PF36P_PLAYO
ID PF36P_PLAYO Reviewed; 480 AA.
AC Q7K5V2;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Sporozoite surface protein P36p;
DE AltName: Full=Sporozoite surface protein P52;
DE Flags: Precursor;
GN Name=P52; Synonyms=P36P; ORFNames=PY01340;
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=17XNL;
RX PubMed=11738705; DOI=10.1016/s0166-6851(01)00377-2;
RA Thompson J., Janse C.J., Waters A.P.;
RT "Comparative genomics in Plasmodium: a tool for the identification of genes
RT and functional analysis.";
RL Mol. Biochem. Parasitol. 118:147-154(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17XNL;
RX PubMed=12368865; DOI=10.1038/nature01099;
RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D.,
RA Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W.,
RA Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA Carucci D.J.;
RT "Genome sequence and comparative analysis of the model rodent malaria
RT parasite Plasmodium yoelii yoelii.";
RL Nature 419:512-519(2002).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17517871; DOI=10.1128/iai.00225-07;
RA Labaied M., Harupa A., Dumpit R.F., Coppens I., Mikolajczak S.A.,
RA Kappe S.H.;
RT "Plasmodium yoelii sporozoites with simultaneous deletion of P52 and P36
RT are completely attenuated and confer sterile immunity against infection.";
RL Infect. Immun. 75:3758-3768(2007).
CC -!- FUNCTION: Involved in sporozoite infection of hepatocytes and
CC replication therein. {ECO:0000305|PubMed:17517871}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Present on
CC the surface of sporozoites. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking both P36 and P52/P36P show
CC attenuated infection and do not form a parasitophorous vacuole within
CC hepatocytes. {ECO:0000269|PubMed:17517871}.
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; AY034178; AAK56487.1; -; Genomic_DNA.
DR EMBL; AABL01000353; EAA20643.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7K5V2; -.
DR SMR; Q7K5V2; -.
DR DIP; DIP-61877N; -.
DR STRING; 73239.Q7K5V2; -.
DR EnsemblProtists; EAA20643; EAA20643; EAA20643.
DR InParanoid; Q7K5V2; -.
DR OMA; CVIHAYP; -.
DR Proteomes; UP000008553; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.2860; -; 2.
DR InterPro; IPR010884; 6_CYS_dom.
DR InterPro; IPR038160; 6_CYS_dom_sf.
DR Pfam; PF07422; s48_45; 1.
DR SMART; SM00970; s48_45; 1.
DR PROSITE; PS51701; 6_CYS; 2.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Malaria; Membrane; Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..457
FT /note="Sporozoite surface protein P36p"
FT /id="PRO_0000423577"
FT PROPEP 458..480
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423578"
FT DOMAIN 23..156
FT /note="6-Cys 1"
FT DOMAIN 159..298
FT /note="6-Cys 2"
FT REGION 358..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 457
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..49
FT /evidence="ECO:0000250"
FT DISULFID 63..137
FT /evidence="ECO:0000250"
FT DISULFID 80..135
FT /evidence="ECO:0000250"
FT DISULFID 163..187
FT /evidence="ECO:0000250"
FT DISULFID 201..280
FT /evidence="ECO:0000250"
FT DISULFID 221..278
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 55658 MW; B7F2A5F186BDF490 CRC64;
MKRRSIFMYY CFCFLLKYVA FSNVPNPNTT IGHFEICEVN TSSGDAEECV LENEFGKMFL
FICDIDYNEM SKNIVLPSEC AKKTYIDHVN PNGTSPEVNT YDIFPDLIAA NESQFRDKFY
FYGTPYSSKD IDFICLCFSE TKPDIKHVMK MSFKKMTKKI KGCDFGDNIP TKKDLTNGKA
LYENSSCHIY AYPGDVIGIN CYKKDINNIY NNNLELQPNN CFHNVYYEDD ILLSSKNLIP
NSRVIPDPSN DVKLSKMHSY MSYIILPDEI NENVKISCAC KRDEYIGTMF LYVNTSKNIL
TSPDNNVEEI APLNDHYISI GDMWDMGLHE NPEQIQGIIS NHANKKYYEH MKIYKSNKMD
SSDDDESNET ESSENESNER THNGNRANKD ANNSEKMTGN RRKKNNSINN TNYYSNYEDD
NGINISTHDK YYEDQHFGNN GPLRKKRTFW QNMFGTSSSY YEVFNYFSIA FILIIHMLLL
