COL11_XENLA
ID COL11_XENLA Reviewed; 271 AA.
AC Q7T0T0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Collectin-11;
DE Flags: Precursor;
GN Name=colec11;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lectin that plays a role in innate immunity, apoptosis and
CC embryogenesis. Calcium-dependent lectin that binds self and non-self
CC glycoproteins presenting high mannose oligosaccharides with at least
CC one terminal alpha-1,2-linked mannose epitope. Primarily recognizes the
CC terminal disaccharide of the glycan. Also recognizes a subset of
CC fucosylated glycans and lipopolysaccharides. Plays a role in innate
CC immunity through its ability to bind non-self sugars presented by
CC microorganisms and to activate the complement through the recruitment
CC of MAPS1. Also plays a role in apoptosis through its ability to bind in
CC a calcium-independent manner the DNA present at the surface of
CC apoptotic cells and to activate the complement in response to this
CC binding. Finally, plays a role in development, probably serving as a
CC guidance cue during the migration of neural crest cells and other cell
CC types during embryogenesis. {ECO:0000250|UniProtKB:Q9BWP8}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Interacts with MASP1; probably
CC triggers the lectin pathway of complement.
CC {ECO:0000250|UniProtKB:Q9BWP8}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9BWP8}.
CC -!- SIMILARITY: Belongs to the COLEC10/COLEC11 family. {ECO:0000305}.
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DR EMBL; BC056052; AAH56052.1; -; mRNA.
DR RefSeq; NP_001080337.1; NM_001086868.1.
DR AlphaFoldDB; Q7T0T0; -.
DR SMR; Q7T0T0; -.
DR PRIDE; Q7T0T0; -.
DR DNASU; 380029; -.
DR GeneID; 380029; -.
DR KEGG; xla:380029; -.
DR CTD; 380029; -.
DR Xenbase; XB-GENE-952509; colec11.L.
DR OMA; HITMYFL; -.
DR OrthoDB; 1105722at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 380029; Expressed in spleen and 13 other tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0120153; F:calcium-dependent carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0042806; F:fucose binding; ISS:UniProtKB.
DR GO; GO:0005537; F:mannose binding; ISS:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR GO; GO:0019730; P:antimicrobial humoral response; ISS:UniProtKB.
DR GO; GO:0001867; P:complement activation, lectin pathway; ISS:UniProtKB.
DR CDD; cd03591; CLECT_collectin_like; 1.
DR Gene3D; 3.10.100.10; -; 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; IPR033990; Collectin_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen; Disulfide bond; Immunity; Innate immunity; Lectin;
KW Mannose-binding; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..271
FT /note="Collectin-11"
FT /id="PRO_0000314235"
FT DOMAIN 50..109
FT /note="Collagen-like"
FT DOMAIN 149..265
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 45..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 240
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 244
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 252..254
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT DISULFID 170..264
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 242..256
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 271 AA; 29334 MW; 587129273C476AE2 CRC64;
MKKDLLFWGT IISLGFLILL GSGYCQHITD ETCSVQILVP GLKGDAGEKG EKGAPGRPGR
VGPPGEKGEI GDKGIKGSMG RHGKIGPIGS KGEKGDVGQI GPPGPNGEPG IPCECGQLRK
AVGEMDIQVA QLATEVKFVK NVVAGVRETE TKIYLLVKEE KKYIDAQDYC QGRGGTLSMP
KDEATNSLIA SYINHAGLSR VFIGINDLER EGHFVYSDRS PMQTFNKWRQ AEPNNAYDEE
DCAEMVSSGG WNDVSCLITM YFICEFDKEN V
