COL11_DANRE
ID COL11_DANRE Reviewed; 271 AA.
AC Q5U3G1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Collectin-11;
DE Flags: Precursor;
GN Name=colec11; ORFNames=zgc:103572;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=21258343; DOI=10.1038/ng.757;
RA Rooryck C., Diaz-Font A., Osborn D.P., Chabchoub E.,
RA Hernandez-Hernandez V., Shamseldin H., Kenny J., Waters A., Jenkins D.,
RA Kaissi A.A., Leal G.F., Dallapiccola B., Carnevale F., Bitner-Glindzicz M.,
RA Lees M., Hennekam R., Stanier P., Burns A.J., Peeters H., Alkuraya F.S.,
RA Beales P.L.;
RT "Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC
RT syndrome.";
RL Nat. Genet. 43:197-203(2011).
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 (By similarity). Finally, plays a role in development, probably
CC serving as a guidance cue during the migration of neural crest cells
CC and other cell types during embryogenesis (PubMed:21258343).
CC {ECO:0000250|UniProtKB:Q9BWP8, ECO:0000269|PubMed:21258343}.
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; BC085557; AAH85557.1; -; mRNA.
DR RefSeq; NP_001007332.1; NM_001007331.1.
DR AlphaFoldDB; Q5U3G1; -.
DR SMR; Q5U3G1; -.
DR STRING; 7955.ENSDARP00000016314; -.
DR PaxDb; Q5U3G1; -.
DR GeneID; 492459; -.
DR KEGG; dre:492459; -.
DR CTD; 78989; -.
DR ZFIN; ZDB-GENE-041114-11; colec11.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q5U3G1; -.
DR OrthoDB; 1105722at2759; -.
DR PhylomeDB; Q5U3G1; -.
DR Reactome; R-DRE-166662; Lectin pathway of complement activation.
DR Reactome; R-DRE-166663; Initial triggering of complement.
DR Reactome; R-DRE-3000480; Scavenging by Class A Receptors.
DR PRO; PR:Q5U3G1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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 GO; GO:0032502; P:developmental process; IDA:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IMP:ZFIN.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..271
FT /note="Collectin-11"
FT /id="PRO_0000315046"
FT DOMAIN 44..103
FT /note="Collagen-like"
FT DOMAIN 149..265
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 46..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 124..148
FT /evidence="ECO:0000255"
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 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; 29284 MW; F945BDB9E79D9490 CRC64;
MVGEKLVAYM LVSVLGLALL RSVFGQHMPE EPCSVQILVP GLKGEAGEKG EKGAPGRPGR
VGPTGEQGPP GDKGQKGSPG RYGKMGPTGP KGLKGDMGDP GPKGPNGEPG VPCECAPLRK
MIGEMDIQVV QLTNELKFIK NAVAGIKETD SKVYLLVKEE KRYREAEVFC QGRGGHLAMP
KDAAANRAIA GYVTDAGLSR VYIGINDLER EGHFVYVERS PMTTFSRWRE GEPNNAYDDE
DCVEMVSSGE WIDVACQLTM YFVCEFDKDT V
