ID D4AFM7_9APIC Unreviewed; 1832 AA.
AC D4AFM7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Merozoite surface protein 1 {ECO:0000256|ARBA:ARBA00022062};
DE AltName: Full=Merozoite surface antigen {ECO:0000256|ARBA:ARBA00031689};
DE AltName: Full=PMMSA {ECO:0000256|ARBA:ARBA00032276};
GN Name=msp1 {ECO:0000313|EMBL:BAI82252.1};
OS Plasmodium fieldi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=77518 {ECO:0000313|EMBL:BAI82252.1};
RN [1] {ECO:0000313|EMBL:BAI82252.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30163 {ECO:0000313|EMBL:BAI82252.1};
RX PubMed=20167126; DOI=10.1186/1471-2148-10-52;
RA Sawai H., Otani H., Arisue N., Palacpac N., de Oliveira Martins L.,
RA Pathirana S., Handunnetti S., Kawai S., Kishino H., Horii T., Tanabe K.;
RT "Lineage-specific positive selection at the merozoite surface protein 1
RT (msp1) locus of Plasmodium vivax and related simian malaria parasites.";
RL BMC Evol. Biol. 10:52-52(2010).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
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DR EMBL; AB444064; BAI82252.1; -; Genomic_DNA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR010901; MSP1_C.
DR InterPro; IPR024730; MSP1_EGF_1.
DR PANTHER; PTHR24216:SF65; PAXILLIN-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR24216; PAXILLIN-RELATED; 1.
DR Pfam; PF12946; EGF_MSP1_1; 1.
DR Pfam; PF07462; MSP1_C; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Merozoite {ECO:0000313|EMBL:BAI82252.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1832
FT /note="Merozoite surface protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003053427"
FT TRANSMEM 1803..1828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1045..1656
FT /note="Merozoite surface 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07462"
FT DOMAIN 1727..1763
FT /note="Merozoite surface protein EGF"
FT /evidence="ECO:0000259|Pfam:PF12946"
FT REGION 203..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 264..291
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 203..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1832 AA; 202711 MW; 8C926A7FA4AB919D CRC64;
MKALLFLFSF IFFVTKCQCE TENYKQLLVK LDKLEALVVD GYELFHKKKI VQSDIQSVSD
VGSNNNVNSL NYKIRDFVGK FLELQIPGHA NLLHMIRELA LDANGIKYLV ESYEEFNQLM
HVINFHYDLS RAKLNDMCAH EYCKIPEHLK ITDKELDMLK KVVLGYRKPL DNIKDDIGKM
EAFITKNKDT ITKINELITT ENGKVRNGQN TNGTNSSGAS VDGAQAVTGS TEVSQSSGSA
GSVSPSAPES YDQKKPIFQA MYNVIFYTNQ LEEAQKLIEV LEKRVKVLKE HKSIKALLDQ
VATEKGKLPS DNPTTANLTP EQTEAKNKIA DLENQIVAIA KTVNFDMDGL FTNTEELEYY
LREKAKMAGT LVTPESNQPV STTEKAVPTM KETYPHGIAY ALPESSIFEL IGKIGSDESF
GDLQNPDDGK QPKKGITISE TKRKELQDKI TNKIKIEEDK LPDLKKEYDE KFKVYEQKVN
DFKPILNHFY EARLDNTLVE TKFDAFKTHR EAYMKEKKEL EKCTYEQNTN MINKLKKQLT
YLEDYSLRKD VSDDEINYFS DMEWKLKNEI YGLAKEIQKN ENKLTVENKF DFSGVVELQV
QKVLIIKKIE ALKNIQNLLK NAKVKDNLYI PKVYKTGEKP EPYYLIVLKK EIDKLKDFIP
KIETMITTEK AKTPTSAVQI RGQSLRGASE TGATGVTSDV GTSAASASQQ SQQTQVETAP
AAPAAPVPQV ITAQPTSQSP TQAAPAPTPA ESPSPATLPS ETATTAPTET STTGTEPAVP
EGESSSEEEA TEGGETPPAV PGAATPGATP GATPAAPAAP SMSKLEYLEK LLDFLKSSYA
CHKHIFITNS TMNKDLLSQY ELTAEEKNKI KESTCDQLDL LFNVQNNLPA MYSIYDTMIN
DLQNLYIELY QKEMVYNIYK NKDTDTKIKA FLETLTSNAA AAAPAAAVAP VSAPASASAA
APVQSAANLN SQVVTNPVTT TTTVSQNNPT SGTVTNTVST TQTVAPGTQA PAATSTQPSV
VTNTPASVET NAQTTPPGEG SLTVQANSEE EAEANNVKLE DIYEKHLSQI DKYNDHFKKF
LESQKERITG MDPAQWKVLG VEIEELKKKI QVSLDHFGKY KLKLERFLKK KNKISNSKEQ
IKKLTSLKNK LERRQNLLNN PTSVLKNYAV FFNKKREAEK KEVANTLKNT EILLKYYKAR
AKYYIGEPFP LKTLSEESLQ KEDNYLNLEK FRVLSRMEGR LGNNIDLEKE NISYLSSGLH
HVFTELKEII SNKRYTGNEH AKNTAAVKEA LQAYQELLPK VGTQVSASVP ALPAGAGAAP
AVPVPVAEGA PAASADVPAA PAVPGAGAPA ASADAQAASA GAPEASAGAS EASAGAPAAL
PAGAPTTGET TGETTGETAT VTTAQDYAED YDKVIALPLF GNNDDDGEEE AEQVISGETE
NAEPEIIVPQ GINEYEVVYI KPLAGVYKTI KRQLENHVTA FNTNIIDMLD SRLKKRNYFL
DVLNSDLNPF KYPASGEYIV KDPYKLLDLE KKKKLLGSYK YIGASIDKDM VTANDGLAYY
NKMGDLYKKH LDAVNAQIKE VQDNINKQDE EIKKLGTGAS NNQNNQFSIK KAELEKYLPF
LSSIQKEYGS LVSKVHSYTE NLKKFLNNCE IEKKETDIII KKLEDYSKMD EKLEVYKRSK
KETDVRSSGL LEKLKNSKLI NEEESKKVLS ELLNVQTQML NMGSEHKCID TNVPENAACY
RYLDGTEEWR CLLNFKEEGG KCVPAPDMTC KDNNGGCAPE AECKMNENKE IVCKCTKEGS
EPLFQGVFCS SSSFLSLSFL LLILLLLLCM EL
//
