P4548_PLABA
ID P4548_PLABA Reviewed; 455 AA.
AC Q4YSU6;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Gametocyte surface protein P45/48;
DE Flags: Precursor;
GN Name=PB45/48; ORFNames=PB001525.02.0, PBANKA_1359600;
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA;
RX PubMed=15637271; DOI=10.1126/science.1103717;
RA Hall N., Karras M., Raine J.D., Carlton J.M., Kooij T.W.A., Berriman M.,
RA Florens L., Janssen C.S., Pain A., Christophides G.K., James K.,
RA Rutherford K., Harris B., Harris D., Churcher C.M., Quail M.A., Ormond D.,
RA Doggett J., Trueman H.E., Mendoza J., Bidwell S.L., Rajandream M.A.,
RA Carucci D.J., Yates J.R. III, Kafatos F.C., Janse C.J., Barrell B.G.,
RA Turner C.M.R., Waters A.P., Sinden R.S.;
RT "A comprehensive survey of the Plasmodium life cycle by genomic,
RT transcriptomic, and proteomic analyses.";
RL Science 307:82-86(2005).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=ANKA;
RX PubMed=11163248; DOI=10.1016/s0092-8674(01)00199-4;
RA van Dijk M.R., Janse C.J., Thompson J., Waters A.P., Braks J.A.,
RA Dodemont H.J., Stunnenberg H.G., van Gemert G.J., Sauerwein R.W., Eling W.;
RT "A central role for P48/45 in malaria parasite male gamete fertility.";
RL Cell 104:153-164(2001).
RN [3]
RP FUNCTION.
RC STRAIN=ANKA;
RX PubMed=20386715; DOI=10.1371/journal.ppat.1000853;
RA van Dijk M.R., van Schaijk B.C., Khan S.M., van Dooren M.W., Ramesar J.,
RA Kaczanowski S., van Gemert G.J., Kroeze H., Stunnenberg H.G., Eling W.M.,
RA Sauerwein R.W., Waters A.P., Janse C.J.;
RT "Three members of the 6-cys protein family of Plasmodium play a role in
RT gamete fertility.";
RL PLoS Pathog. 6:E1000853-E1000853(2010).
CC -!- FUNCTION: Gametocyte surface protein required for male fertility.
CC {ECO:0000269|PubMed:11163248, ECO:0000269|PubMed:20386715}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with PF230.
CC {ECO:0000250|UniProtKB:Q8I6T1}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:11163248}. Cell
CC membrane {ECO:0000269|PubMed:11163248}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:11163248}. Note=Present on the surface of male and
CC female gametocytes. {ECO:0000269|PubMed:11163248}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in sporogonic
CC (macrogametes) stages of parasites. {ECO:0000269|PubMed:11163248}.
CC -!- DISRUPTION PHENOTYPE: Male gametes fail to attach at fertile female
CC gametes. {ECO:0000269|PubMed:11163248}.
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; CAAI01002547; CAH98911.1; -; Genomic_DNA.
DR RefSeq; XP_679694.1; XM_674602.1.
DR AlphaFoldDB; Q4YSU6; -.
DR STRING; 5821.PBANKA_135960; -.
DR VEuPathDB; PlasmoDB:PBANKA_1359600; -.
DR eggNOG; ENOG502QX5B; Eukaryota.
DR HOGENOM; CLU_611777_0_0_1; -.
DR InParanoid; Q4YSU6; -.
DR OMA; VLKYPHK; -.
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; 2.
DR SMART; SM00970; s48_45; 2.
DR PROSITE; PS51701; 6_CYS; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Malaria; Membrane; Repeat; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..433
FT /note="Gametocyte surface protein P45/48"
FT /id="PRO_0000423562"
FT PROPEP 434..455
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423563"
FT DOMAIN 48..186
FT /note="6-Cys 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 302..433
FT /note="6-Cys 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT LIPID 433
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 106..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 306..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 351..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 359..417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
SQ SEQUENCE 455 AA; 52907 MW; 66BFD1D1B53CFC16 CRC64;
MLYFFGNSRF FLFFFYFFFY FVLVIKSSVG KNEYVSPDEL NIKTSGFLGY KCDFSTEGIH
NLEPDIVERR SVICSINSYF IYDKIKLIIP KQDDPKSKFK LLPENCFAKV YSDIEGKTEI
PIEQTGLIEY TLEENDTNQD YSERIIQISP FNNKDIEFYC ICDNTEQVIS HIDGRSALVH
VTVLKYPHKI VSVNLTDQKY PYLFDAYNKN DFINYKLEIG LKEGELLVLA CKQIDNKCFQ
KNDESKNGDL YKTNKIIYHK DFAIFKAPIY VKSNNATAEC KCKIDEANIY TLVVKPDYDE
KVIYGCNFSK DLSFRTFTNN MNLLKYNENT NINCNVEISQ PFYDHLIGIS CPGTIIPDCF
FQIYKPLTNE LKSSEITYLD SQLNIGNIEY YEDIHGNNEI RIFSIVGAIP QSASFTCMCK
MDKITGFMNI KIGSAYYAFL SKLFIIFIPL FFMWL