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MSP1_PLAF3
ID   MSP1_PLAF3              Reviewed;        1682 AA.
AC   P19598; Q25921;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Merozoite surface protein 1;
DE   AltName: Full=Merozoite surface antigens;
DE   AltName: Full=PMMSA;
DE   AltName: Full=p190;
DE   Flags: Precursor;
GN   Name=MSP-1;
OS   Plasmodium falciparum (isolate ro-33 / Ghana).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-1061.
RX   PubMed=3327688; DOI=10.1002/j.1460-2075.1987.tb02759.x;
RA   Certa U., Rotmann D., Matile H., Reber-Liske R.;
RT   "A naturally occurring gene encoding the major surface antigen precursor
RT   p190 of Plasmodium falciparum lacks tripeptide repeats.";
RL   EMBO J. 6:4137-4142(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1032-1682.
RX   PubMed=7628566; DOI=10.1006/expr.1995.1091;
RA   Tolle R., Bujard H., Cooper J.A.;
RT   "Plasmodium falciparum: variations within the C-terminal region of
RT   merozoite surface antigen-1.";
RL   Exp. Parasitol. 81:47-54(1995).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- PTM: Merozoite surface antigen contain the sequence of 83 kDa, 42 kDa
CC       and 19 kDa antigens which are the major surface antigens of merozoites.
CC       The maturation take place during schizont.
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DR   EMBL; M35727; AAA29715.1; -; mRNA.
DR   EMBL; Y00087; CAA68280.1; -; Genomic_DNA.
DR   EMBL; Z35326; CAA84555.1; -; Genomic_DNA.
DR   AlphaFoldDB; P19598; -.
DR   BMRB; P19598; -.
DR   SMR; P19598; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR010901; MSP1_C.
DR   InterPro; IPR024730; MSP1_EGF_1.
DR   Pfam; PF12946; EGF_MSP1_1; 1.
DR   Pfam; PF07462; MSP1_C; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Malaria; Membrane; Merozoite; Repeat; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1661
FT                   /note="Merozoite surface protein 1"
FT                   /id="PRO_0000024552"
FT   PROPEP          1662..1682
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000024553"
FT   REGION          68..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          870..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1212..1241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1433..1453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..715
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        870..914
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1221..1241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           1661
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        599
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        785
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        881
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        901
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        947
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1071
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1569
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1575..1586
FT                   /evidence="ECO:0000250"
FT   DISULFID        1580..1596
FT                   /evidence="ECO:0000250"
FT   DISULFID        1598..1609
FT                   /evidence="ECO:0000250"
FT   DISULFID        1617..1630
FT                   /evidence="ECO:0000250"
FT   DISULFID        1624..1644
FT                   /evidence="ECO:0000250"
FT   DISULFID        1646..1660
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1682 AA;  192463 MW;  C82A1E159948CAD6 CRC64;
     MKIIFFLCSF LFFIINTQCV THESYQELVK KLEALEDAVL TGYSLFQKEK MVLKDGANTQ
     VVAKPADAVS TQSAKNPPGA TVPSGTASTK GAIRSPGAAN PSDDSSDSDA KSYADLKHRV
     QNYLFTIKEL KYPELFDLTN HMLTLCDNIH GFKYLIDGYE EINELLYKLN FYFDLLRAKL
     NDVCANDYCQ IPFNLKIRAN ELDVLKKLVF GYRKPLDFIK DNVGKMEDYI KKNKTTIANI
     NELIEGSKKT IDQNKNADNE EGKKKLYQAQ YDLFIYNKQL QEAHNLISVL EKRIDTLKKN
     ENIKKLLEDI DKIKIDAEKP TTGVNQILSL RLEKESRHEE KIKEIAKTIK FNIDRLFTDP
     LELEYYLREK NKKVDVTPKS QDPTKSVQIP KVPYPNGIVY PLPLTDIHNS LAADNDKNSY
     GDLMNPHTKE KINEKIITDN KERKIFINNI KKQIDLEEKN INHTKEQNKK LLEDYEKSKK
     DYEELLEKFY EMKFNNNFNK DVVDKIFSAR YTYNVEKQRY NNKFSSSNNS VYNVQKLKKA
     LSYLEDYSLR KGISEKDFNH YYTLKTGLEA DIKKLTEEIK SSENKILEKN FKGLTHSANA
     SLEVSDIVKL QVQKVLLIKK IEDLRKIELF LKNAQLKDSI HVPNIYKPQN KPEPYYLIVL
     KKEVDKLKEF IPKVKDMLKK EQAVLSSITQ PLVAASETTE DGGHSTHTLS QSGETEVTEE
     TEETVGHTTT VTITLPPKEV KVVENSIEHK SNDNSQALTK TVYLKKLDEF LTKSYICHKY
     ILVSNSSMDQ KLLEVYNLTP EENELKSCDR LDLLFNIQNN IPAMYSLYDS MNNDLQHLFF
     ELYQKEMIYY LHKLKEENHI KKLLEEPKQI TGTSSTSSPG NTTVNTAQSA THSNSQNQQS
     NASSTNTQNG VAVSSGPAVV EESHDPLTVL SISNDLKGIV SLLNLGNKTK VPNPLTISTT
     EMEKFYENIL KIMIPIFNDD IKQFVKSNSK VITGLTETQK NALNDEIKKL KDTLQLSFDL
     YNKYKLKLDR LFNKKKELGQ DKMQIKKLTL LKEQLESKLN SLNNPHNVLQ NFSVFFNKKK
     EAEIAETENT LENTKILLKH YKGLVKYYNG ESSPLKTLSE VSIQTEDNYA NLEKFRVLSK
     IDGKLNDNLH LGKKKLSFLS SGLHHLITEL KEVIKNKNYT GNSPSENNKK VNEALKSYEN
     FLPEAKVTTV VTPPQPDVTP SPLSVRVSGS SGSTKEETQI PTSGSLLTEL QQVVQLQNYD
     EEDDSLVVLP IFGESEDNDE YLDQVVTGEA ISVTMDNILS GFENEYDVIY LKPLAGVYRS
     LKKQIEKNIF TFNLNLNDIL NSRLKKRKYF LDVLESDLMQ FKHISSNEYI IEDSFKLLNS
     EQKNTLLKSY KYIKESVEND IKFAQEGISY YEKVLAKYKD DLESIKKVIK EEKEFPSSPP
     TTPPSPAKTD EQKKESKFLP FLTNIETLYN NLVNKIDDYL INLKAKINDC NVEKDEAHVK
     ITKLSDLKAI DDKIDLFKNP YDFEAIKKLI NDDTKKDMLG KLLSTGLVQN FPNTIISKLI
     EGKFQDMLNI SQHQCVKKQC PQNSGCFRHL DEREECKCLL NYKQEGDKCV ENPNPTCNEN
     NGGCDADAKC TEEDSGSNGK KITCECTKPD SYPLFDGIFC SSSNFLGISF LLILMLILYS
     FI
 
 
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