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