COL12_RAT
ID COL12_RAT Reviewed; 742 AA.
AC Q4V885; Q76LC3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Collectin-12;
DE AltName: Full=Collectin placenta protein 1;
DE Short=CL-P1;
DE AltName: Full=Nurse cell scavenger receptor 2;
GN Name=Colec12; Synonyms=Clp1, Nsr2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-356, AND TISSUE SPECIFICITY.
RX PubMed=16868960; DOI=10.1002/jnr.20992;
RA Nakamura K., Ohya W., Funakoshi H., Sakaguchi G., Kato A., Takeda M.,
RA Kudo T., Nakamura T.;
RT "Possible role of scavenger receptor SRCL in the clearance of amyloid-beta
RT in Alzheimer's disease.";
RL J. Neurosci. Res. 84:874-890(2006).
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}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, spleen, small and large
CC intestine, stomach and brain. Expressed in neonatal microglia.
CC {ECO:0000269|PubMed:16868960}.
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DR EMBL; BC097495; AAH97495.1; -; mRNA.
DR EMBL; AB080968; BAD06456.1; -; mRNA.
DR RefSeq; NP_001020892.1; NM_001025721.1.
DR AlphaFoldDB; Q4V885; -.
DR SMR; Q4V885; -.
DR STRING; 10116.ENSRNOP00000059663; -.
DR GlyGen; Q4V885; 3 sites.
DR PaxDb; Q4V885; -.
DR PRIDE; Q4V885; -.
DR Ensembl; ENSRNOT00000065494; ENSRNOP00000059663; ENSRNOG00000016366.
DR GeneID; 361289; -.
DR KEGG; rno:361289; -.
DR UCSC; RGD:735039; rat.
DR CTD; 81035; -.
DR RGD; 735039; Colec12.
DR eggNOG; ENOG502QQKQ; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_022132_0_0_1; -.
DR InParanoid; Q4V885; -.
DR OMA; KDMDKGQ; -.
DR OrthoDB; 565046at2759; -.
DR PhylomeDB; Q4V885; -.
DR TreeFam; TF332426; -.
DR PRO; PR:Q4V885; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000016366; Expressed in lung and 19 other tissues.
DR Genevisible; Q4V885; RN.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; ISO:RGD.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0006955; P:immune response; ISO:RGD.
DR GO; GO:0006910; P:phagocytosis, recognition; ISS:UniProtKB.
DR GO; GO:0044857; P:plasma membrane raft organization; ISO:RGD.
DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; ISO:RGD.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISO:RGD.
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_0000318683"
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 452..511
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..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..142
FT /evidence="ECO:0000255"
FT COILED 220..301
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 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"
FT CONFLICT 248
FT /note="F -> S (in Ref. 2; BAD06456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 742 AA; 81546 MW; B1EB2768DB1C39F0 CRC64;
MKDDFAEEEE VQSFGYKRFG IQEGTQCTKC KNNWALKFSI ILLYVLCALL TITVAILGYK
VVEKMDTVTD GMETSRQTYD NKLIAVESDL KKLGDQTGKK ALSTNSELST FRSDILDLRQ
QLQEITEKTS KNKDMLEKLQ ANGDSLVDRQ SQLKETLQNN SFLITTVNKT LQAYNGYVTN
LQQDTSVLQG NLQSQMYSQN VVIMNLNNLN LTQVQQRNLI TNLQRSVDDT SLAIQQIKND
FQNLQQVFLQ AKKDTDWLKE KVQSLQTLAA NNSALAKANN DTLEDMNNQL SSFTGQMDNI
TTISQANEQS MKDLQDLHKD TENRTAVKFS QLEERFQVFE TDIVNIINNI SYTAHHLRTL
TSNLNDVRTT CTDTLTRHTD DLTSLNNTLV NIRLDSISLR MQQDMMRSRL DTEVANLSVV
MEEMKLVDSK HGQLIKNFTI LQGPPGPRGP KGDRGSQGPP GPTGNKGQKG EKGEPGPPGP
AGERGTIGPV GPPGERGSKG SKGSQGPKGS RGSPGKPGPQ GPSGDPGPPG PPGKDGLPGP
QGPPGFQGLQ GTVGEPGVPG PRGLPGLPGV PGMPGPKGPP GPPGPSGAME PLALQNEPTP
ASEVNGCPPH WKNFTDKCYY FSVEKEIFED AKLFCEDKSS HLVFINSREE QQWIKKQTMG
RESHWIGLTD SEQESEWKWL DGTPVDYKNW KAGQPDNWGS GHGPGEDCAG LIYAGQWNDF
QCDEINNFIC EKEREAVPSS IL
