ID   MSA2_PLAFH              Reviewed;         281 AA.
AC   Q99319;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Merozoite surface antigen 2, allelic form 3;
DE            Short=MSA-2;
DE   Flags: Precursor;
GN   Name=MSA2;
OS   Plasmodium falciparum (isolate thtn / Thailand).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=70151;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2090943; DOI=10.1016/0166-6851(90)90146-d;
RA   Thomas A.W., Carr D.A., Carter J.M., Lyon J.A.;
RT   "Sequence comparison of allelic forms of the Plasmodium falciparum
RT   merozoite surface antigen MSA2.";
RL   Mol. Biochem. Parasitol. 43:211-220(1990).
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.
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; M60189; AAA29689.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q99319; -.
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..255
FT                   /note="Merozoite surface antigen 2, allelic form 3"
FT                   /id="PRO_0000024596"
FT   PROPEP          256..281
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000024597"
FT   REGION          42..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..207
FT                   /note="Polymorphic region"
FT   COMPBIAS        100..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           255
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        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   281 AA;  28892 MW;  50598AA42D64CCBC CRC64;
     MKVIKTLSII NFFIFVTFNI KNESKYSNTF INNAYNMSIR RSMEESNPPT GASGRAGAGA
     SGRAGAGASG RAGAGAGAVA SAGSGDGAVA SAGNGANPGA DAKRSTSTPA TTTTTTTTND
     AEASTSTSSE NPNHNNAKTN PKGKEVQEPN KANTETQNNS NVQQDSQTKS NVPPTQDADT
     KSPTAQPEQA ENSAPTAEQT ESPELQSAPE NKGTGQHGHM HGSRNNHPQN TSDSQKECTD
     GNKENCGAAT SLLNNSSNIA SINKFVVLIS ATLVLSFAIF I