LRRCB_BRAFL
ID LRRCB_BRAFL Reviewed; 265 AA.
AC C3YZ59;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Leucine-rich repeat-containing protein Bf66946 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=BRAFLDRAFT_66946 {ECO:0000312|EMBL:EEN54567.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739 {ECO:0000312|Proteomes:UP000001554};
RN [1] {ECO:0000312|Proteomes:UP000001554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000312|EMBL:EEN54567.1};
RC TISSUE=Testis {ECO:0000312|EMBL:EEN54567.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
RN [2] {ECO:0007744|PDB:4XSQ}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 21-202, FUNCTION, SUBCELLULAR
RP LOCATION, DISULFIDE BONDS, AND MUTAGENESIS OF 32-TYR--GLU-34 AND
RP 105-ASP--ASP-107.
RX PubMed=26821753; DOI=10.1038/srep19951;
RA Cao D.D., Liao X., Cheng W., Jiang Y.L., Wang W.J., Li Q., Chen J.Y.,
RA Chen Y., Zhou C.Z.;
RT "Structure of a variable lymphocyte receptor-like protein from the
RT amphioxus Branchiostoma floridae.";
RL Sci. Rep. 6:19951-19951(2016).
CC -!- FUNCTION: Binds selectively to the Gram-positive bacteria S.aureus and
CC S.pneumoniae. Does not adhere to the Gram-negative bacteria E.coli and
CC S.enterica. Probably recognizes peptidoglycans expressed on the
CC bacterial cell surface. {ECO:0000269|PubMed:26821753}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:26821753};
CC Single-pass type I membrane protein {ECO:0000255}.
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DR EMBL; GG666565; EEN54567.1; -; Genomic_DNA.
DR RefSeq; XP_002598555.1; XM_002598509.1.
DR PDB; 4XSQ; X-ray; 1.79 A; A/B=21-202.
DR PDBsum; 4XSQ; -.
DR AlphaFoldDB; C3YZ59; -.
DR SMR; C3YZ59; -.
DR STRING; 7739.XP_002598555.1; -.
DR eggNOG; KOG4237; Eukaryota.
DR InParanoid; C3YZ59; -.
DR OrthoDB; 1050061at2759; -.
DR Proteomes; UP000001554; Partially assembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 2.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..265
FT /note="Leucine-rich repeat-containing protein Bf66946"
FT /id="PRO_5002936227"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 21..50
FT /note="LRRNT"
FT /evidence="ECO:0000255"
FT REPEAT 51..75
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 76..99
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 100..123
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT DOMAIN 142..193
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 21..27
FT /evidence="ECO:0000269|PubMed:26821753,
FT ECO:0007744|PDB:4XSQ"
FT DISULFID 25..39
FT /evidence="ECO:0000269|PubMed:26821753,
FT ECO:0007744|PDB:4XSQ"
FT DISULFID 146..171
FT /evidence="ECO:0000269|PubMed:26821753,
FT ECO:0007744|PDB:4XSQ"
FT DISULFID 148..192
FT /evidence="ECO:0000269|PubMed:26821753,
FT ECO:0007744|PDB:4XSQ"
FT MUTAGEN 32..34
FT /note="YGE->AGA: No effect on binding to the bacteria
FT S.aureus and S.pneumoniae."
FT /evidence="ECO:0000269|PubMed:26821753"
FT MUTAGEN 105..107
FT /note="DID->KIK: Abolishes binding to the bacteria S.aureus
FT and S.pneumoniae."
FT /evidence="ECO:0000269|PubMed:26821753"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:4XSQ"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:4XSQ"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:4XSQ"
FT TURN 70..75
FT /evidence="ECO:0007829|PDB:4XSQ"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4XSQ"
FT TURN 94..99
FT /evidence="ECO:0007829|PDB:4XSQ"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4XSQ"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:4XSQ"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:4XSQ"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4XSQ"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4XSQ"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:4XSQ"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4XSQ"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:4XSQ"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4XSQ"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:4XSQ"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:4XSQ"
SQ SEQUENCE 265 AA; 29133 MW; 6C962257EB8AE4F9 CRC64;
MALRDIFLLS MAMTAVTVQA CPSACKCTVS LYGEMVVACG GMGLTEIPED IPHRAVYLVL
KDNNITKITS YSFKGLRNLQ GIDLSNNKIN HISSAALRHL GHLDDIDLSR NELTSVSEKL
FDFPISSAKA QGRRFFVYLA NNPWGCDCRM AWLAQELAGG SKTFGDRHME CATPAALAGR
GLSEIPQTSF VCTGRDISFD SDGIIATPEE STAFPVAYKV AVVFGCITGL VTILLLVLTA
MLYQKRRIRL GSKYELRWNK HPEFV
