COL12_CHICK
ID COL12_CHICK Reviewed; 742 AA.
AC Q2LK54;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Collectin-12;
DE AltName: Full=Collectin-3;
DE Short=CL-3;
DE Short=cCL-3;
GN Name=COLEC12; Synonyms=CL3;
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: Scavenger receptor that displays several functions associated
CC with host defense. Binds to carbohydrates (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16289291}.
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DR EMBL; DQ157755; AAZ80767.1; -; mRNA.
DR RefSeq; NP_001034688.1; NM_001039599.1.
DR AlphaFoldDB; Q2LK54; -.
DR SMR; Q2LK54; -.
DR STRING; 9031.ENSGALP00000030293; -.
DR PaxDb; Q2LK54; -.
DR GeneID; 421061; -.
DR KEGG; gga:421061; -.
DR CTD; 81035; -.
DR VEuPathDB; HostDB:geneid_421061; -.
DR eggNOG; ENOG502QQKQ; Eukaryota.
DR InParanoid; Q2LK54; -.
DR OrthoDB; 565046at2759; -.
DR PhylomeDB; Q2LK54; -.
DR PRO; PR:Q2LK54; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038187; F:pattern recognition receptor activity; IBA:GO_Central.
DR CDD; cd03590; CLECT_DC-SIGN_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; IPR033989; CD209-like_CTLD.
DR InterPro; IPR008160; Collagen.
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; Disulfide bond; Lectin; Membrane;
KW Metal-binding; Receptor; Reference proteome; Repeat; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..742
FT /note="Collectin-12"
FT /id="PRO_0000318684"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..742
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 467..526
FT /note="Collagen-like 1"
FT DOMAIN 527..586
FT /note="Collagen-like 2"
FT DOMAIN 614..731
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 439..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 71..101
FT /evidence="ECO:0000255"
FT COILED 271..334
FT /evidence="ECO:0000255"
FT COMPBIAS 479..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..538
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..592
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 644
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 650
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 674
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 691
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 694
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 694
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 696
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 696
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 697
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 707
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 718
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 718
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 731
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT DISULFID 607..618
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 635..730
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 708..722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 742 AA; 81837 MW; D39D2464BF081769 CRC64;
MKDDFAEEEE VQSFGYKRFG IQEGTQCTKC KNNWALKFSI ILLYILCVLL TITIAILGYK
VVEKMDNVTG GLETSHRRYT EKLTEVESDL KKLDDQAGQK ALNTNTELSS FRSDILALRQ
QLHDIAEKTT RNKDTLEKLQ ESGNVLDDRQ SQIRSALDSN SFMIISVNKT LQAYTGYINN
LQQDTSNIQS DLQNQVHSHN VVIMNLNNLN LTQIQQRNLI SVLQKSMEDK SLAILRIKND
FQNLQQVVLQ ARKDTDWLKE KVQNLQTLAA NNSALAKANN DTLEDMNNQL SSFSGQMENI
STIAQANEQN LKDLQEQHKE YENRTSAKFN QLEERFQVFE TDIVNIISNI SYTAHHLRTL
TSNLNEVRTT CTDTLSKHSD ELIFMNSTLA NIRLDSASLK MQQDLMRSRL DVEVANLSVI
MEEMKLVDSK HGQLIKNFTI LQGPPGPRGP KGDRGPQGPL GPAGLKGQKG EKGEPGPPGP
AGEKGPPGPI GPPGEKGGKG SRGSPGSKGQ RGSPGKTGLP GPSGDPGPPG PQGKDGPQGP
QGPPGFQGLQ GTVGEPGVPG PRGLPGLPGV PGLPGPKGPP GPPGPPGPGM PMALQSEPTS
VPEANGCSPH WKNYTEKCYY FSIEREIFEE AKLFCEEKAS RLVIINNKEE QQWIKRQISG
KGSFWIGLTD SEKENEWRWL DGSLPLYTNW KTGQPDNWNH GHGPGEDCAG LIYAGLWNDF
YCEDVNNFIC EKDMDKEQIF GV
