MSA2_PLAFK
ID MSA2_PLAFK Reviewed; 280 AA.
AC Q03643;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Merozoite surface antigen 2;
DE Short=MSA-2;
DE Flags: Precursor;
GN Name=MSA2;
OS Plasmodium falciparum (isolate K1 / Thailand).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5839;
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; M59766; AAA29693.1; -; Genomic_DNA.
DR PDB; 4QXT; X-ray; 1.58 A; Q=33-49.
DR PDB; 4QYO; X-ray; 1.21 A; Q=33-41.
DR PDBsum; 4QXT; -.
DR PDBsum; 4QYO; -.
DR AlphaFoldDB; Q03643; -.
DR SMR; Q03643; -.
DR ABCD; Q03643; 2 sequenced antibodies.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein;
KW Malaria; Membrane; Merozoite; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..254
FT /note="Merozoite surface antigen 2"
FT /id="PRO_0000024602"
FT PROPEP 255..280
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000024603"
FT REGION 44..206
FT /note="Polymorphic region"
FT REGION 47..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 254
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 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:4QYO"
SQ SEQUENCE 280 AA; 29542 MW; 9395D8AFB6B473EF CRC64;
MKVIKTLSII NFFIFVTFNI KNGSKYSNTF INNAYNMSIR RSMANEGSNT KSVGANAPKA
DTIASGSQSS TNSASTSTTN NGESQTTTPT AADTPTATES NSRSPPITTT ESNSRSPPIT
TTESNSRSPP ITTTESNSRS PPITTTESNS RSPPITTTES SSSGNAPNKT DGKGEESEKQ
NELNESTEEG PKAPQEPQTA ENENPAAPEN KGTGQHGHMH GSRNNHPQNT SDSQKECTDG
NKENCGAATS LLNNSSNIAS INKFVVLISA TLVLSFAIFI
