ID   P230P_PLAFO             Reviewed;        2508 AA.
AC   W7K265;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Male gametocyte surface protein P230p {ECO:0000305};
DE   Flags: Precursor;
GN   Name=P230p {ECO:0000303|PubMed:30297725};
GN   ORFNames=CK202_3183 {ECO:0000312|EMBL:PKC46394.1},
GN   PFNF54_00246 {ECO:0000312|EMBL:EWC91001.1};
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:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=30297725; DOI=10.1038/s41598-018-33236-x;
RA   Marin-Mogollon C., van de Vegte-Bolmer M., van Gemert G.J., van Pul F.J.A.,
RA   Ramesar J., Othman A.S., Kroeze H., Miao J., Cui L., Williamson K.C.,
RA   Sauerwein R.W., Janse C.J., Khan S.M.;
RT   "The Plasmodium falciparum male gametocyte protein P230p, a paralog of
RT   P230, is vital for ookinete formation and mosquito transmission.";
RL   Sci. Rep. 8:14902-14902(2018).
CC   -!- FUNCTION: Plays an essential role in male gamete fertility
CC       (PubMed:30297725). Required for the binding to erythrocytes and thus,
CC       for the formation of exflagellation centers (PubMed:30297725).
CC       {ECO:0000269|PubMed:30297725}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:O96175}. Cell
CC       membrane {ECO:0000269|PubMed:30297725}; Peripheral membrane protein
CC       {ECO:0000305}. Note=Present on the surface of male gametocytes.
CC       {ECO:0000269|PubMed:30297725}.
CC   -!- DEVELOPMENTAL STAGE: Specifically present on the surface of stage V
CC       male gametocytes (at protein level). {ECO:0000269|PubMed:30297725}.
CC   -!- DISRUPTION PHENOTYPE: Normal numbers of exflagellating male gametocytes
CC       (PubMed:30297725). However, male gamete attachment to uninfected
CC       erythrocytes is impaired resulting in a failure to form exflagellation
CC       centers and a subsequent reduced ookinete formation (PubMed:30297725).
CC       {ECO:0000269|PubMed:30297725}.
CC   -!- MISCELLANEOUS: In P.berghei, dispensable male gamete attachment to
CC       erythrocytes and the formation of exflagellation centers.
CC       {ECO:0000269|PubMed:30297725}.
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; EWC91001.1; -; Genomic_DNA.
DR   EMBL; NYMT01000009; PKC46394.1; -; Genomic_DNA.
DR   SMR; W7K265; -.
DR   PRIDE; W7K265; -.
DR   EnsemblProtists; EWC91001; EWC91001; PFNF54_00246.
DR   VEuPathDB; PlasmoDB:PfNF54_020013700; -.
DR   OMA; FYCTCED; -.
DR   Proteomes; UP000030673; Unassembled WGS sequence.
DR   Proteomes; UP000232684; Unassembled WGS sequence.
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; -; 6.
DR   InterPro; IPR010884; 6_CYS_dom.
DR   InterPro; IPR038160; 6_CYS_dom_sf.
DR   Pfam; PF07422; s48_45; 6.
DR   SMART; SM00970; s48_45; 6.
DR   PROSITE; PS51701; 6_CYS; 10.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Membrane; Reference proteome;
KW   Repeat; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..2508
FT                   /note="Male gametocyte surface protein P230p"
FT                   /id="PRO_0000455040"
FT   DOMAIN          394..516
FT                   /note="6-Cys 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DOMAIN          676..800
FT                   /note="6-Cys 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DOMAIN          831..1096
FT                   /note="6-Cys 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DOMAIN          1099..1231
FT                   /note="6-Cys 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DOMAIN          1268..1428
FT                   /note="6-Cys 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DOMAIN          1433..1565
FT                   /note="6-Cys 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DOMAIN          1656..1804
FT                   /note="6-Cys 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DOMAIN          1807..1984
FT                   /note="6-Cys 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DOMAIN          2197..2354
FT                   /note="6-Cys 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DOMAIN          2357..2481
FT                   /note="6-Cys 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   REGION          2081..2113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2085..2110
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        601
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        674
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        703
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        779
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        849
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        986
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        995
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1065
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1074
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1525
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1550
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1567
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1750
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1755
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1788
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2016
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2047
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        292..367
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        443..493
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        680..700
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        714..775
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        725..773
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        835..856
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        871..1072
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1103..1129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1144..1206
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1157..1204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1272..1293
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1308..1404
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1437..1464
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1478..1547
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1488..1545
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1704..1782
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1811..1883
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1897..1966
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        1908..1964
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        2361..2386
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        2400..2461
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT   DISULFID        2411..2459
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
SQ   SEQUENCE   2508 AA;  293647 MW;  628E126648E40F1C CRC64;
     MFIYLFIYLF FKMDKKRTFY YLFFFFTFLV YVLYFDNIKS VLRSSTKKKK KKKICKSTFY
     VHEESEEIKS WLRNSNERDK GKKFFIFERL IKERKYICVN KYKRNNKLKW IYKNTYEKTK
     NICDDYNILF KCIKGIIYDK NKETFFETFF ENFWDNIFYM NKYIFNIYYY MFDYTKKVKK
     KIEGIKENMN IRHNNNYNNI FYVHKFFLFN DDEEKKKRND DIKINIKLHN NTRKLSVSEE
     NVELKPYIKQ GERNETVVNL YEYFTGGVKR SNNNNEIVVT STEQFHRIVI ICFKPTVKHS
     HIITSPHDAL NHIVEENDKI KLSEEIYSIP FYPIYGNLGL KNVITTGIVE FMIPYFSRTQ
     MNFTVTCANG EMNDLYKFED LIKIRIRIPR NTKKILGLST NEKDKTVFER IVDNTSNEYR
     FKSYNNKIVG IKLENSILDP PGCFKTVYED DKILQLEVFL QYVKCINLDR DNYKIRFFFL
     PEDFGDEEIE FSCKFTYKKK TSKIIFGLGE TSVDKDIFYL EDEHVKLNIN QDISGDEPYY
     SHLNYNGIPY NICNFQYKSE YDSQVCERTI HEFSLFIYNC DTLVGTQIQT TEPITSVKYL
     NSTYPINKFS DITLLSKDID IEGLEEAFRN SKFFLTSYIN HGPFPLIIEC VISNSNKDYQ
     NVYILLHLRT SIKNRSVSFC DFEKVQGYNY LNNYIDGKIC NINITSNSVF GFRCPSNSIK
     EPKDCFSQVY IDKKVYKLND KLSNKLILYS MKQENLAIAG FNNYISNSFS FECYCIDKNQ
     TYSSYERTSG EDIFNHIVKR IHVHYKNYDE LYDYNIHDKI TYEPIMKNPP ITYLCDFLNK
     KQILQPLNNK TKNYICTIWY PKPLNYIALN CPTNRRDEQN DQTISEVYNS LQKDLLKPTG
     IEQQIDQKKK ELNLLFNKRN IYSNLYHLPK NAPKRTINKN GLNIVNIDEI IPGILIKDVI
     NMKLEDVIKP DLLTPTSFLH KTYNTNKSYL FSTRNKSTSV FNTPSIYTPL THTSFSISPK
     SVPLTKSRIE ETHSSSNTYE QYIGKRNSIE NGFFIFQLPP YLKKNQTIEF ACINDSTIKN
     KNVGNNGIMT IHLKSFGNPI EGCYFYKNSA KYNYLKKSIK IDDLKKEECT IRSDGEIEFV
     GIMCPYENNL YLTPSSCFLK TYDNTDNLVE LLDINENFEY YSNDKGISYL KIPQEFLNHV
     HLFCYCNVDK DSVSDTNVLV KKENKISLEL NYSNKGFNII KTIDYQYEAD ILIGYSYYFK
     RVTPIYRKKH ICDFTTEDNS LEPESEDKMI YSCYLSLENN LNFIEVKCPK NKKSSNSEWL
     FKYGTFDKSS EIMEDDENIK KYEHMKYMPE DKDEIIYLFK KQKLEDILPG VIIFDKNRYF
     FEKGNFSFVT PLIVKEDVTI KLLCDNSETK IDDKIGKKGI ILIKIPQHIT DKKFYGCDFS
     GDSNKKSSFY YTSVYDLKTQ NQYCEVKLKE NIIISLNCPN GNINPNNCFN NVFLKTNMNE
     QIHEKIQNIF DQVKVINTKS HVLLNSSSTF LIISKITKKE LNFFCTCHHN ETKNVGTIYI
     KNEDIINFSK AYNKESSILQ YIDVTPYYLK DTYICDFTQN HYSISFDTSV NVQNVLERYL
     KILSDLYNTH EEFTYFSIHL KLKKEIMKKK YIDYLKKKIN EYKEKETSDK IKRVTLSTND
     NINTILVYRC NIDLGSFDKF KIKCPSKLNE EEVENNKLYP NLIYSSNLGL DETDMLNGLT
     KLLYGSVLIN KTEKNVSFFE KGELELIISP YTDSSKNIIF SCENVPRNLS KGIIGSASIF
     IKKNDNKILG CDFIDTPSTL SSASTLESSY GSHASSPLSS SHHVLHNDNQ GHDVHMINHI
     DISNKKNSFE FEIELIEGKN TYCNIEAIEN DIVGFSCPYN FLTTPSDCFE SIQIEGVDKE
     LETHKLEKLL KGVKILNNDI YKYNFTPSYI ILPKKIKKSL KIFCRCNSVK LIKTGIIQIN
     IVGDDLNNWF KKEITHNIFA YQKMDYFYDF SKGPTNISSE NVLGISTMSL MSSNKKVSRK
     KNHKEENRTQ QNVYKEIEND HKNINENVNK YDNLPVTLLS SDEGDGYQAD EDIGGEDDAE
     DVDGEGDDED DNILNPLRTK QVYDIIVAAS EFSKIEVVCP LRNSSQFRQS KISPENFFEY
     VYVLEDKNDD KRKRSIEENE KLVKAILEGK KNIDGHIINI EDINNKKSSK NASVEYDDMG
     NKIFISIISE KPKAVIGDNI SSSRSSVHIS NNIMNSSFQS NIHPDPITSD TTTSEYEQYN
     SYFKDILVIK NINEVISFAN IKIDINEQTY SSSLHIPPLI LKDAEFLISC DNSLTLNENT
     RGKTATVKIK VKSNFLKIYG CDFVGEFSTH FLFSKKWDDI PKNYICKINI QDDMLIGLAC
     PSFTKLHPPD CFENIIVNQN VYKKNIIMET KNMFFYKQND KPILSFVHVK KILVETFLCK
     CYQVTKADYK EVTIQILYEP YVMGTPKYTL EKSIIQYRYA NLKPPLHI