MIA2_SARMU
ID MIA2_SARMU Reviewed; 138 AA.
AC P81860; Q549G0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Microneme antigen L2;
DE AltName: Full=Lectin SML2;
OS Sarcocystis muris.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Sarcocystis.
OX NCBI_TaxID=5813;
RN [1]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, DISULFIDE BONDS, AND CRYSTALLIZATION.
RX PubMed=11418777; DOI=10.1107/s0907444901007284;
RA Mueller J.J., Mueller E.-C., Montag T., Zyto N., Loeschner B., Klein H.,
RA Heineman U., Otto A.;
RT "Characterization and crystallization of a novel Sarcocystis muris lectin,
RT SML-2.";
RL Acta Crystallogr. D 57:1042-1045(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=12743810; DOI=10.1007/s00436-002-0600-0;
RA Klein H., Mueller S., Loeschner B., Toenjes R.R., Braun G., Mueller E.-C.,
RA Otto A., Montag T.;
RT "Cloning, sequencing and recombinant expression of the open reading frame
RT encoding a novel member of the Sarcocystis muris (Apicomplexa) microneme
RT lectin family.";
RL Parasitol. Res. 90:84-86(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH
RP 1-THIO-BETA-D-GALACTOSE, FUNCTION, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=22101820; DOI=10.1107/s0907444911037796;
RA Muller J.J., Weiss M.S., Heinemann U.;
RT "PAN-modular structure of microneme protein SML-2 from the parasite
RT Sarcocystis muris at 1.95 A resolution and its complex with 1-thio-beta-D-
RT galactose.";
RL Acta Crystallogr. D 67:936-944(2011).
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:12743810, ECO:0000269|PubMed:22101820}.
CC -!- SUBUNIT: Homodimer or heterodimer. {ECO:0000269|PubMed:22101820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC microneme.
CC -!- DEVELOPMENTAL STAGE: Cyst merozoites.
CC -!- PTM: Contains six disulfide bonds.
CC -!- MASS SPECTROMETRY: Mass=15066; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11418777};
CC -!- SIMILARITY: Belongs to the microneme antigen family. {ECO:0000305}.
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DR EMBL; AF130977; AAF36512.1; -; Genomic_DNA.
DR PDB; 2YIL; X-ray; 1.95 A; A/B/C/D/E/F=1-138.
DR PDB; 2YIO; X-ray; 2.43 A; A/B=1-138.
DR PDB; 2YIP; X-ray; 2.14 A; A/B/C/D/E/F=1-138.
DR PDBsum; 2YIL; -.
DR PDBsum; 2YIO; -.
DR PDBsum; 2YIP; -.
DR AlphaFoldDB; P81860; -.
DR SMR; P81860; -.
DR UniLectin; P81860; -.
DR EvolutionaryTrace; P81860; -.
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 3D-structure; Cell adhesion; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Lectin; Repeat.
FT CHAIN 1..138
FT /note="Microneme antigen L2"
FT /id="PRO_0000096479"
FT DOMAIN 9..78
FT /note="PAN 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 82..138
FT /note="PAN 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT BINDING 18
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 59
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 66
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 71
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT DISULFID 9..78
FT DISULFID 34..56
FT DISULFID 38..44
FT DISULFID 82..86
FT DISULFID 107..127
FT DISULFID 111..117
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:2YIL"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2YIL"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:2YIL"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:2YIL"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:2YIL"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2YIL"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2YIL"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2YIL"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:2YIL"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2YIL"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2YIL"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:2YIL"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2YIL"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2YIL"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2YIL"
SQ SEQUENCE 138 AA; 15078 MW; B37D3010A5E52E6B CRC64;
AGPQLDVSCF AHDKNIGSRT EQLSVVHVAS AQDCMKECQA LPTCSHFTYN KNSKKCHLKA
GAPEFYTYTG DMTGPRSCEH NCSDACWMDG NNPLAVWDYS GQPPALCWAA CMGTPGCDLY
TFQGMTCKLY SQTSSKRA
