ID C3ZFY2_BRAFL Unreviewed; 346 AA.
AC C3ZFY2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 13-SEP-2023, entry version 71.
DE RecName: Full=C-type lectin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_68932 {ECO:0000313|EMBL:EEN48457.1};
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:EEN48457.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN48457.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN48457.1};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR EMBL; GG666616; EEN48457.1; -; Genomic_DNA.
DR RefSeq; XP_002592446.1; XM_002592400.1.
DR AlphaFoldDB; C3ZFY2; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; C3ZFY2; -.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR CDD; cd10909; ChtBD1_GH18_2; 1.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00108; KR; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 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 InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR PANTHER; PTHR24261:SF7; KRINGLE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00130; KR; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}.
FT DOMAIN 126..201
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 217..341
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 144..183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 346 AA; 38957 MW; 0D6C39E9987322FA CRC64;
MAYTKAQLSH IARRLSQINE KVNRINLKVA NTSLYLQAKA TTGLPQVIPV TQSTHVPKKK
WREDLRCGQG YPAPNGNPAE CDPAGTVPCC SPGHWCGKTV YHCDCAGCID YRDQDVHQPG
DCQAEGNGVS YRGTVSVTET GRTCQRWDSQ FPHPHDRTPE NYPLSGLEGN YCRNPDGSRR
VWCYTRDDLF MRWDYCDVPI CEAVHVENRC PDGYKLLVGT CIRLFIDGMS HHMATQACES
ERATLAMPKT GAFDGALRDL VMHEGGNNNY WIGLWEGETD TGWQWVDGTP LQTNDYTGWN
PGEPSNYGFV WGNCVQYWSG SIGYPMWDDT DCFVFKRFIC QAPALR
//
