PHPA_PLACH
ID PHPA_PLACH Reviewed; 441 AA.
AC Q02752;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Acidic phosphoprotein;
DE AltName: Full=50 kDa antigen;
DE Flags: Precursor;
GN Name=PCEMA1;
OS Plasmodium chabaudi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5825;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IP-PC1;
RX PubMed=1475002; DOI=10.1016/0166-6851(92)90154-c;
RA Deleersnijder W., Prasomsitti P., Tungpradubkul S., Hendrix D.,
RA Hamers-Casterman C., Hamers R.;
RT "Structure of a Plasmodium chabaudi acidic phosphoprotein that is
RT associated with the host erythrocyte membrane.";
RL Mol. Biochem. Parasitol. 56:59-68(1992).
CC -!- FUNCTION: During infection, this phosphoprotein probably modulates the
CC structure of the red cell membrane to the advantage of the parasite,
CC although its precise function is not known.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Note=Peripheral membrane protein on the cytoplasmic
CC face of the host erythrocyte membrane.
CC -!- MISCELLANEOUS: Associated with the host red cell membrane throughout
CC the entire erythrocytic cycle.
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DR EMBL; M95789; AAA29732.1; -; Genomic_DNA.
DR PIR; A48455; A48455.
DR AlphaFoldDB; Q02752; -.
DR VEuPathDB; PlasmoDB:PCHAS_1001500; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR010882; PCEMA1.
DR Pfam; PF07418; PCEMA1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Repeat; Signal.
FT SIGNAL 1..15
FT /note="Or 24"
FT /evidence="ECO:0000255"
FT CHAIN 16..441
FT /note="Acidic phosphoprotein"
FT /id="PRO_0000024575"
FT REPEAT 186..193
FT /note="1-1"
FT REPEAT 194..201
FT /note="1-2"
FT REPEAT 202..209
FT /note="1-3"
FT REPEAT 210..217
FT /note="1-4"
FT REPEAT 218..225
FT /note="1-5"
FT REPEAT 226..233
FT /note="1-6"
FT REPEAT 234..241
FT /note="1-7"
FT REPEAT 242..249
FT /note="1-8"
FT REPEAT 250..257
FT /note="1-9"
FT REPEAT 258..265
FT /note="1-10"
FT REPEAT 266..273
FT /note="1-11"
FT REPEAT 274..281
FT /note="1-12"
FT REPEAT 282..289
FT /note="1-13"
FT REPEAT 290..297
FT /note="1-14"
FT REPEAT 298..305
FT /note="1-15"
FT REPEAT 306..313
FT /note="1-16"
FT REPEAT 353..360
FT /note="2-1"
FT REPEAT 361..368
FT /note="2-2"
FT REGION 186..313
FT /note="16 X 8 AA tandem repeats"
FT REGION 232..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..370
FT /note="2 X 9 AA tandem repeats"
FT COMPBIAS 288..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..340
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..411
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 441 AA; 49708 MW; DB85E83E795EE7E5 CRC64;
MKAISLGLIS SIIFSIVLAK NSSGSGSSTG CFGCFRKKPK KKILATEVAK PVKAPETADF
DPKLPNLKFI EEFEPITIEG CKSRLHELDE PFVSETDGMI IDKVTGFSRR ENDSVLSGWY
IRPYEEGYEN MIKVNFIPLR EYYKRMENRP PKQYDGPPPI PDMPQGYVPP KKEEIPVEQY
VIQLSEEDPY LLQEEDALSL MEYDAETLNE GDAETLNEGD AETLNEYDAG TLNEEDAGTT
NEAGEGTTNE EGEGAANEYD AETLNEYDAD TLNEYDAGTL NEYDAGTLNE EEGSTTNEAG
EGTSNEAGEG TANDDEELDE EVASIFDDDE HADDLSLLDY DENSNENQEN VKKGNENEGE
QKGNENEGEQ KGKKKKAKEK SKKKVKNKPT MTTKKKKKKE KKKKKKEKEK KKEKKVKVEV
IMDHFSEMEK MMNNKIKHWN K