ID C3XSE4_BRAFL Unreviewed; 450 AA.
AC C3XSE4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=C-type lectin domain-containing protein {ECO:0000259|PROSITE:PS50041};
GN ORFNames=BRAFLDRAFT_82209 {ECO:0000313|EMBL:EEN69072.1};
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:EEN69072.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN69072.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN69072.1};
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).
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DR EMBL; GG666458; EEN69072.1; -; Genomic_DNA.
DR RefSeq; XP_002613063.1; XM_002613017.1.
DR AlphaFoldDB; C3XSE4; -.
DR STRING; 7739.C3XSE4; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; C3XSE4; -.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR22801:SF53; 27 KDA PRIMARY MESENCHYME-SPECIFIC SPICULE PROTEIN; 1.
DR PANTHER; PTHR22801; LITHOSTATHINE; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 324..446
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 47017 MW; AF172F0AE0FF8A65 CRC64;
MPGGQQQSQT GDTEGPDTTP TQQAPTDWKS LADAAANIPN NMYVSSAATT PTQQAPTDWK
SVADAAANIP NNMYVSRADA YGTEMDKKIK WIRLCKRFVQ ATAAGVVVVI AVLLPYFAGK
GIPMGQNFPY VKAHGHRTAG PVGSPGPPGP LNRSGEKGPM DTDGRPGVPM SAGAPGLPVE
KRPMGPVGPM GPACEAGVSG PPGPPGEKGP MGPAGPMGPP GEAGVPGPPG PPGEKGPMGP
AGPMGPTGSR GPRGKAGVPG PPAPPGNSGP EGSPGLPGPV GPPGLPGRET CPKPAGPPGH
PQTYIQGKSF KMSCPRGYTM NMKRLGFCYK LFEIPKNFIG ASEICREDGG TLAMPRDAET
NSFLVSMIRS NMLRAVWFGL RYNREKGKFE WVDGTPLGKF NAWAPGNPRK WPKRPKHANC
VVYWPISGTV LWRDGECRPN FIFICQVILT
//
