Plasmodium falciparum (isolate NF54).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5843 {ECO:0000312|Proteomes:UP000030673};
RN [1] {ECO:0000312|Proteomes:UP000030673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000312|Proteomes:UP000030673};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum NF54.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000232684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000312|EMBL:PKC46375.1};
RA Bryant J.M., Baumgarten S., Scheidig-Benatar C., Scherf A.;
RT "Plasmodium falciparum NF54 genome assembly.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=31413195; DOI=10.1073/pnas.1900266116;
RA Singh P., Alaganan A., More K.R., Lorthiois A., Thiberge S., Gorgette O.,
RA Guillotte Blisnick M., Guglielmini J., Aguilera S.S., Touqui L., Singh S.,
RA Chitnis C.E.;
RT "Role of a patatin-like phospholipase in Plasmodium falciparum
RT gametogenesis and malaria transmission.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:17498-17508(2019).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=31734953; DOI=10.1111/cmi.13146;
RA Flammersfeld A., Panyot A., Yamaryo-Botte Y., Aurass P., Przyborski J.M.,
RA Flieger A., Botte C., Pradel G.;
RT "A patatin-like phospholipase functions during gametocyte induction in the
RT malaria parasite Plasmodium falciparum.";
RL Cell. Microbiol. 22:e13146-e13146(2020).
CC -!- FUNCTION: Hydrolyzes the ester bond of the fatty acyl group attached at
CC the sn-2 position of phospholipids such as phosphatidylcholine
CC (PubMed:31413195). Involved in gametogenesis; however, it is not clear
CC whether it is involved in gametocytes development in host erythrocytes
CC or in gametocyte activation in the mosquito midgut (PubMed:31413195,
CC PubMed:31734953). Involved in gametocyte development in host
CC erythrocytes; however, not involved in gametocytes activation including
CC male gamete exflagellation (PubMed:31734953). Involved in the rounding
CC up of gametocytes following activation in the mosquito midgut; however,
CC not required for gametocyte development in host erythrocytes
CC (PubMed:31413195). Required for exflagellation of activated male
CC gametocytes (PubMed:31413195). Involved in gametocytes egress from host
CC erythrocytes by promoting the relocalization of perforin-like protein
CC PLP2-containing vesicles to the periphery of gametocytes; PLP2
CC secretion is required for permeabilization of the erythrocyte membrane
CC and thus, promotes gametocyte egress (PubMed:31413195). Dispensable for
CC asexual blood stage development (PubMed:31413195).
CC {ECO:0000269|PubMed:31413195, ECO:0000269|PubMed:31734953}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:31413195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:31413195};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31413195,
CC ECO:0000269|PubMed:31734953}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage,
CC including in rings, trophozoites and schizonts (at protein level)
CC (PubMed:31413195, PubMed:31734953). Expressed in male and female
CC gametocytes from stage II to stage V (at protein level)
CC (PubMed:31413195, PubMed:31734953). {ECO:0000269|PubMed:31413195,
CC ECO:0000269|PubMed:31734953}.
CC -!- DISRUPTION PHENOTYPE: Gametocyte maturation is delayed
CC (PubMed:31734953). No defect in exflagellation of male gametes,
CC formation of macrogametes and zygotes following gametocyte activation
CC (PubMed:31734953). At the ring stage, levels of phosphatidylcholine are
CC increased (PubMed:31734953). Dispensable for asexual blood stage growth
CC (PubMed:31734953). {ECO:0000269|PubMed:31734953}.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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; KE123721; EWC91003.1; -; Genomic_DNA.
DR EMBL; NYMT01000009; PKC46375.1; -; Genomic_DNA.
DR SMR; W7K139; -.
DR PRIDE; W7K139; -.
DR EnsemblProtists; EWC91003; EWC91003; PFNF54_00248.
DR VEuPathDB; PlasmoDB:PfNF54_020013900; -.
DR OMA; ANETHRE; -.
DR Proteomes; UP000030673; Unassembled WGS sequence.
DR Proteomes; UP000232684; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0007276; P:gamete generation; IMP:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..679
FT /note="Patatin-like phospholipase 1"
FT /id="PRO_0000453176"
FT DOMAIN 338..544
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 19..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 381..385
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 531..533
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 383
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 531
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 679 AA; 78305 MW; F53B3DD6C73A32E5 CRC64;
MSDDDDKIYI YSDLFSKNFS DDEKDDSYER EKQVYSGSET QNAENEYSKL RAQNSTILNN
YFDNDNIKNV ENLKSNDPDQ IDLILFPVNK NYYMNLFDGQ LIENIHSIKL RKAGFYAIYV
ENNNNSKWDG IYFGLSRMQV ELDYKLITKK NKDGGEYEKR NTSSYDNTES VQNTVGSEKE
ETENKNEETS NYNSNLNNEI NKICKYNLDQ TDILLDDSNS ERRRNSKFKI KNTNYYDNLM
LQNKYTNSIL YDDDDDKNNT ETYTCTFKTE DQIRVPSQKK KYIYLYNKYD NATLDLNVHT
YMSLGMSILC KYSLLYCGKY NHIPRDPYTP FKKPVSILSL DGGGILTIST LLVLNRLEAE
LRKEIGSDDI KLIDCFDMVC GTSAGGLISL ALLREIDLQD VSNMWPSTIK KVFEGNRNII
SGIFFEGYDV NNVKDVFLER MGNKFMSSYK KFYCFVTATD VKHKPYKLFL IRNYTHKYNS
INAESYDGIN KVPLWLAAWA TASAPTYLKG PSAEDIKKLG INIKPEIHLV DGALKASNPA
LIALEECARL NNKNLSTFIK EDLDTLVSIG TGQVPTKLTQ SGASSKSAST FEILINSTHL
LTRANDTHRE VLQRLADREN TYFRFNVPHI GDIEIDSQDV RDFDLISKAT QDYLFDEKFY
EIKRLAHKLA NNYIRSKYL
