ID   MSA2_PLAF2              Reviewed;         347 AA.
AC   Q03646;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Merozoite surface antigen 2;
DE            Short=MSA-2;
DE   Flags: Precursor;
GN   Name=MSA2;
OS   Plasmodium falciparum (isolate Nig32 / Nigeria).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=70150;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2000383; DOI=10.1073/pnas.88.5.1751;
RA   Smythe J.A., Coppel R.L., Day K.P., Martin R.K., Oduola A.M.J., Kemp D.J.,
RA   Anders R.F.;
RT   "Structural diversity in the Plasmodium falciparum merozoite surface
RT   antigen 2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:1751-1755(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; M59765; AAA29691.1; -; Genomic_DNA.
DR   PIR; B39112; B39112.
DR   AlphaFoldDB; Q03646; -.
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.
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..321
FT                   /note="Merozoite surface antigen 2"
FT                   /id="PRO_0000024580"
FT   PROPEP          322..347
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000024581"
FT   REGION          44..273
FT                   /note="Polymorphic region"
FT   REGION          165..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           321
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        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   347 AA;  33786 MW;  ABCF24BB560BF537 CRC64;
     MKVIKTLSII NFFIFVTFNI KNESKYSNTF INNAYNMSIR RSMAESKPPT GDGAVASAGN
     GAVASAGNGA VASAGNGAVA SAGNGAGNGA GNGAGNGAGN GAGNGAGNGA GNGAGNGAGN
     GAGNGAGNGA GNGAGNGAGN GAGNGAVASA GNGAGNGAVA SAGNGAVAER SSSTPATTTT
     TTTTNDAEAS TSTSSENSNH NNAETNPKGN GEVQPNQANK ETQNNSNVQQ DSQTKSNVPR
     TQDADTKSPT AQPEQAENSA PTAEQTESPE LQSAPENKGT GQHGHMHGSR NNHPQNTSDS
     QKECTDGNKE NCGAATSLLN NSSNIASINK FVVLISATLV LSFAIFI