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MSA2_PLAF9
ID   MSA2_PLAF9              Reviewed;         302 AA.
AC   Q03994;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Merozoite surface antigen 2;
DE            Short=MSA-2;
DE   Flags: Precursor;
GN   Name=MSA2;
OS   Plasmodium falciparum (isolate tak 9).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=57276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1990294; DOI=10.1128/mcb.11.2.963-971.1991;
RA   Fenton B., Clark J.T., Khan C.M.A., Robinson J.V., Walliker D., Ridley R.,
RA   Scaife J.G., McBride J.S.;
RT   "Structural and antigenic polymorphism of the 35- to 48-kilodalton
RT   merozoite surface antigen (MSA-2) of the malaria parasite Plasmodium
RT   falciparum.";
RL   Mol. Cell. Biol. 11:963-971(1991).
CC   -!- FUNCTION: May play a role in the merozoite attachment to the
CC       erythrocyte.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- DEVELOPMENTAL STAGE: During the trophozoite and schizont stages.
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DR   EMBL; X53833; CAA37830.1; -; Genomic_DNA.
DR   PIR; A39615; A39615.
DR   AlphaFoldDB; Q03994; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   InterPro; IPR001136; MSA_2.
DR   Pfam; PF00985; MSA_2; 1.
DR   PIRSF; PIRSF003575; MSA_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Malaria; Membrane;
KW   Merozoite; Repeat; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..276
FT                   /note="Merozoite surface antigen 2"
FT                   /id="PRO_0000024588"
FT   PROPEP          277..302
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000024589"
FT   REGION          44..228
FT                   /note="Polymorphic region"
FT   REGION          114..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           276
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
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        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   302 AA;  30260 MW;  4E0A7EB08227CF66 CRC64;
     MKVIKTLSII NFFIFVTFNI KNESKYSNTF INNAYNMSIR RSMEESKPPT GAVAGSGAGA
     GSGAGAVAGS GAGAVAGSGA GAVAGSGAGA VAGSGAGAVA GSGAGAVAGS GAGNGANPGA
     DAERSPSTPA TTTTTTTTND AEASTSTSSE NRNHNNAETN PKGKGEVQKP NQANKETQNN
     SNVQQDSQTK SNVPRTQDAD TKSPTAQPEQ AENSAPTAEQ TESPELQSAP ENKGTGQHGH
     MHGSRNNHPQ NTSDSQKECT DGNKENCGAA TSLLNNSSNI ASINKFVVLI SATLVLSFAI
     FI
 
 
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