MIC4_TOXGO
ID MIC4_TOXGO Reviewed; 580 AA.
AC Q9XZH7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Micronemal protein 4;
DE Flags: Precursor;
GN Name=MIC4 {ECO:0000312|EMBL:AAD33906.1}; ORFNames=TgIb.0680;
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD33906.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=RH {ECO:0000312|EMBL:AAD33906.1};
RX PubMed=11053441; DOI=10.1074/jbc.m008294200;
RA Brecht S., Carruthers V.B., Ferguson D.J.P., Giddings O.K., Wang G.,
RA Jakle U., Harper J.M., Sibley L.D., Soldati D.;
RT "The toxoplasma micronemal protein MIC4 is an adhesin composed of six
RT conserved apple domains.";
RL J. Biol. Chem. 276:4119-4127(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAJ20543.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RH {ECO:0000312|EMBL:CAJ20543.1};
RX PubMed=16902086; DOI=10.1101/gr.5318106;
RA Khan A., Bohme U., Kelly K.A., Adlem E., Brooks K., Simmonds M.,
RA Mungall K., Quail M.A., Arrowsmith C., Chillingworth T., Churcher C.,
RA Harris D., Collins M., Fosker N., Fraser A., Hance Z., Jagels K., Moule S.,
RA Murphy L., O'Neil S., Rajandream M.-A., Saunders D., Seeger K.,
RA Whitehead S., Mayr T., Xuan X., Watanabe J., Suzuki Y., Wakaguri H.,
RA Sugano S., Sugimoto C., Paulsen I., Mackey A.J., Roos D.S., Hall N.,
RA Berriman M., Barrell B., Sibley L.D., Ajioka J.W.;
RT "Common inheritance of chromosome Ia associated with clonal expansion of
RT Toxoplasma gondii.";
RL Genome Res. 16:1119-1125(2006).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 45-54, AND INTERACTION WITH MIC1.
RX PubMed=11447133; DOI=10.1093/glycob/11.7.541;
RA Lourenco E.V., Pereira S.R., Faca V.M., Coelho-Castelo A.A., Mineo J.R.,
RA Roque-Barreira M.-C., Greene L.J., Panunto-Castelo A.;
RT "Toxoplasma gondii micronemal protein MIC1 is a lactose-binding lectin.";
RL Glycobiology 11:541-547(2001).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MIC1, AND SUBCELLULAR LOCATION.
RC STRAIN=RH {ECO:0000269|PubMed:11157983};
RX PubMed=11157983; DOI=10.1083/jcb.152.3.563;
RA Reiss M., Viebig N., Brecht S., Fourmaux M.-N., Soete M., Di Cristina M.,
RA Dubremetz J.F., Soldati D.;
RT "Identification and characterization of an escorter for two secretory
RT adhesins in Toxoplasma gondii.";
RL J. Cell Biol. 152:563-578(2001).
CC -!- FUNCTION: Adhesin. Required for attachment of the parasite to the host
CC cell prior to invasion. {ECO:0000269|PubMed:11053441,
CC ECO:0000269|PubMed:11157983}.
CC -!- SUBUNIT: Monomer. Part of the MIC6-MIC1-MIC4 complex. Interacts
CC directly with MIC1. {ECO:0000269|PubMed:11157983,
CC ECO:0000269|PubMed:11447133}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, microneme
CC {ECO:0000269|PubMed:11053441, ECO:0000269|PubMed:11157983}.
CC -!- DEVELOPMENTAL STAGE: Not detected in unsporulated or partially
CC sporulated oocysts, but present at approximately equal levels in fully
CC sporulated oocysts (sporozoites), bradyzoites, and tachyzoites.
CC {ECO:0000269|PubMed:11053441}.
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DR EMBL; AF143487; AAD33906.1; -; Genomic_DNA.
DR EMBL; AM055943; CAJ20543.1; -; Genomic_DNA.
DR PDB; 2LL3; NMR; -; A=410-491.
DR PDB; 2LL4; NMR; -; M=410-491.
DR PDB; 4A5V; NMR; -; A=58-218.
DR PDBsum; 2LL3; -.
DR PDBsum; 2LL4; -.
DR PDBsum; 4A5V; -.
DR AlphaFoldDB; Q9XZH7; -.
DR BMRB; Q9XZH7; -.
DR SMR; Q9XZH7; -.
DR TCDB; 9.B.87.3.1; the selenoprotein p receptor (selp-receptor) family.
DR UniLectin; Q9XZH7; -.
DR EnsemblProtists; TGME49_208030-t26_1; TGME49_208030-t26_1-p1-CDS1; TGME49_208030.
DR VEuPathDB; ToxoDB:TGARI_208030; -.
DR VEuPathDB; ToxoDB:TGCAST_208030; -.
DR VEuPathDB; ToxoDB:TGCOUG_208030; -.
DR VEuPathDB; ToxoDB:TGDOM2_208030; -.
DR VEuPathDB; ToxoDB:TGFOU_208030; -.
DR VEuPathDB; ToxoDB:TGGT1_208030; -.
DR VEuPathDB; ToxoDB:TGMAS_208030; -.
DR VEuPathDB; ToxoDB:TGME49_208030; -.
DR VEuPathDB; ToxoDB:TGP89_208030; -.
DR VEuPathDB; ToxoDB:TGPRC2_208030; -.
DR VEuPathDB; ToxoDB:TGRH88_022630; -.
DR VEuPathDB; ToxoDB:TGRUB_208030; -.
DR VEuPathDB; ToxoDB:TGVAND_208030; -.
DR VEuPathDB; ToxoDB:TGVEG_208030; -.
DR OMA; DTEDCQA; -.
DR Proteomes; UP000002437; Chromosome Ib.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd01100; APPLE_Factor_XI_like; 6.
DR InterPro; IPR000177; Apple.
DR InterPro; IPR003609; Pan_app.
DR Pfam; PF00024; PAN_1; 4.
DR Pfam; PF14295; PAN_4; 2.
DR SMART; SM00223; APPLE; 6.
DR SMART; SM00473; PAN_AP; 4.
DR PROSITE; PS50948; PAN; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Reference proteome; Repeat;
KW Signal; Virulence.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..580
FT /note="Micronemal protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000289154"
FT DOMAIN 68..137
FT /note="Apple 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 141..214
FT /note="Apple 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 232..301
FT /note="Apple 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 305..375
FT /note="Apple 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 419..488
FT /note="Apple 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 492..565
FT /note="Apple 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 93..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 97..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 137..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 166..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 170..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 232..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 257..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 261..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 305..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 332..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 336..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 419..492
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 444..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 448..454
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:4A5V"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:4A5V"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:4A5V"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:4A5V"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:4A5V"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4A5V"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:4A5V"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:4A5V"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4A5V"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:4A5V"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:4A5V"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:4A5V"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:4A5V"
FT TURN 193..198
FT /evidence="ECO:0007829|PDB:4A5V"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:4A5V"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:4A5V"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:4A5V"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:2LL3"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:2LL3"
FT HELIX 441..450
FT /evidence="ECO:0007829|PDB:2LL3"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:2LL3"
FT TURN 461..464
FT /evidence="ECO:0007829|PDB:2LL3"
FT STRAND 465..472
FT /evidence="ECO:0007829|PDB:2LL3"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:2LL3"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:2LL3"
SQ SEQUENCE 580 AA; 63021 MW; 7C8D6ECC7B859AC4 CRC64;
MRASLPVHLV VCTQLSAVWF GVAKAHGGHR LEPHVPGFLQ GFTDITPAGD DVSANVTSSE
PAKLDLSCVH SDNKGSRAPT IGEPVPDVSL EQCAAQCKAV DGCTHFTYND DSKMCHVKEG
KPDLYDLTGG KTASRSCDRS CFEQHVSYEG APDVMTAMVT SQSADCQAAC AADPSCEIFT
YNEHDQKCTF KGRGFSAFKE RGVLGVTSGP KQFCDEGGKL TQEEMEDQIS GCIQLSDVGS
MTADLEEPME ADSVGACMER CRCDGRCTHF TFNDNTRMCY LKGDKMQLYS SPGDRTGPKS
CDSSCFSNGV SYVDDPATDV ETVFEISHPI YCQVICAANP LCTVFQWYAS EAKCVVKRKG
FYKHRKTGVT GVTVGPREFC DFGGSIRDRE EADAVGSDDG LNAEATMANS PDFHDEVECV
HTGNIGSKAQ TIGEVKRASS LSECRARCQA EKECSHYTYN VKSGLCYPKR GKPQFYKYLG
DMTGSRTCDT SCLRRGVDYS QGPEVGKPWY STLPTDCQVA CDAEDACLVF TWDSATSRCY
LIGSGFSAHR RNDVDGVVSG PYTFCDNGEN LQVLEAKDTE
