MIA1_SARMU
ID MIA1_SARMU Reviewed; 241 AA.
AC Q26539;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Microneme antigen;
DE AltName: Full=Lectin SML3;
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 [GENOMIC DNA], 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).
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 -!- SUBUNIT: Homodimer or heterodimer of major microneme antigen and
CC microneme antigen.
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}.
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DR EMBL; U21964; AAB18146.1; -; Genomic_DNA.
DR AlphaFoldDB; Q26539; -.
DR SMR; Q26539; -.
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:0007155; P:cell adhesion; 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 Cell adhesion; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; Lectin; Repeat; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT PROPEP 35..103
FT /evidence="ECO:0000269|PubMed:8801555"
FT /id="PRO_0000021722"
FT CHAIN 104..241
FT /note="Microneme antigen"
FT /id="PRO_0000021723"
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 61..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..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; 26510 MW; E25B1B18A6CA0162 CRC64;
MRLPIRFPKY VLYGMASAVW SILFLHILVG DTMSAADALS WSGGLIHSPA HRVNVMRSHH
HEMGKELEQQ HGAEEQQMQR DTKPAAFSNP PHLATGRGPS FVHADGQLDV SCFPHDKNIG
SRTTEVAVVQ VSSVQDCMKQ CQSRPTCSHF TYNKNSKACH LKDGAPVFYT YNGDMTGPRS
CDYSCTDNCW MNSETAVKAL DYSGHGPGLC WAACKGTAGC IMYTFKGSTC TLYAKDSFNK
S