ID C3YF16_BRAFL Unreviewed; 713 AA.
AC C3YF16;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=C-type lectin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_92276 {ECO:0000313|EMBL:EEN61260.1};
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:EEN61260.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN61260.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN61260.1};
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:PRU00076}.
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DR EMBL; GG666507; EEN61260.1; -; Genomic_DNA.
DR RefSeq; XP_002605250.1; XM_002605204.1.
DR AlphaFoldDB; C3YF16; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; C3YF16; -.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0010001; P:glial cell differentiation; IBA:GO_Central.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00037; CLECT; 2.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 2.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR24044:SF417; EGF-LIKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF00059; Lectin_C; 2.
DR SMART; SM00034; CLECT; 2.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 2.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..713
FT /note="C-type lectin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002935592"
FT DOMAIN 138..229
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 235..349
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 351..388
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 390..426
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 615..703
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 378..387
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 416..425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 713 AA; 77872 MW; 17EA4CD0E26F7DFC CRC64;
MANSGLWWSH RLLAFVLLSH LLFVSTAQNS VTLPDDGTTR TNLGDDALLE YGYTTEPGAS
MLFEVWKKMP SSGIGNKANN GSFDVFAAYR GRVEPVGEAS LRLLSVTKDD AGEYQLSTTF
SDGTSDRKER TLIVQFAPED TTVTATPGLI AQEGVTEVLL TCQAGGIPAP TYTWTGANLP
ADAAQDPNTG TLTLTNIQRA AAGQYTCTAD NGVPQLPGDD PAALTNSVNV QVQFHNNKCY
RQSRDALSHK EAAAACVFMG GQLVDIKDPH EQQILNDIIR STNDVSHWTF MKSQSPELLH
IDGSTLSLQS SWMASDIYGP FDICVLLDRE QSYKGDFHAC TEQHNYFCES PVIQCQPNVC
QNGGFCKSCF NGSPMCACSP GYTGVFCETD INECASNPCQ NGGTCHDHVN SFACFCRLGY
DGDVCENDID YCATSPCPPG WTCVDQEVGF HCDAGYQLST TLGSRCLGIL TTCPSHRNLA
FWISVESLGC PHLANQTFTT NLSFGVTGHE LDTTSSLENM TTTLPVVKTT APAVTTLLQD
GTTPVPNVTT TRTVVTTELK AVTTILMDMI TTYRECLFAT GVMKRSKILG NTNQDTSTTR
KTSRIGCRQV GYKLLAGTCI RLNLRKLSYK TARKTCKKDG ARLAMPETEE LDLALRNLVQ
KEGHNINFWI GLRNKGGFFL RKRHWLWEDG SKLGHYKVFT TGEQSRGQGV IYT
//
