MIC6_TOXGO
ID MIC6_TOXGO Reviewed; 349 AA.
AC Q9XYH7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Micronemal protein 6;
DE Flags: Precursor;
GN Name=MIC6 {ECO:0000312|EMBL:AAD28185.1};
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:AAD28185.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MIC1, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=RH {ECO:0000312|EMBL:AAD28185.1};
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).
RN [2]
RP SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, DEVELOPMENTAL STAGE, PROTEOLYTIC
RP PROCESSING, CLEAVAGE SITE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11861763; DOI=10.1242/jcs.115.3.563;
RA Meissner M., Reiss M., Viebig N., Carruthers V.B., Toursel C., Tomavo S.,
RA Ajioka J.W., Soldati D.;
RT "A family of transmembrane microneme proteins of Toxoplasma gondii contain
RT EGF-like domains and function as escorters.";
RL J. Cell Sci. 115:563-574(2002).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MIC1, AND DOMAIN EGF-LIKE 3.
RX PubMed=16166092; DOI=10.1074/jbc.c500365200;
RA Saouros S., Edwards-Jones B., Reiss M., Sawmynaden K., Cota E., Simpson P.,
RA Dowse T.J., Jakle U., Ramboarina S., Shivarattan T., Matthews S.,
RA Soldati-Favre D.;
RT "A novel galectin-like domain from Toxoplasma gondii micronemal protein 1
RT assists the folding, assembly, and transport of a cell adhesion complex.";
RL J. Biol. Chem. 280:38583-38591(2005).
RN [4]
RP STRUCTURE BY NMR OF 87-174 IN COMPLEX WITH MIC1, DOMAIN, FUNCTION,
RP DISULFIDE BONDS, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18818666; DOI=10.1038/embor.2008.179;
RA Sawmynaden K., Saouros S., Friedrich N., Marchant J., Simpson P.,
RA Bleijlevens B., Blackman M.J., Soldati-Favre D., Matthews S.;
RT "Structural insights into microneme protein assembly reveal a new mode of
RT EGF domain recognition.";
RL EMBO Rep. 9:1149-1155(2008).
CC -!- FUNCTION: Escorter protein required for import of MIC1 and MIC4
CC adhesins into the microneme. {ECO:0000269|PubMed:11157983,
CC ECO:0000269|PubMed:16166092, ECO:0000269|PubMed:18818666}.
CC -!- SUBUNIT: Interacts directly with MIC1. Part of the MIC6-MIC1-MIC4
CC complex. {ECO:0000269|PubMed:11157983, ECO:0000269|PubMed:16166092,
CC ECO:0000269|PubMed:18818666}.
CC -!- INTERACTION:
CC Q9XYH7; O00834: MIC1; NbExp=3; IntAct=EBI-8078076, EBI-8078093;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, microneme
CC membrane {ECO:0000269|PubMed:11157983, ECO:0000269|PubMed:11861763,
CC ECO:0000269|PubMed:18818666}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:11157983, ECO:0000269|PubMed:11861763}. Secreted.
CC Note=Released as soluble 35 kDa protein after proteolytic processing of
CC the C-terminus (PubMed:11861763).
CC -!- DEVELOPMENTAL STAGE: Detected in tachyzoites (at protein level).
CC Expressed in rapidly dividing tachyzoites.
CC {ECO:0000269|PubMed:11861763}.
CC -!- DOMAIN: The EGF-like domains 2 and 3 and part of the acidic domain
CC interact with the galectin-like domain of MIC1. The presence of at
CC least one of the EGF-like domains, EGF-like domain 2 or EGF-like domain
CC 3, is required for targeting of MIC1 and MIC4 into the microneme.
CC {ECO:0000269|PubMed:16166092, ECO:0000269|PubMed:18818666}.
CC -!- PTM: Subject to proteolytic processing involving both the N-terminus
CC and the C-terminus. The first EGF-like domain (EGF-like domain 1) is
CC removed by proteolytic cleavage and is not present in the mature
CC protein. Released as soluble 35 kDa protein after proteolytic
CC processing at the C-terminus. {ECO:0000269|PubMed:11861763}.
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DR EMBL; AF110270; AAD28185.1; -; mRNA.
DR PDB; 2K2S; NMR; -; B=87-147.
DR PDB; 2K2T; NMR; -; A=87-147.
DR PDBsum; 2K2S; -.
DR PDBsum; 2K2T; -.
DR AlphaFoldDB; Q9XYH7; -.
DR BMRB; Q9XYH7; -.
DR SMR; Q9XYH7; -.
DR IntAct; Q9XYH7; 1.
DR MINT; Q9XYH7; -.
DR TCDB; 9.B.87.3.1; the selenoprotein p receptor (selp-receptor) family.
DR VEuPathDB; ToxoDB:TGARI_218520; -.
DR VEuPathDB; ToxoDB:TGCAST_218520; -.
DR VEuPathDB; ToxoDB:TGCOUG_218520; -.
DR VEuPathDB; ToxoDB:TGDOM2_218520; -.
DR VEuPathDB; ToxoDB:TGFOU_218520; -.
DR VEuPathDB; ToxoDB:TGGT1_218520; -.
DR VEuPathDB; ToxoDB:TGMAS_218520; -.
DR VEuPathDB; ToxoDB:TGME49_218520; -.
DR VEuPathDB; ToxoDB:TGP89_218520; -.
DR VEuPathDB; ToxoDB:TGPRC2_218520; -.
DR VEuPathDB; ToxoDB:TGRH88_058880; -.
DR VEuPathDB; ToxoDB:TGRUB_218520; -.
DR VEuPathDB; ToxoDB:TGVAND_218520; -.
DR VEuPathDB; ToxoDB:TGVEG_218520; -.
DR EvolutionaryTrace; Q9XYH7; -.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033163; C:microneme membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cytoplasmic vesicle; Disulfide bond;
KW EGF-like domain; Membrane; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix; Virulence.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..349
FT /note="Micronemal protein 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000289155"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 36..80
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 96..134
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 147..192
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000269|PubMed:11157983"
FT REGION 194..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..283
FT /note="Acidic domain"
FT /evidence="ECO:0000269|PubMed:11157983"
FT COMPBIAS 197..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 94..95
FT /note="Cleavage"
FT DISULFID 40..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 45..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 64..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 100..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000269|PubMed:18818666"
FT DISULFID 105..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000269|PubMed:18818666"
FT DISULFID 124..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000269|PubMed:18818666"
FT DISULFID 148..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 153..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 175..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:2K2S"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2K2S"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2K2S"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2K2S"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:2K2S"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2K2S"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:2K2S"
SQ SEQUENCE 349 AA; 36656 MW; F0EEBD19DEBB29C8 CRC64;
MRLFRCCAAA VVAAESLLWL KNGSPFFAFL PGNGEIADNC SGNPCGGTAA GTCINTPSGY
DCRCEPGYVL GVENDQVTCM MPSGVPMANF VQLSETPAAC SSNPCGPEAA GTCKETNSGY
ICRCNQGYRI SLDGTGNVTC IVRQESGCEE NGCGPPDAVQ SCRRLTGTAG RLCVCKENFI
ATIDASAHIT CKRVPPHYRK PPFEFGKGGH PVDSEPSKRQ REDEGESREP ESDSTEPGRD
QERRTPLEES QEPEGSTPDS QQSRGGSGSD STESEEQGKE REEGSGHAGA IAGGVIGGLL
LLSAAGAGVA YMRKSGSGGG EEIEYERGIE AAEASEVEVL VDLDSKTWD
