MIAM_SARMU
ID MIAM_SARMU Reviewed; 241 AA.
AC Q08668;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Major microneme antigen;
DE AltName: Full=Lectin SML1;
DE Flags: Precursor;
OS Sarcocystis muris.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Sarcocystis.
OX NCBI_TaxID=5813;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 104-126.
RX PubMed=8114823; DOI=10.1016/0166-6851(93)90174-v;
RA Eschenbacher K.-H., Klein H., Sommer I., Meyer H.E., Entzeroth R.,
RA Mehlhorn H., Rueger W.;
RT "Characterization of cDNA clones encoding a major microneme antigen of
RT Sarcocystis muris (Apicomplexa) cyst merozoites.";
RL Mol. Biochem. Parasitol. 62:27-36(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 104-126.
RX PubMed=8801555; DOI=10.1007/s004360050101;
RA Klein H., Mehlhorn H., Rueger W.;
RT "Characterization of genomic clones encoding two microneme antigens of
RT Sarcocystis muris (Apicomplexa).";
RL Parasitol. Res. 82:230-237(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-241.
RA Klein H., Eschenbacher K.-H., Sommer I., Entzeroth R., Mehlhorn H.,
RA Rueger W.;
RT "Cloning and expression in E.coli of cDNAs encoding a 16/17 kDa major
RT microneme protein of Sarcocystis muris?";
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9557874; DOI=10.1023/a:1006964105349;
RA Klein H., Loeschner B., Zyto N., Poertner M., Montag T.;
RT "Expression, purification, and biochemical characterization of a
RT recombinant lectin of Sarcocystis muris (Apicomplexa) cyst merozoites.";
RL Glycoconj. J. 15:147-153(1998).
CC -!- FUNCTION: Galactose-binding lectin. Plays a role in adhesion to the
CC host cell. Has a potential role in invasion of host cells.
CC {ECO:0000269|PubMed:9557874}.
CC -!- SUBUNIT: Homodimer or heterodimer of major microneme antigen and
CC microneme antigen. {ECO:0000269|PubMed:9557874}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC microneme.
CC -!- DEVELOPMENTAL STAGE: Cyst merozoites.
CC -!- PTM: Contains six disulfide bonds. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the microneme antigen family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB42049.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L13471; AAB42048.1; -; mRNA.
DR EMBL; L08892; AAB42049.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q08668; -.
DR SMR; Q08668; -.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0020009; C:microneme; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd01100; APPLE_Factor_XI_like; 1.
DR InterPro; IPR000177; Apple.
DR InterPro; IPR003609; Pan_app.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF14295; PAN_4; 1.
DR SMART; SM00223; APPLE; 1.
DR SMART; SM00473; PAN_AP; 1.
DR PROSITE; PS50948; PAN; 2.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; Lectin;
KW Repeat; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT PROPEP 35..103
FT /evidence="ECO:0000269|PubMed:8114823,
FT ECO:0000269|PubMed:8801555"
FT /id="PRO_0000021724"
FT CHAIN 104..241
FT /note="Major microneme antigen"
FT /id="PRO_0000021725"
FT DOMAIN 112..181
FT /note="PAN 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 185..241
FT /note="PAN 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT REGION 64..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT DISULFID 112..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 137..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 141..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 185..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 210..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 214..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
SQ SEQUENCE 241 AA; 26483 MW; 12E063841BE72012 CRC64;
MTLPIHFPRC VLYGMASAVW SILFLHILVG DTMSAADALS WSGGLIHSPA HRVNVMRSHH
HEMGKELEQQ HGGEEQQMQR DTKPAAFSNP PHLATGRGPS FVHADGQLDV SCFPHDKNIG
SRTTEVAVVQ VSSVQDCMKQ CQSRPTCSHF TYNKNSKKCH LKDGAPVFYT YTGDMTGPRS
CEHTCTDNCW MHSGNPLGTF QYSGHAPAFC WAACKGTAGC VMYTFQGGVC KLYSKNSVER
A
