BSL1_TRIVA
ID BSL1_TRIVA Reviewed; 625 AA.
AC Q8MTI2;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Putative surface protein bspA-like;
DE AltName: Full=TvBspA-like-625;
GN Name=BSPAL1;
OS Trichomonas vaginalis.
OC Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC Trichomonas.
OX NCBI_TaxID=5722;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12467987; DOI=10.1016/s0166-6851(02)00211-6;
RA Hirt R.P., Harriman N., Kajava A.V., Embley T.M.;
RT "A novel potential surface protein in Trichomonas vaginalis contains a
RT leucine-rich repeat shared by micro-organisms from all three domains of
RT life.";
RL Mol. Biochem. Parasitol. 125:195-199(2002).
CC -!- FUNCTION: May bind host tissue.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Note=Surface membrane. {ECO:0000305}.
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DR EMBL; AY101349; AAM51159.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8MTI2; -.
DR SMR; Q8MTI2; -.
DR VEuPathDB; TrichDB:TVAG_073760; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13306; LRR_5; 2.
PE 4: Predicted;
KW Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..625
FT /note="Putative surface protein bspA-like"
FT /id="PRO_0000064998"
FT TOPO_DOM 1..548
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 38..60
FT /note="LRR 1"
FT REPEAT 61..83
FT /note="LRR 2"
FT REPEAT 85..106
FT /note="LRR 3"
FT REPEAT 107..129
FT /note="LRR 4"
FT REPEAT 153..175
FT /note="LRR 5"
FT REPEAT 176..198
FT /note="LRR 6"
FT REPEAT 200..221
FT /note="LRR 7"
FT REPEAT 222..245
FT /note="LRR 8"
FT REPEAT 247..267
FT /note="LRR 9"
FT REPEAT 271..293
FT /note="LRR 10"
FT REPEAT 325..347
FT /note="LRR 11"
FT REPEAT 348..368
FT /note="LRR 12"
FT REPEAT 369..392
FT /note="LRR 13"
FT REGION 439..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 625 AA; 67022 MW; 62EF37BDA8AD001A CRC64;
MMTPGKSSKT PIVGNLTTLG ITIPDTVTSI GFKTFYGCSS FTSIIIPNSV TSIGTKAFTG
CSSLTSITIG NSVTSFGQEA FSECSSITSI TIPNSVTTIR DFAFSGCSKL TSITIPNSVT
SLGSHAFRGC SGLTSIIIPD SVTLIRGSIF YGCSSLTSIT IPNSVTSIYS SAFYGCSSLT
SITIPDSVLD FGSAAFQECS KLTNIKIGNN VDSIGSLAFK RCSSLTNITI PDSVTTIANS
AFYECSKLTS ITIGKSVTRI EGNAFSKCYS LTSITIKTTN DITSSITTDV FLNCPITELI
YETTGLTFLT YEYFKDKVTL IKFNIPKSDS NSMIRLQEIT SLPTLTHFTN LNKVTIENIN
ELTIPESFIE GDNFEILITN NIKSIDPNAF KDCSINKFTY LGTDKLENDF LKNAKSCEEV
ITSTKYSDNE IGGMTITHKQ SEENPNQPGE NPNQPGENPN QPGENPNQPG ENPSQPGENP
SQPGENPNQP GENPSQPGEN PNQPGENPNQ PGENPNQPGE NPSQPGENTD DPSKSKENKA
IKGGEIAGII IGSLIGICLV VAICFGVYYY FMRIKPKNKN DDNEGNQEDT IANGTNEVTN
ENVLATFDEQ PNNESDSNGL DSAEV
