MSA2_PLAFC
ID MSA2_PLAFC Reviewed; 262 AA.
AC Q99317;
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 1;
DE Short=MSA-2;
DE Flags: Precursor;
GN Name=MSA2;
OS Plasmodium falciparum (isolate Camp / Malaysia).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5835;
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; M60186; AAA29687.1; -; Genomic_DNA.
DR AlphaFoldDB; Q99317; -.
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..236
FT /note="Merozoite surface antigen 2, allelic form 1"
FT /id="PRO_0000024590"
FT PROPEP 237..262
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000024591"
FT REGION 44..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..188
FT /note="Polymorphic region"
FT COMPBIAS 44..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 236
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 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 262 AA; 27375 MW; 72E0B2A315E9D154 CRC64;
MKVIKTLSII NFFIFVTFNI KNESKYSNTF INNAYNMSIR RSMAESKPPT GTGGSGSAGS
GAGASAGNGA NPGADAERSP STPATPATPA TTTTTTTTND AEASTSTSSE NPNHKNAETN
PKGKGEVQKP NQANKETQNN SNVQQDSQTK SNVPPTQDAD TKSPTAQPEQ AENSAPTAEQ
TESPELQSAP ENKGTGQHGH MHGSRNNHPQ NTSDSQKECT DGNKENCGAA TSLLNNSSNI
ASINKFVVLI SATLVLSFAI FI