COL12_BOVIN
ID COL12_BOVIN Reviewed; 742 AA.
AC A6QP79;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Collectin-12;
DE AltName: Full=Collectin placenta protein 1;
DE Short=CL-P1;
GN Name=COLEC12; Synonyms=CLP1;
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 muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Scavenger receptor that displays several functions associated
CC with host defense. Promotes binding and phagocytosis of Gram-positive,
CC Gram-negative bacteria and yeast. Mediates the recognition,
CC internalization and degradation of oxidatively modified low density
CC lipoprotein (oxLDL) by vascular endothelial cells. Binds to several
CC carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose,
CC GalNAc, T and Tn antigens in a calcium-dependent manner and
CC internalizes specifically GalNAc in nurse-like cells. Binds also to
CC sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: The extracellular domain forms a stable trimer. The
CC extracellular domain interacts with fibrillar amyloid-beta peptide (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}. Note=Forms clusters on the cell
CC surface. {ECO:0000250}.
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DR EMBL; BC149193; AAI49194.1; -; mRNA.
DR RefSeq; NP_001095313.1; NM_001101843.1.
DR AlphaFoldDB; A6QP79; -.
DR SMR; A6QP79; -.
DR STRING; 9913.ENSBTAP00000044662; -.
DR PaxDb; A6QP79; -.
DR PRIDE; A6QP79; -.
DR Ensembl; ENSBTAT00000047455; ENSBTAP00000044662; ENSBTAG00000007705.
DR GeneID; 504741; -.
DR KEGG; bta:504741; -.
DR CTD; 81035; -.
DR VEuPathDB; HostDB:ENSBTAG00000007705; -.
DR VGNC; VGNC:27579; COLEC12.
DR eggNOG; ENOG502QQKQ; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_022132_0_0_1; -.
DR InParanoid; A6QP79; -.
DR OMA; KDMDKGQ; -.
DR OrthoDB; 565046at2759; -.
DR TreeFam; TF332426; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000007705; Expressed in anterior segment of eyeball and 102 other tissues.
DR ExpressionAtlas; A6QP79; baseline and differential.
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; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:Ensembl.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0006910; P:phagocytosis, recognition; ISS:UniProtKB.
DR GO; GO:0044857; P:plasma membrane raft organization; IEA:Ensembl.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IEA:Ensembl.
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; 3.
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; Glycoprotein; Lectin;
KW Membrane; Metal-binding; Receptor; Reference proteome; Repeat;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..742
FT /note="Collectin-12"
FT /id="PRO_0000318680"
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 443..502
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..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..141
FT /evidence="ECO:0000255"
FT COILED 215..254
FT /evidence="ECO:0000255"
FT COILED 296..328
FT /evidence="ECO:0000255"
FT COMPBIAS 519..539
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..587
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 CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 81751 MW; F569E3703431959D CRC64;
MKDDFAEEEE VHSFGYKRFG IQEGTQCTKC KNNWALKLSI ILLYILCALL TITVAILGYK
VVEKMDNVTG GMETSRQTYD DKLTAVESDL KKLGDQTGKK ALSTNSELST FRSDILDLRQ
QLREITEKTS KNKDTLEKLQ ASGDALVDRQ SQLKETLENN SFLITTVNKT LQAYNGYVTN
LQQDTSVLQG NLQSQMYSHN VVIMNLNNLN LTQVQQRNLI TNLQRSVDDT SQAIQRIKND
FQNLQQVFLQ AKKDTDWLKE KVQSLQTLAA NNSALAKANN DTLEDMNSQL SSFTGQMDNI
TTASQANEQN LKDLQDVHRD AENRTAAKFS QLEERFQLFE SDIVNIISNI SYTAHYLRTL
TSNLNEVRTT CTDTLTKHTD DLTSLNNTLA NIRLDSVSLR MQQDLMRSRL DTEVANLSVI
MEEMKLVDSK HGQLIKNFTI LQGPPGPRGP KGDRGQQGPP GPTGNKGQKG EKGEPGPPGP
AGERGPIGPV GPPGERGSKG SKGLQGSKGS RGSPGKPGPQ GPSGDPGPPG PPGKDGLPGP
QGPPGFQGLQ GTVGEPGVPG PRGLPGLPGM PGMPGIKGPP GPPGPSGAAV PLALKTEPTT
APEDNGCLPY WKNFTDKCYY FSTERDFFED AKLFCERMSS HLVFINTGEE QQWIKNQMVA
KQNYWIGLTD LEQENEWRWL DGTLLEYKNW KAGQPDNWGH GHGPGEDCAG LINFGQWNDF
PCEDMNHFIC EKDRERELAI TL
