COL11_CHICK
ID COL11_CHICK Reviewed; 271 AA.
AC Q2LK94;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Collectin-11;
DE AltName: Full=Collectin-2;
DE Short=CL-2;
DE Short=cCL-2;
DE Flags: Precursor;
GN Name=COLEC11; Synonyms=CL2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16289291; DOI=10.1016/j.molimm.2005.09.015;
RA Hogenkamp A., van Eijk M., van Dijk A., van Asten A.J.A.M.,
RA Veldhuizen E.J.A., Haagsman H.P.;
RT "Characterization and expression sites of newly identified chicken
RT collectins.";
RL Mol. Immunol. 43:1604-1616(2006).
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 -!- TISSUE SPECIFICITY: Expressed in the tongue, crop, crop mucosa,
CC coprodeum, urodeum, proctoderm, colon, lung, ovary, uterus, testis,
CC vitelline membrane, kidney, ureter, liver and skin.
CC {ECO:0000269|PubMed:16289291}.
CC -!- SIMILARITY: Belongs to the COLEC10/COLEC11 family. {ECO:0000305}.
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DR EMBL; DQ129669; AAZ29618.1; -; mRNA.
DR RefSeq; NP_001038130.1; NM_001044665.1.
DR AlphaFoldDB; Q2LK94; -.
DR SMR; Q2LK94; -.
DR STRING; 9031.ENSGALP00000042407; -.
DR PaxDb; Q2LK94; -.
DR GeneID; 428649; -.
DR KEGG; gga:428649; -.
DR CTD; 78989; -.
DR VEuPathDB; HostDB:geneid_428649; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q2LK94; -.
DR OrthoDB; 1105722at2759; -.
DR PhylomeDB; Q2LK94; -.
DR PRO; PR:Q2LK94; -.
DR Proteomes; UP000000539; 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; 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; 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_5000140435"
FT DOMAIN 56..115
FT /note="Collagen-like"
FT DOMAIN 149..265
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 46..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 116..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 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; 29503 MW; CBC7F99D1DDFF5C5 CRC64;
MKRDLVFLVT LISLAFLSLL RSGYPQHIAE ESCSVQILVP GLKGEAGEKG EKGAPGRPGR
VGPPGEKGEM GDKGQKGSMG RHGKIGPIGS KGEKGDNGDM GPPGPNGDPG IPCECSQLRK
AIGEMDIQVA QLTTELKFIK NAVAGVRETD NKIYLLVKEE KRYKEAQLYC HGRGGTLSMP
KDENANNLIA SYINQAGLTR VFIGINDLEK EGNFVYSDRS PMQTFNKWRS GEPNNAYDEE
DCVEMVASGG WNDVACHITM YFVCEFDKEN V
