ID C3Z037_BRAFL Unreviewed; 1078 AA.
AC C3Z037;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=SUEL-type lectin domain-containing protein {ECO:0000259|PROSITE:PS50228};
GN ORFNames=BRAFLDRAFT_85699 {ECO:0000313|EMBL:EEN54096.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN54096.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54096.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN54096.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
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).
CC -!- FUNCTION: Acts as a defensive agent. Recognizes blood group fucosylated
CC oligosaccharides including A, B, H and Lewis B-type antigens. Does not
CC recognize Lewis A antigen and has low affinity for monovalent haptens.
CC {ECO:0000256|ARBA:ARBA00002219}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
CC -!- SIMILARITY: Belongs to the fucolectin family.
CC {ECO:0000256|ARBA:ARBA00010147}.
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DR EMBL; GG666567; EEN54096.1; -; Genomic_DNA.
DR RefSeq; XP_002598084.1; XM_002598038.1.
DR AlphaFoldDB; C3Z037; -.
DR eggNOG; KOG2177; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR InParanoid; C3Z037; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042806; F:fucose binding; IEA:UniProt.
DR GO; GO:0010185; P:regulation of cellular defense response; IEA:UniProt.
DR GO; GO:0001868; P:regulation of complement activation, lectin pathway; IEA:UniProt.
DR CDD; cd10909; ChtBD1_GH18_2; 1.
DR CDD; cd22827; Gal_Rha_Lectin_SUL-I-like; 1.
DR CDD; cd05819; NHL; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR006585; FTP1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR001258; NHL_repeat.
DR PANTHER; PTHR45713:SF6; F5_8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45713; FTP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01436; NHL; 1.
DR SMART; SM00607; FTP; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51125; NHL; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 3: Inferred from homology;
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 69..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 685..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 319..362
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT DOMAIN 757..839
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT REGION 17..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1078 AA; 117495 MW; 91EA60460037A620 CRC64;
MATGNIHTGT RITVQKPMAA SNSVSNVSGN QSSHGANSND SVLNALPPNP MYVPNVHHPT
SCECTRHRVC VAVTTGTILM LCIVAGFFLW SFLSTIPPAL TTTVATTFTS GPTGYYGSVP
TPPAVSNSSQ REGTWRQWER SPTPKDWCCR SKRTASVASD DVDIEPYAVA YMEQDDMAAG
GTHTETRMQK PTAASSHNND VSANPSSNDS NSSDVVSEER QHVPNALQPN QHPSTFECTR
HRVFSAVTTA TVLVSCIVGG VFLWVLGSTN PPALTTTVAT TFTSGPTGAE CCSSVPTPPA
VSNSSQREEN HERYRKMQKI TFGGRGKEPG KFRENNGVAV SADNEVFVTD LSNNRVQVFN
MNGTYLRLFP TVVPGESGRI YPFSVAIDVK PGYLWVVGGK VIFSADAHVV QYRRDGLPIK
KFDVRFLNQI PQPRIAIDAR NNKVIVGEGQ TIMMFQPNGF LVRSFKALGI ERIRSVGIHR
VMSDKDGNIL LTDYVSVQGY SHSGHKIFTF GSFGHQEGRL IFPKDICITP LGHINVANSG
NNRPYAVRYQ EDHESALGPV DTDVTQPYAV KYQEHGDRGD DHPLSRADVA DQNGQTANVA
CDDTDIEPYA VAYMDQDDMA AGDTHTETRM QKPTAASSHN NDVSANPSSN DSNSSDVVSE
ERQRVPNALQ PNQHPSTFEC TRHRVFSAVT TATVLVLCIV GGVFLWVLGS TNPPALTTFT
SGPTGAECCS SVPTPPAVSN SSQREATAYA CGESGTLQLS CVEGKTLLIL DANYGRTSTD
HACPCSTCRA DCRAVNSLSV VRSACQGKRQ CAVRAAYSIF GEDPCWGVQK YLEASYRSSS
HPSLWGPEKA VDGFRGTAVS WYNQCLHTNQ VYQPWWKVDL GAGDPYTVNR VSVLNRGDCC
GDRLRNFQVR VGPNENFAQN DQCGETYTAR PANGATIVVY CDQPMSGRYV SIQVMGRSEY
LQICDVEVFA ETADGPKSWR DDLRCGQHYH AENGQPAECD PDGVLPCCST AAWCGNTVHH
CNCRGCVDYR NTLAGCLCPM WWMVWLLLAR RKENISDTLT RVVGWRIAAV LHSLKLNL
//
