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Database: UniProt
Entry: Q9XYH7
LinkDB: Q9XYH7
Original site: Q9XYH7 
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   28-FEB-2018, entry version 94.
DE   RecName: Full=Micronemal protein 6;
DE   Flags: Precursor;
GN   Name=MIC6 {ECO:0000312|EMBL:AAD28185.1};
OS   Toxoplasma gondii.
OC   Eukaryota; 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.,
RA   Di Cristina M., 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,
RP   PROTEOLYTIC PROCESSING, CLEAVAGE SITE, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=11861763;
RA   Meissner M., Reiss M., Viebig N., Carruthers V.B., Toursel C.,
RA   Tomavo S., Ajioka J.W., Soldati D.;
RT   "A family of transmembrane microneme proteins of Toxoplasma gondii
RT   contain 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.,
RA   Simpson P., Dowse T.J., Jakle U., Ramboarina S., Shivarattan T.,
RA   Matthews S., Soldati-Favre D.;
RT   "A novel galectin-like domain from Toxoplasma gondii micronemal
RT   protein 1 assists the folding, assembly, and transport of a cell
RT   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
RT   of 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,
CC       ECO:0000269|PubMed:16166092, ECO:0000269|PubMed:18818666}.
CC   -!- INTERACTION:
CC       O00834:MIC1; NbExp=3; IntAct=EBI-8078076, EBI-8078093;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       microneme membrane {ECO:0000269|PubMed:11157983,
CC       ECO:0000269|PubMed:11861763, ECO:0000269|PubMed:18818666}; Single-
CC       pass type I membrane protein {ECO:0000269|PubMed:11157983,
CC       ECO:0000269|PubMed:11861763}. Secreted. Note=Released as soluble
CC       35 kDa protein after proteolytic processing of the C-terminus
CC       (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
CC       domain 3, is required for targeting of MIC1 and MIC4 into the
CC       microneme. {ECO:0000269|PubMed:16166092,
CC       ECO:0000269|PubMed:18818666}.
CC   -!- PTM: Subject to proteolytic processing involving both the N-
CC       terminus and the C-terminus. The first EGF-like domain (EGF-like
CC       domain 1) is removed by proteolytic cleavage and is not present in
CC       the mature protein. Released as soluble 35 kDa protein after
CC       proteolytic processing at the C-terminus.
CC       {ECO:0000269|PubMed:11861763}.
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   ProteinModelPortal; Q9XYH7; -.
DR   SMR; Q9XYH7; -.
DR   IntAct; Q9XYH7; 1.
DR   MINT; Q9XYH7; -.
DR   EvolutionaryTrace; Q9XYH7; -.
DR   PMAP-CutDB; 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   GO; GO:0009405; P:pathogenesis; 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       {ECO:0000255}.
FT   CHAIN        24    349       Micronemal protein 6. {ECO:0000255}.
FT                                /FTId=PRO_0000289155.
FT   TRANSMEM    290    310       Helical. {ECO:0000255}.
FT   DOMAIN       36     80       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       96    134       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      147    192       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076,
FT                                ECO:0000269|PubMed:11157983}.
FT   REGION      204    283       Acidic domain.
FT                                {ECO:0000269|PubMed:11157983}.
FT   COMPBIAS    299    302       Poly-Leu. {ECO:0000255}.
FT   SITE         94     95       Cleavage.
FT   DISULFID     40     53       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     45     62       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     64     79       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    100    113       {ECO:0000255|PROSITE-ProRule:PRU00076,
FT                                ECO:0000269|PubMed:18818666}.
FT   DISULFID    105    122       {ECO:0000255|PROSITE-ProRule:PRU00076,
FT                                ECO:0000269|PubMed:18818666}.
FT   DISULFID    124    140       {ECO:0000255|PROSITE-ProRule:PRU00076,
FT                                ECO:0000269|PubMed:18818666}.
FT   DISULFID    148    162       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    153    173       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    175    191       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   HELIX        99    102       {ECO:0000244|PDB:2K2S}.
FT   STRAND      107    109       {ECO:0000244|PDB:2K2S}.
FT   STRAND      112    115       {ECO:0000244|PDB:2K2S}.
FT   STRAND      117    123       {ECO:0000244|PDB:2K2S}.
FT   STRAND      128    132       {ECO:0000244|PDB:2K2S}.
FT   STRAND      134    136       {ECO:0000244|PDB:2K2S}.
FT   STRAND      138    145       {ECO:0000244|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
//
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