COL11_BOVIN
ID COL11_BOVIN Reviewed; 267 AA.
AC Q17QH6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Collectin-11;
DE AltName: Full=Collectin kidney protein 1;
DE Short=CL-K1;
DE Flags: Precursor;
GN Name=COLEC11;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) 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; BC118358; AAI18359.1; -; mRNA.
DR RefSeq; NP_001069771.1; NM_001076303.2.
DR RefSeq; XP_015328215.1; XM_015472729.1.
DR AlphaFoldDB; Q17QH6; -.
DR SMR; Q17QH6; -.
DR STRING; 9913.ENSBTAP00000021590; -.
DR PaxDb; Q17QH6; -.
DR PRIDE; Q17QH6; -.
DR Ensembl; ENSBTAT00000021590; ENSBTAP00000021590; ENSBTAG00000016225.
DR GeneID; 613991; -.
DR KEGG; bta:613991; -.
DR CTD; 78989; -.
DR VEuPathDB; HostDB:ENSBTAG00000016225; -.
DR VGNC; VGNC:27578; COLEC11.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000159468; -.
DR HOGENOM; CLU_049894_3_2_1; -.
DR InParanoid; Q17QH6; -.
DR OMA; HITMYFL; -.
DR OrthoDB; 1105722at2759; -.
DR TreeFam; TF330481; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000016225; Expressed in liver and 49 other tissues.
DR ExpressionAtlas; Q17QH6; baseline and differential.
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:0042802; F:identical protein binding; IEA:Ensembl.
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 GO; GO:0032502; P:developmental process; ISS:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:Ensembl.
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; Coiled coil; Collagen; Developmental protein; Disulfide bond;
KW Immunity; Innate immunity; Lectin; Mannose-binding; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..267
FT /note="Collectin-11"
FT /id="PRO_0000315043"
FT DOMAIN 49..108
FT /note="Collagen-like"
FT DOMAIN 145..261
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 40..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 110..144
FT /evidence="ECO:0000255"
FT BINDING 196
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 236
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 237
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 248..250
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT DISULFID 166..260
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 238..252
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 267 AA; 28333 MW; CF7CDD91045CB33F CRC64;
MKRALALMGL AFLCVLRAGA AQQTVDDACS VQILVPGLKG DAGEKGDKGA PGRPGRVGPT
GEKGDVGDKG QKGGVGRHGK IGPIGSKGEK GDSGDIGPPG PNGEPGIPCE CSQLRKAIGE
MDNQVTQLTA ELKFIKNAVA GVRETEQKMY LLVKEEKRYL DAQLACQGRG GTLSMPKDEA
ANALLAAYIT QAGLARVFIG INDLEREGAF VYADRSPMQT FSKWRSGEPN NAYDEEDCVE
LVASGGWNDV ACHLTMHFLC EFDKEHV
