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Collectin-12 (Collectin placenta protein 1) (CL-P1) (hCL-P1) (Nurse cell scavenger receptor 2) (Scavenger receptor class A member 4) (Scavenger receptor with C-type lectin)

 COL12_HUMAN             Reviewed;         742 AA.
Q5KU26; Q6P9F2; Q8TCR2; Q8WZA4; Q9BY85; Q9BYH7;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
12-SEP-2018, entry version 125.
RecName: Full=Collectin-12;
AltName: Full=Collectin placenta protein 1;
Short=CL-P1;
Short=hCL-P1;
AltName: Full=Nurse cell scavenger receptor 2;
AltName: Full=Scavenger receptor class A member 4;
AltName: Full=Scavenger receptor with C-type lectin;
Name=COLEC12; Synonyms=CLP1, NSR2, SCARA4, SRCL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND VARIANTS PRO-522 AND SER-606.
TISSUE=Placenta;
PubMed=11162630; DOI=10.1006/bbrc.2000.4210;
Nakamura K., Funakoshi H., Miyamoto K., Tokunaga F., Nakamura T.;
"Molecular cloning and functional characterization of a human
scavenger receptor with C-type lectin (SRCL), a novel member of a
scavenger receptor family.";
Biochem. Biophys. Res. Commun. 280:1028-1035(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT
PRO-522.
TISSUE=Lung, and Placenta;
PubMed=11564734; DOI=10.1074/jbc.M103942200;
Ohtani K., Suzuki Y., Eda S., Kawai T., Kase T., Keshi H., Sakai Y.,
Fukuoh A., Sakamoto T., Itabe H., Suzutani T., Ogasawara M.,
Yoshida I., Wakamiya N.;
"The membrane-type collectin CL-P1 is a scavenger receptor on vascular
endothelial cells.";
J. Biol. Chem. 276:44222-44228(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT
PRO-522.
PubMed=12761161; DOI=10.1093/jb/mvg037;
Yoshida T., Tsuruta Y., Iwasaki M., Yamane S., Ochi T., Suzuki R.;
"SRCL/CL-P1 recognizes GalNAc and a carcinoma-associated antigen, Tn
antigen.";
J. Biochem. 133:271-277(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-91; PRO-522
AND SER-606.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-742.
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
VARIANTS PRO-522 AND SER-606.
PubMed=12601552; DOI=10.1007/s100380300011;
Ohmori H., Makita Y., Funamizu M., Chiba S., Ohtani K., Suzuki Y.,
Wakamiya N., Hata A.;
"Haplotype analysis of the human collectin placenta 1 (hCL-P1) gene.";
J. Hum. Genet. 48:82-85(2003).
[8]
FUNCTION, AND SUBUNIT.
PubMed=15845541; DOI=10.1074/jbc.M504197200;
Coombs P.J., Graham S.A., Drickamer K., Taylor M.E.;
"Selective binding of the scavenger receptor C-type lectin to Lewis X
trisaccharide and related glycan ligands.";
J. Biol. Chem. 280:22993-22999(2005).
[9]
INTERACTION WITH FIBRILLAR AMYLOID-BETA PEPTIDE, FUNCTION IN CLEARANCE
OF AMYLOID-BETA, AND TISSUE SPECIFICITY.
PubMed=16868960; DOI=10.1002/jnr.20992;
Nakamura K., Ohya W., Funakoshi H., Sakaguchi G., Kato A., Takeda M.,
Kudo T., Nakamura T.;
"Possible role of scavenger receptor SRCL in the clearance of amyloid-
beta in Alzheimer's disease.";
J. Neurosci. Res. 84:874-890(2006).
[10]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 603-742 IN COMPLEX WITH
CALCIUM IONS, AND DISULFIDE BONDS.
PubMed=17420244; DOI=10.1074/jbc.M701624200;
Feinberg H., Taylor M.E., Weis W.I.;
"Scavenger receptor C-type lectin binds to the leukocyte cell surface
glycan Lewis X by a novel mechanism.";
J. Biol. Chem. 282:17250-17258(2007).
-!- FUNCTION: Scavenger receptor that displays several functions
associated with host defense. Promotes binding and phagocytosis of
Gram-positive, Gram-negative bacteria and yeast. Mediates the
recognition, internalization and degradation of oxidatively
modified low density lipoprotein (oxLDL) by vascular endothelial
cells. Binds to several carbohydrates including Gal-type ligands,
D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a
calcium-dependent manner and internalizes specifically GalNAc in
nurse-like cells. Binds also to sialyl Lewis X or a trisaccharide
and asialo-orosomucoid (ASOR). May also play a role in the
clearance of amyloid-beta in Alzheimer disease.
{ECO:0000269|PubMed:11162630, ECO:0000269|PubMed:11564734,
ECO:0000269|PubMed:12761161, ECO:0000269|PubMed:15845541,
ECO:0000269|PubMed:16868960}.
-!- SUBUNIT: The extracellular domain forms a stable trimer. The
extracellular domain interacts with fibrillar amyloid-beta
peptide. {ECO:0000269|PubMed:15845541,
ECO:0000269|PubMed:16868960, ECO:0000269|PubMed:17420244}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11162630};
Single-pass type II membrane protein
{ECO:0000269|PubMed:11162630}. Note=Forms clusters on the cell
surface.
-!- TISSUE SPECIFICITY: Expressed in perivascular macrophages.
Expressed in plaques-surrounding reactive astrocytes and in
perivascular astrocytes associated with cerebral amyloid
angiopathy (CAA) in the temporal cortex of Alzheimer patient (at
protein level). Strongly expressed in placenta. Moderately
expressed in heart, skeletal muscle, small intestine and lung.
Weakly expressed in brain, colon, thymus and kidney. Expressed in
nurse-like cells. Expressed in reactive astrocytes and
vascular/perivascular cells in the brain of Alzheimer patient.
{ECO:0000269|PubMed:11162630, ECO:0000269|PubMed:11564734,
ECO:0000269|PubMed:12761161, ECO:0000269|PubMed:16868960}.
-!- SEQUENCE CAUTION:
Sequence=BAB39148.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB038518; BAB39147.1; -; mRNA.
EMBL; AB052103; BAB39148.1; ALT_SEQ; mRNA.
EMBL; AB005145; BAB72147.1; -; mRNA.
EMBL; AB034251; BAD83592.1; -; mRNA.
EMBL; AP000915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP005240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC060789; AAH60789.1; -; mRNA.
EMBL; AL713657; CAD28466.1; -; mRNA.
CCDS; CCDS32782.1; -.
PIR; JC7595; JC7595.
RefSeq; NP_569057.1; NM_130386.2.
UniGene; Hs.464422; -.
PDB; 2OX8; X-ray; 2.50 A; A/B/C/D=607-742.
PDBsum; 2OX8; -.
ProteinModelPortal; Q5KU26; -.
SMR; Q5KU26; -.
BioGrid; 123353; 38.
IntAct; Q5KU26; 1.
STRING; 9606.ENSP00000383115; -.
UniLectin; Q5KU26; -.
iPTMnet; Q5KU26; -.
PhosphoSitePlus; Q5KU26; -.
BioMuta; COLEC12; -.
DMDM; 296439391; -.
MaxQB; Q5KU26; -.
PaxDb; Q5KU26; -.
PeptideAtlas; Q5KU26; -.
PRIDE; Q5KU26; -.
ProteomicsDB; 63550; -.
DNASU; 81035; -.
Ensembl; ENST00000400256; ENSP00000383115; ENSG00000158270.
GeneID; 81035; -.
KEGG; hsa:81035; -.
UCSC; uc002kkm.4; human.
CTD; 81035; -.
DisGeNET; 81035; -.
EuPathDB; HostDB:ENSG00000158270.11; -.
GeneCards; COLEC12; -.
HGNC; HGNC:16016; COLEC12.
HPA; HPA047917; -.
HPA; HPA071056; -.
MIM; 607621; gene.
neXtProt; NX_Q5KU26; -.
OpenTargets; ENSG00000158270; -.
PharmGKB; PA26738; -.
eggNOG; ENOG410IIUI; Eukaryota.
eggNOG; ENOG41101BT; LUCA.
GeneTree; ENSGT00820000126981; -.
HOGENOM; HOG000111886; -.
HOVERGEN; HBG107745; -.
InParanoid; Q5KU26; -.
KO; K10062; -.
OMA; TQCTKCK; -.
OrthoDB; EOG091G0OLC; -.
PhylomeDB; Q5KU26; -.
TreeFam; TF332426; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
ChiTaRS; COLEC12; human.
EvolutionaryTrace; Q5KU26; -.
GenomeRNAi; 81035; -.
PRO; PR:Q5KU26; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000158270; Expressed in 219 organ(s), highest expression level in tendon.
CleanEx; HS_CLP1; -.
CleanEx; HS_COLEC12; -.
Genevisible; Q5KU26; HS.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005534; F:galactose binding; NAS:UniProtKB.
GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005044; F:scavenger receptor activity; TAS:UniProtKB.
GO; GO:0008329; F:signaling pattern recognition receptor activity; IDA:UniProtKB.
GO; GO:0009756; P:carbohydrate mediated signaling; NAS:UniProtKB.
GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB.
GO; GO:0006952; P:defense response; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0006910; P:phagocytosis, recognition; IDA:UniProtKB.
GO; GO:0060355; P:positive regulation of cell adhesion molecule production; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; NAS:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IMP:UniProtKB.
CDD; cd03590; CLECT_DC-SIGN_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR033989; CD209-like_CTLD.
InterPro; IPR008160; Collagen.
InterPro; IPR016187; CTDL_fold.
Pfam; PF01391; Collagen; 2.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
3D-structure; Calcium; Coiled coil; Collagen; Complete proteome;
Disulfide bond; Glycoprotein; Lectin; Membrane; Metal-binding;
Polymorphism; Receptor; Reference proteome; Repeat; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 742 Collectin-12.
/FTId=PRO_0000318681.
TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.
TRANSMEM 38 58 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 59 742 Extracellular. {ECO:0000255}.
DOMAIN 443 472 Collagen-like 1.
DOMAIN 473 529 Collagen-like 2.
DOMAIN 530 589 Collagen-like 3.
DOMAIN 614 731 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
COILED 73 141 {ECO:0000255}.
COILED 215 328 {ECO:0000255}.
METAL 644 644 Calcium 1; via carbonyl oxygen.
METAL 646 646 Calcium 1.
METAL 650 650 Calcium 1.
METAL 670 670 Calcium 2.
METAL 674 674 Calcium 2.
METAL 694 694 Calcium 3.
METAL 696 696 Calcium 3.
METAL 697 697 Calcium 2.
METAL 706 706 Calcium 2; via carbonyl oxygen.
METAL 706 706 Calcium 3.
METAL 707 707 Calcium 2.
METAL 718 718 Calcium 3.
METAL 719 719 Calcium 3.
METAL 731 731 Calcium 1.
BINDING 691 691 Carbohydrate. {ECO:0000250}.
BINDING 694 694 Carbohydrate. {ECO:0000250}.
BINDING 696 696 Carbohydrate. {ECO:0000250}.
BINDING 706 706 Carbohydrate. {ECO:0000250}.
BINDING 718 718 Carbohydrate. {ECO:0000250}.
BINDING 719 719 Carbohydrate; via carbonyl oxygen.
{ECO:0000250}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 607 618 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:17420244}.
DISULFID 635 730 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:17420244}.
DISULFID 708 722 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:17420244}.
VARIANT 91 91 K -> E (in dbSNP:rs17855029).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_038853.
VARIANT 487 487 I -> V (in dbSNP:rs8098850).
/FTId=VAR_038854.
VARIANT 522 522 S -> P (in dbSNP:rs2305025).
{ECO:0000269|PubMed:11162630,
ECO:0000269|PubMed:11564734,
ECO:0000269|PubMed:12601552,
ECO:0000269|PubMed:12761161,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_038855.
VARIANT 606 606 G -> S (in dbSNP:rs2305027).
{ECO:0000269|PubMed:11162630,
ECO:0000269|PubMed:12601552,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_038856.
CONFLICT 12 12 Q -> P (in Ref. 1; BAB39148).
{ECO:0000305}.
CONFLICT 16 16 Y -> F (in Ref. 1; BAB39148).
{ECO:0000305}.
CONFLICT 22 22 Q -> H (in Ref. 1; BAB39148).
{ECO:0000305}.
CONFLICT 28 28 T -> P (in Ref. 1; BAB39148).
{ECO:0000305}.
CONFLICT 31 31 K -> H (in Ref. 1; BAB39148).
{ECO:0000305}.
CONFLICT 72 72 M -> V (in Ref. 3; BAD83592).
{ECO:0000305}.
STRAND 612 614 {ECO:0000244|PDB:2OX8}.
STRAND 617 621 {ECO:0000244|PDB:2OX8}.
HELIX 628 637 {ECO:0000244|PDB:2OX8}.
HELIX 648 657 {ECO:0000244|PDB:2OX8}.
STRAND 664 669 {ECO:0000244|PDB:2OX8}.
STRAND 671 673 {ECO:0000244|PDB:2OX8}.
TURN 692 700 {ECO:0000244|PDB:2OX8}.
STRAND 708 711 {ECO:0000244|PDB:2OX8}.
STRAND 717 720 {ECO:0000244|PDB:2OX8}.
STRAND 726 733 {ECO:0000244|PDB:2OX8}.
SEQUENCE 742 AA; 81515 MW; 85A003C1D6A83949 CRC64;
MKDDFAEEEE VQSFGYKRFG IQEGTQCTKC KNNWALKFSI ILLYILCALL TITVAILGYK
VVEKMDNVTG GMETSRQTYD DKLTAVESDL KKLGDQTGKK AISTNSELST FRSDILDLRQ
QLREITEKTS KNKDTLEKLQ ASGDALVDRQ SQLKETLENN SFLITTVNKT LQAYNGYVTN
LQQDTSVLQG NLQNQMYSHN VVIMNLNNLN LTQVQQRNLI TNLQRSVDDT SQAIQRIKND
FQNLQQVFLQ AKKDTDWLKE KVQSLQTLAA NNSALAKANN DTLEDMNSQL NSFTGQMENI
TTISQANEQN LKDLQDLHKD AENRTAIKFN QLEERFQLFE TDIVNIISNI SYTAHHLRTL
TSNLNEVRTT CTDTLTKHTD DLTSLNNTLA NIRLDSVSLR MQQDLMRSRL DTEVANLSVI
MEEMKLVDSK HGQLIKNFTI LQGPPGPRGP RGDRGSQGPP GPTGNKGQKG EKGEPGPPGP
AGERGPIGPA GPPGERGGKG SKGSQGPKGS RGSPGKPGPQ GSSGDPGPPG PPGKEGLPGP
QGPPGFQGLQ GTVGEPGVPG PRGLPGLPGV PGMPGPKGPP GPPGPSGAVV PLALQNEPTP
APEDNGCPPH WKNFTDKCYY FSVEKEIFED AKLFCEDKSS HLVFINTREE QQWIKKQMVG
RESHWIGLTD SERENEWKWL DGTSPDYKNW KAGQPDNWGH GHGPGEDCAG LIYAGQWNDF
QCEDVNNFIC EKDRETVLSS AL


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