ID C3XZP4_BRAFL Unreviewed; 522 AA.
AC C3XZP4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=C-type lectin domain-containing protein {ECO:0000259|PROSITE:PS50041};
GN ORFNames=BRAFLDRAFT_85571 {ECO:0000313|EMBL:EEN66442.1};
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:EEN66442.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN66442.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN66442.1};
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; GG666476; EEN66442.1; -; Genomic_DNA.
DR RefSeq; XP_002610432.1; XM_002610386.1.
DR AlphaFoldDB; C3XZP4; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; C3XZP4; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR016187; CTDL_fold.
DR PANTHER; PTHR20003; GLYCOPROTEIN-RELATED; 1.
DR PANTHER; PTHR20003:SF4; PROLINE-RICH PROTEIN BSTNI SUBFAMILY 3; 1.
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 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 290..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 394..511
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 51..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 57087 MW; 8334A74BEE7DBECE CRC64;
MIMAEDIITT DAVPRVHTDG VLEGTVTQIR SDAEIQKVAN VVSNWLPNPT YETGHCPEND
ANSSPPVQDN TTNPELYYIH NKEERLTNPG SLDNDVSNGY KENDYKNHML YTTDAKVCAA
EAIKISSADA NIHPSSDENT CQNDIVASKA YINSPSRQNS GYTTDRSYSR NSLYEKATST
TTTNGDGNDK DVIPKDDAYS EIPEQVDVTD DDANLDHSLP YAVECEFTNP SYISDCNLTK
HNSEKMVPGN NNNDKPPKRH VPTMEPADAL NRNPMYVQNA PQQGRCQCTY GWVCIVVTIA
ALSFASGFFG IWLHYNNNGW KAQENADATT TSVQPAWDAT YTYGHLAVDT NFTNGQSAAD
TTNTHGQTSS DTISHLAADT TENPVCPIAG YVSFNGVCYK DFAERKTYCD ARQTCAADGG
LLAMPKDKAT NAFIHDLGGA TDQRWIGLTD ADSDGKWAFA DGQTLEASGY NNWEPGEPNN
LSGGEDCAEV GTKVHFWNDE RCSRTKGFIC QLVDTARTAT VV
//
