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CERI1_PLAF7
ID   CERI1_PLAF7             Reviewed;         446 AA.
AC   O96188;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Rhoptry surface protein CERLI1 {ECO:0000305};
DE   AltName: Full=Cytosolically exposed rhoptry leaflet interacting protein 1 {ECO:0000303|PubMed:32179747};
DE            Short=PfCERLI1 {ECO:0000303|PubMed:32179747};
DE   AltName: Full=Rhoptry apical surface protein 2 {ECO:0000303|PubMed:31492901};
DE            Short=PfRASP2 {ECO:0000303|PubMed:31492901};
GN   Name=CERLI1 {ECO:0000303|PubMed:32179747};
GN   Synonyms=RASP2 {ECO:0000303|PubMed:31492901};
GN   ORFNames=PF3D7_0210600 {ECO:0000312|EMBL:CZT98120.1};
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=9804551; DOI=10.1126/science.282.5391.1126;
RA   Gardner M.J., Tettelin H., Carucci D.J., Cummings L.M., Aravind L.,
RA   Koonin E.V., Shallom S.J., Mason T., Yu K., Fujii C., Pederson J., Shen K.,
RA   Jing J., Aston C., Lai Z., Schwartz D.C., Pertea M., Salzberg S.L.,
RA   Zhou L., Sutton G.G., Clayton R., White O., Smith H.O., Fraser C.M.,
RA   Adams M.D., Venter J.C., Hoffman S.L.;
RT   "Chromosome 2 sequence of the human malaria parasite Plasmodium
RT   falciparum.";
RL   Science 282:1126-1132(1998).
RN   [2] {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   [3] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=31492901; DOI=10.1038/s41467-019-11979-z;
RA   Suarez C., Lentini G., Ramaswamy R., Maynadier M., Aquilini E.,
RA   Berry-Sterkers L., Cipriano M., Chen A.L., Bradley P., Striepen B.,
RA   Boulanger M.J., Lebrun M.;
RT   "A lipid-binding protein mediates rhoptry discharge and invasion in
RT   Plasmodium falciparum and Toxoplasma gondii parasites.";
RL   Nat. Commun. 10:4041-4041(2019).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=32179747; DOI=10.1038/s41467-020-15127-w;
RA   Liffner B., Froelich S., Heinemann G.K., Liu B., Ralph S.A., Dixon M.W.A.,
RA   Gilberger T.W., Wilson D.W.;
RT   "PfCERLI1 is a conserved rhoptry associated protein essential for
RT   Plasmodium falciparum merozoite invasion of erythrocytes.";
RL   Nat. Commun. 11:1411-1411(2020).
CC   -!- FUNCTION: Essential for merozoite invasion of host cells by controlling
CC       rhoptry secretion (PubMed:31492901, PubMed:32179747). Binds to
CC       phosphatidic acid (PA) and phosphatidylinositol 4,5-bisphosphate (PIP2)
CC       lipids and thus, likely contributes to the assembly of the machinery
CC       that docks or primes the rhoptry to the parasite cell membrane prior to
CC       the fusion with the host cell membrane (PubMed:31492901).
CC       {ECO:0000269|PubMed:31492901, ECO:0000269|PubMed:32179747}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, rhoptry
CC       membrane {ECO:0000269|PubMed:31492901, ECO:0000269|PubMed:32179747};
CC       Peripheral membrane protein {ECO:0000269|PubMed:32179747}; Cytoplasmic
CC       side {ECO:0000269|PubMed:32179747}. Note=Localizes to the neck (apical
CC       part) of rhoptries in merozoites (PubMed:31492901). In the mature
CC       merozoite, localizes to the cytosolic face of the rhoptry bulb membrane
CC       (PubMed:32179747). {ECO:0000269|PubMed:31492901,
CC       ECO:0000269|PubMed:32179747}.
CC   -!- DEVELOPMENTAL STAGE: During parasite asexual blood stages, expressed at
CC       the late schizont stage and in free merozoites (at protein level).
CC       {ECO:0000269|PubMed:31492901, ECO:0000269|PubMed:32179747}.
CC   -!- DOMAIN: The C2 domain is a non-calcium binding domain (By similarity).
CC       Cooperates with the PH domain in the binding to phosphatidic acid (PA)
CC       and phosphatidylinositol 4,5-bisphosphate (PIP2) (By similarity).
CC       {ECO:0000250|UniProtKB:S7UMJ0}.
CC   -!- DOMAIN: The PH domain cooperates with the C2 domain in the binding to
CC       phosphatidic acid (PA) and phosphatidylinositol 4,5-bisphosphate
CC       (PIP2). {ECO:0000250|UniProtKB:S7UMJ0}.
CC   -!- DISRUPTION PHENOTYPE: Conditional knockout at the ring stage has no
CC       effect on parasite development during the first cycle and merozoites
CC       egress normally from host erythrocytes. However, these merozoites are
CC       unable to reinvade new erythrocytes (PubMed:31492901, PubMed:32179747).
CC       Impaired rhoptry secretion during merozoite invasion of host
CC       erythrocytes (PubMed:31492901, PubMed:32179747). Increases the spatial
CC       segregation between rhoptry neck protein RON4 and bulb protein RAP1,
CC       and impairs RAP1 processing (PubMed:32179747). No effect on rhoptry
CC       morphology (PubMed:31492901, PubMed:32179747). Microneme secretion is
CC       not affected (PubMed:31492901). {ECO:0000269|PubMed:31492901,
CC       ECO:0000269|PubMed:32179747}.
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DR   EMBL; LN999943; CZT98120.1; -; Genomic_DNA.
DR   RefSeq; XP_001349613.1; XM_001349577.1.
DR   AlphaFoldDB; O96188; -.
DR   STRING; 5833.PFB0475c; -.
DR   SwissPalm; O96188; -.
DR   PRIDE; O96188; -.
DR   EnsemblProtists; CZT98120; CZT98120; PF3D7_0210600.
DR   GeneID; 812695; -.
DR   KEGG; pfa:PF3D7_0210600; -.
DR   VEuPathDB; PlasmoDB:PF3D7_0210600; -.
DR   HOGENOM; CLU_614653_0_0_1; -.
DR   InParanoid; O96188; -.
DR   OMA; IHHINLK; -.
DR   PhylomeDB; O96188; -.
DR   Proteomes; UP000001450; Chromosome 2.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Membrane; Reference proteome.
FT   CHAIN           1..446
FT                   /note="Rhoptry surface protein CERLI1"
FT                   /id="PRO_0000456207"
FT   DOMAIN          39..208
FT                   /note="C2"
FT                   /evidence="ECO:0000250|UniProtKB:S7UMJ0"
FT   DOMAIN          252..363
FT                   /note="PH"
FT                   /evidence="ECO:0000250|UniProtKB:S7UMJ0"
SQ   SEQUENCE   446 AA;  53675 MW;  C67972E6A84F6572 CRC64;
     MFYLDTHNIL YLGSCLLASV CTLCICRNRE LFPHISENKP IGQLYRLMNI HKYESFSIII
     QIHHLNLKFG DDDNAKFIVH LKIGNRYAYT HYHKQYQNKV HIEERKNMVV KQNNNTLRLE
     VYKKGTLKNT FFGSAEIHIY SEIVKKLFPC NVYFNITNKN QIVGTACLSF HYINLDCIKK
     DDQIYTSLFI ETIISVQKNQ TKNNEKIEKL IDEGKEHFEA IKETDLSTTI YKNISNLVLE
     DKIRLFCKNL NGYLLHSNFY IKRFYNKYYF YLHFFKGKFY WCYYNEEADA KMDKNRVGYV
     RLEYVANVYS DVYSHKYFYI KYRKKNERKE NYLYLKTIDK DRNIWVNIIH DFIILVSNYK
     RERKNKKYKI KEFKDNLIED TPKEILEINK TLSRSLSNNS MKNKYLDKKK KVEVLSDMDN
     EENYMNSGDL GPVFKDMSKN MYNYSD
 
 
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