P113_PLAF7
ID P113_PLAF7 Reviewed; 969 AA.
AC Q8ILP3;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Surface protein P113 {ECO:0000312|EMBL:CZT99914.1};
DE Flags: Precursor;
GN Name=P113 {ECO:0000303|PubMed:28186186};
GN ORFNames=PF3D7_1420700 {ECO:0000312|EMBL:CZT99914.1};
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=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 [2] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=16203726; DOI=10.1074/jbc.m509631200;
RA Sanders P.R., Gilson P.R., Cantin G.T., Greenbaum D.C., Nebl T.,
RA Carucci D.J., McConville M.J., Schofield L., Hodder A.N., Yates J.R. III,
RA Crabb B.S.;
RT "Distinct protein classes including novel merozoite surface antigens in
RT Raft-like membranes of Plasmodium falciparum.";
RL J. Biol. Chem. 280:40169-40176(2005).
RN [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH RH5 AND HUMAN BSG, AND INTERACTION
RP WITH RH5.
RX PubMed=28186186; DOI=10.1038/ncomms14333;
RA Galaway F., Drought L.G., Fala M., Cross N., Kemp A.C., Rayner J.C.,
RA Wright G.J.;
RT "P113 is a merozoite surface protein that binds the N terminus of
RT Plasmodium falciparum RH5.";
RL Nat. Commun. 8:14333-14333(2017).
CC -!- FUNCTION: Membrane receptor which tethers secreted RH5 to the merozoite
CC membrane during merozoite invasion of host erythocytes.
CC {ECO:0000269|PubMed:28186186}.
CC -!- SUBUNIT: Forms a complex composed of RH5, P113 and human BSG/basigin;
CC the complex bridges the merozoite and host erythrocyte membranes
CC (PubMed:28186186). Within the complex, interacts with RH5 (via N-
CC terminus); the interaction tethers RH5 to the merozoite membrane
CC (PubMed:28186186). {ECO:0000269|PubMed:28186186}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16203726,
CC ECO:0000269|PubMed:28186186}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:16203726}.
CC -!- DEVELOPMENTAL STAGE: Expressed during parasite asexual blood stages,
CC specifically at the schizont stage and in free merozoites (at protein
CC level). {ECO:0000269|PubMed:28186186}.
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DR EMBL; LN999946; CZT99914.1; -; Genomic_DNA.
DR RefSeq; XP_001348374.1; XM_001348338.1.
DR PDB; 6Z2L; X-ray; 1.95 A; A=23-219.
DR PDBsum; 6Z2L; -.
DR AlphaFoldDB; Q8ILP3; -.
DR SMR; Q8ILP3; -.
DR IntAct; Q8ILP3; 9.
DR STRING; 5833.PF14_0201; -.
DR SwissPalm; Q8ILP3; -.
DR PRIDE; Q8ILP3; -.
DR ABCD; Q8ILP3; 1 sequenced antibody.
DR EnsemblProtists; CZT99914; CZT99914; PF3D7_1420700.
DR GeneID; 811782; -.
DR KEGG; pfa:PF3D7_1420700; -.
DR VEuPathDB; PlasmoDB:PF3D7_1420700; -.
DR HOGENOM; CLU_306005_0_0_1; -.
DR InParanoid; Q8ILP3; -.
DR OMA; NATIHYT; -.
DR PhylomeDB; Q8ILP3; -.
DR Proteomes; UP000001450; Chromosome 14.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0020005; C:symbiont-containing vacuole membrane; IDA:GeneDB.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..945
FT /note="Surface protein P113"
FT /evidence="ECO:0000255"
FT /id="PRO_5019107734"
FT PROPEP 946..969
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000448667"
FT REGION 223..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 945
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 697
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 876
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 40..54
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6Z2L"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:6Z2L"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 146..161
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6Z2L"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6Z2L"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:6Z2L"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:6Z2L"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:6Z2L"
SQ SEQUENCE 969 AA; 112574 MW; 323C98B89520153C CRC64;
MKIPFFILHI LLLQFLLCLI RCYVHNDVIK FGEENSLKCS QGNLYVLHCE VQCLNGNNEI
IHKRCNDDIE KKCNGNNKCI YFFEYELRKK TQSFRNKNSI EISECVESEQ NEVKTSTTCL
LSNSFILDEA FIQYFFFIKN KNEEPVICKD GNINIKSALL HSPFCEIKLK DISEYIRKKC
DNNKECLIDP LDVQKNLLNE EDPCYINNSY VSVNVVCNKE EEIGDESTDS SSMEIQDSTS
NEQDENVKGM SSSQEMNSNN DENKNQDNES DDDVNNNNNN NNDDQDEQGN DGDVTSSMNK
NEDNKDLEHG SSNDVNNNTD TLVNNKENKE FVLKEKSSLT SKINKELAHR TALFNKLADN
ISLLLNKKYD SFEIKDVLED RYNEMKRDAN PDVYYIYLMD TLDIEKIEDI NLEEVKMSLL
ASLKETMNKI DTIEKKIEEF KNKYISLYNK VKTTMPELFD LNEDLVLLYN DFPFDNGMIS
SDIFFKYNPS ENIMDHQEMV KKGSITEDEL RIVNDLEPLD NYRRRKRITE LRKILVEKLR
ILYLEKNNLF NTQASCIKSY CYKNPLNLKT LEVLLKKNYY RLKENKDYDV VSSIIQHLDN
VDANKKKKWL THERILKKLQ VLIAEGYKRI NEKEKDIDRR MAVYNALYEK AQSYNLQKLF
NDSNDFLKKY AIMGNSFDDG DEVFGSQSSN FNIFDSNNTD QNNEQEQPKQ DDQLLNNNND
DVLSESNNEN KEKTSDDATH KETQEKSDQE PSQNIQEDNS DEKHAENEEN VEQIETDSNV
SEEANDENKD NMQTTTDEGT EELQQNDEDA ESLTKENSKS EEQENEDSTD AEAIDKEEVE
TEEKGKDEQK KDEQKEQDEE EDGEKENKHK SSETTNETVT DIEENKNEVK GEEHLQGSEQ
SIEASESSQK DETKETEDKE EYVNANDDES SEEDTTPNET NKTDNGSSFF FAMSNALLVI
LLLLFIEFL
