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MSA2_PLAF1
ID   MSA2_PLAF1              Reviewed;         286 AA.
AC   P50496;
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;
DE            Short=MSA-2;
DE   Flags: Precursor;
GN   Name=MSA2;
OS   Plasmodium falciparum (isolate 311).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=57265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1542312; DOI=10.1016/0166-6851(92)90255-i;
RA   Marshall V.M., Coppel R.L., Anders R.F., Kemp D.J.;
RT   "Two novel alleles within subfamilies of the merozoite surface antigen 2
RT   (MSA-2) of Plasmodium falciparum.";
RL   Mol. Biochem. Parasitol. 50:181-184(1992).
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; M73809; AAA29697.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50496; -.
DR   BMRB; P50496; -.
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..260
FT                   /note="Merozoite surface antigen 2"
FT                   /id="PRO_0000024578"
FT   PROPEP          261..286
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000024579"
FT   REGION          43..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..212
FT                   /note="Polymorphic region"
FT   COMPBIAS        43..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           260
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        163
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        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   286 AA;  28844 MW;  D1F4947CE68D5805 CRC64;
     MKVIKTLSII NFFIFVTFNI KNESKYSNTF INNAYNMSIR RSMTESKTPT PTGAGAGASG
     SAGSGDGASG SASGSASGSA SGSAGASGSA SGSAGASGSA SGSAGAEGSP STPATTTTTT
     TTNDAEASTS TSSENPNHNN AKTNPKGNGG VQKPNQANKE TQNNSNVQQD SQTKSNVPPT
     QDADTKSPTA QPEQAENSAP TAEQTESPEL QSAPENKGTG QHGHMHGSRN NHPQNTSDSQ
     KECTDGNKEN CGAATSLLNN SSNIASINKF VVLISATLVL SFAIFI
 
 
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