MSA2_PLAFJ
ID MSA2_PLAFJ Reviewed; 264 AA.
AC P50499;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Merozoite surface antigen 2;
DE Short=MSA-2;
DE Flags: Precursor;
GN Name=MSA2;
OS Plasmodium falciparum (isolate fid3 / India).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=70152;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8719253; DOI=10.1016/0166-6851(96)83010-6;
RA Bhattacharya P., Malhotra P., Sharma P., Okenu D.M.N., Chauhan V.S.;
RT "Merozoite surface antigen 2 (MSA-2) gene of Plasmodium falciparum strains
RT from India.";
RL Mol. Biochem. Parasitol. 74:125-128(1995).
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 -!- MISCELLANEOUS: Same sequence in Indian isolates FIS1 and FIJ4.
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DR EMBL; X87249; CAA60699.1; -; Genomic_DNA.
DR PIR; S55367; S55367.
DR AlphaFoldDB; P50499; -.
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..238
FT /note="Merozoite surface antigen 2"
FT /id="PRO_0000024600"
FT PROPEP 239..264
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000024601"
FT REPEAT 60..91
FT /note="1"
FT REPEAT 92..123
FT /note="2"
FT REGION 44..190
FT /note="Polymorphic region"
FT REGION 46..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..123
FT /note="2 X 32 AA perfects repeats"
FT COMPBIAS 46..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 238
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 152
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 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 264 AA; 27948 MW; 267829A62FA6FE31 CRC64;
MKVIKTLSII NFFIFVTFNI KNESKYSNTF INNAYNMSIR RSMANEGSNT NSVGANAPNA
DTIASGSQRS TNSASTSTTN NGESQTTTPT AADTIASGSQ RSTNSASTST TNNGESQTTT
PTAADTPTTT ESNSPSPPIT TTESSKFWQC TNKTDGKGEE SEKQNELNES TEEGPKAPQE
PQTAENENPA APENKGTGQH GHMHGSRNNH PQNTSDSQKE CTDGNKENCG AATSLLNNSS
NIASINKFVV LISATLVLSF AIFI
