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CD209 antigen-like protein B (DC-SIGN-related protein 1) (DC-SIGNR1) (OtB7) (CD antigen CD209)

 C209B_MOUSE             Reviewed;         325 AA.
Q8CJ91; Q8BGZ0; Q8BHK7; Q8CJ86; Q8CJ87; Q8CJ88; Q8CJ89; Q8CJ90;
Q8CJ92; Q8CJ93; Q8CJ94; Q91ZW4; Q91ZX0; Q9D8V4;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 2.
12-SEP-2018, entry version 123.
RecName: Full=CD209 antigen-like protein B;
AltName: Full=DC-SIGN-related protein 1;
Short=DC-SIGNR1;
AltName: Full=OtB7;
AltName: CD_antigen=CD209;
Name=Cd209b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J;
PubMed=11581173; DOI=10.1093/intimm/13.10.1283;
Park C.G., Takahara K., Umemoto E., Yashima Y., Matsubara K.,
Matsuda Y., Clausen B.E., Inaba K., Steinman R.M.;
"Five mouse homologues of the human dendritic cell C-type lectin, DC-
SIGN.";
Int. Immunol. 13:1283-1290(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND TISSUE
SPECIFICITY.
STRAIN=Swiss Webster; TISSUE=Skin, and Spleen;
PubMed=12137941; DOI=10.1016/S0378-1119(02)00722-9;
Parent S.A., Zhang T., Chrebet G., Clemas J.A., Figueroa D.J., Ky B.,
Blevins R.A., Austin C.P., Rosen H.;
"Molecular characterization of the murine SIGNR1 gene encoding a C-
type lectin homologous to human DC-SIGN and DC-SIGNR.";
Gene 293:33-46(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Lymph node;
PubMed=12351402; DOI=10.1182/blood-2002-04-1044;
Geijtenbeek T.B.H., Groot P.C., Nolte M.A., Van Vliet S.J.,
Gangaram-Panday S.T., Van Duijnhoven G.C.F., Kraal G.,
Van Oosterhout A.J.M., Van Kooyk Y.;
"Marginal zone macrophages express a murine homologue of DC-SIGN that
captures blood-borne antigens in vivo.";
Blood 100:2908-2916(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-325 (ISOFORM 1), AND INTERACTION WITH
HIV-1; HIV-2; SIV AND ICAM3.
PubMed=11581396; DOI=10.1128/JVI.75.21.10281-10289.2001;
Baribaud F., Pohlmann S., Sparwasser T., Kimata M.T., Choi Y.K.,
Haggarty B.S., Ahmad N., Macfarlan T., Edwards T.G., Leslie G.J.,
Arnason J., Reinhart T.A., Kimata J.T., Littman D.R., Hoxie J.A.,
Doms R.W.;
"Functional and antigenic characterization of human, rhesus macaque,
pigtailed macaque, and murine DC-SIGN.";
J. Virol. 75:10281-10289(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-325 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Probable pathogen-recognition receptor. May mediate the
endocytosis of pathogens which are subsequently degraded in
lysosomal compartments. May recognize in a calcium-dependent
manner high mannose N-linked oligosaccharides in a variety of
pathogen antigens. Is a receptor for ICAM3, probably by binding to
mannose-like carbohydrates.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=alpha;
IsoId=Q8CJ91-1; Sequence=Displayed;
Name=2; Synonyms=beta, TM-less;
IsoId=Q8CJ91-2; Sequence=VSP_010069;
Name=3; Synonyms=gamma;
IsoId=Q8CJ91-3; Sequence=VSP_010069, VSP_010070;
Name=4;
IsoId=Q8CJ91-4; Sequence=VSP_010068;
-!- TISSUE SPECIFICITY: Expressed in skin, spleen and lung, probably
in a subset of dendritic cells. Detected in spleen extrafollicular
paracortical areas including the red pulp and marginal zones, and
at lower levels, in the follicular area. Detected in skin
suprabasal areas adjacent to the epidermis and in epidermal cell
layer. {ECO:0000269|PubMed:12137941}.
-!- MISCELLANEOUS: In vitro, is a receptor for HIV-1, HIV-2 and SIV,
but does not transmit virus to permissive T-cells under the
conditions tested.
-!- CAUTION: In mouse, 5 genes homologous to human CD209/DC-SIGN and
CD209L/DC-SIGNR have been identified. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB25166.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=SIGNR1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_00131";
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EMBL; AF373409; AAL13235.1; -; mRNA.
EMBL; AF374471; AAL27540.1; -; mRNA.
EMBL; AF424790; AAN75585.1; -; mRNA.
EMBL; AF424791; AAN75586.1; -; mRNA.
EMBL; AF424792; AAN75587.1; -; mRNA.
EMBL; AF424793; AAN75588.1; -; mRNA.
EMBL; AF424794; AAN75589.1; -; mRNA.
EMBL; AF424795; AAN75590.1; -; mRNA.
EMBL; AF424797; AAN75592.1; -; mRNA.
EMBL; AF424798; AAN75593.1; -; mRNA.
EMBL; AF424796; AAN75591.1; -; mRNA.
EMBL; AF424799; AAN75594.1; -; mRNA.
EMBL; AF424800; AAN75595.1; -; mRNA.
EMBL; AF424801; AAN75596.1; -; mRNA.
EMBL; AF424802; AAN75597.1; -; mRNA.
EMBL; AF422108; AAN31450.1; -; mRNA.
EMBL; AK007656; BAB25166.1; ALT_INIT; mRNA.
CCDS; CCDS22076.1; -. [Q8CJ91-2]
CCDS; CCDS22077.1; -. [Q8CJ91-1]
CCDS; CCDS72089.1; -. [Q8CJ91-3]
RefSeq; NP_001032889.3; NM_001037800.3. [Q8CJ91-2]
RefSeq; NP_001274140.1; NM_001287211.1. [Q8CJ91-3]
RefSeq; NP_081248.4; NM_026972.5. [Q8CJ91-1]
UniGene; Mm.175163; -.
PDB; 3ZHG; X-ray; 1.87 A; A/B/C=191-325, D=190-325.
PDB; 4C9F; X-ray; 2.60 A; A/B/C/D=191-323.
PDB; 4CAJ; X-ray; 2.19 A; A/B/C/D=191-325.
PDBsum; 3ZHG; -.
PDBsum; 4C9F; -.
PDBsum; 4CAJ; -.
ProteinModelPortal; Q8CJ91; -.
SMR; Q8CJ91; -.
DIP; DIP-61328N; -.
STRING; 10090.ENSMUSP00000081104; -.
UniLectin; Q8CJ91; -.
PhosphoSitePlus; Q8CJ91; -.
PaxDb; Q8CJ91; -.
PRIDE; Q8CJ91; -.
DNASU; 69165; -.
Ensembl; ENSMUST00000084086; ENSMUSP00000081104; ENSMUSG00000065987. [Q8CJ91-1]
Ensembl; ENSMUST00000171635; ENSMUSP00000126070; ENSMUSG00000065987. [Q8CJ91-2]
Ensembl; ENSMUST00000188386; ENSMUSP00000140695; ENSMUSG00000065987. [Q8CJ91-3]
GeneID; 69165; -.
KEGG; mmu:69165; -.
UCSC; uc009ksu.2; mouse. [Q8CJ91-1]
UCSC; uc009ksv.2; mouse. [Q8CJ91-2]
UCSC; uc012fyw.2; mouse. [Q8CJ91-3]
CTD; 69165; -.
MGI; MGI:1916415; Cd209b.
eggNOG; ENOG410IS3Z; Eukaryota.
eggNOG; ENOG410YSMB; LUCA.
GeneTree; ENSGT00760000118924; -.
HOVERGEN; HBG050992; -.
InParanoid; Q8CJ91; -.
KO; K06563; -.
OMA; NLAKFWI; -.
OrthoDB; EOG091G0G9W; -.
PhylomeDB; Q8CJ91; -.
TreeFam; TF333341; -.
Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-MMU-8851680; Butyrophilin (BTN) family interactions.
PRO; PR:Q8CJ91; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000065987; Expressed in 48 organ(s), highest expression level in mesenteric lymph node.
CleanEx; MM_CD209B; -.
ExpressionAtlas; Q8CJ91; baseline and differential.
Genevisible; Q8CJ91; MM.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; TAS:MGI.
GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IDA:MGI.
GO; GO:0005537; F:mannose binding; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030247; F:polysaccharide binding; IDA:MGI.
GO; GO:0016045; P:detection of bacterium; IDA:MGI.
GO; GO:0001879; P:detection of yeast; IDA:MGI.
GO; GO:0006897; P:endocytosis; IDA:MGI.
GO; GO:0006910; P:phagocytosis, recognition; IDA:MGI.
GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IDA:MGI.
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; IPR016187; CTDL_fold.
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; Alternative splicing; Calcium; Complete proteome;
Disulfide bond; Endocytosis; Glycoprotein; Lectin; Mannose-binding;
Membrane; Metal-binding; Receptor; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 325 CD209 antigen-like protein B.
/FTId=PRO_0000046605.
TOPO_DOM 1 52 Cytoplasmic. {ECO:0000255}.
TRANSMEM 53 73 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 74 325 Extracellular. {ECO:0000255}.
DOMAIN 201 316 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
METAL 285 285 Calcium. {ECO:0000250}.
METAL 287 287 Calcium. {ECO:0000250}.
METAL 289 289 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 292 292 Calcium. {ECO:0000250}.
METAL 303 303 Calcium. {ECO:0000250}.
METAL 304 304 Calcium. {ECO:0000250}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 195 206 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 223 315 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 294 307 {ECO:0000255|PROSITE-ProRule:PRU00040}.
VAR_SEQ 1 183 Missing (in isoform 4).
{ECO:0000303|PubMed:12137941}.
/FTId=VSP_010068.
VAR_SEQ 45 74 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:11581173,
ECO:0000303|PubMed:12137941}.
/FTId=VSP_010069.
VAR_SEQ 275 275 S -> SSRPRHAPISRGRPIYNMHSGR (in isoform
3). {ECO:0000303|PubMed:12137941}.
/FTId=VSP_010070.
CONFLICT 71 71 I -> V (in Ref. 2; AAN75588).
{ECO:0000305}.
CONFLICT 87 87 Q -> P (in Ref. 2; AAN75589).
{ECO:0000305}.
CONFLICT 112 112 N -> D (in Ref. 2; AAN75586).
{ECO:0000305}.
CONFLICT 124 124 M -> T (in Ref. 2; AAN75585).
{ECO:0000305}.
CONFLICT 138 138 Q -> R (in Ref. 2; AAN75588).
{ECO:0000305}.
CONFLICT 163 163 I -> V (in Ref. 2; AAN75586).
{ECO:0000305}.
CONFLICT 226 226 V -> A (in Ref. 2; AAN75588).
{ECO:0000305}.
CONFLICT 229 229 Q -> R (in Ref. 2; AAN75589).
{ECO:0000305}.
CONFLICT 232 232 I -> T (in Ref. 2; AAN75587).
{ECO:0000305}.
CONFLICT 235 235 S -> G (in Ref. 2; AAN75587).
{ECO:0000305}.
CONFLICT 267 267 W -> R (in Ref. 2; AAN75589).
{ECO:0000305}.
CONFLICT 308 308 E -> G (in Ref. 2; AAN75585).
{ECO:0000305}.
CONFLICT 312 312 F -> L (in Ref. 2; AAN75597).
{ECO:0000305}.
CONFLICT 321 325 PCTEG -> HA (in Ref. 2; AAN75590).
{ECO:0000305}.
CONFLICT 323 325 TEG -> P (in Ref. 2; AAN75585/AAN75586/
AAN75587/AAN75588/AAN75589/AAN75591/
AAN75592/AAN75593/AAN75594).
{ECO:0000305}.
STRAND 200 202 {ECO:0000244|PDB:3ZHG}.
STRAND 205 209 {ECO:0000244|PDB:3ZHG}.
HELIX 216 224 {ECO:0000244|PDB:3ZHG}.
TURN 225 227 {ECO:0000244|PDB:3ZHG}.
HELIX 236 249 {ECO:0000244|PDB:3ZHG}.
STRAND 252 261 {ECO:0000244|PDB:3ZHG}.
STRAND 264 267 {ECO:0000244|PDB:3ZHG}.
HELIX 275 280 {ECO:0000244|PDB:3ZHG}.
TURN 289 291 {ECO:0000244|PDB:3ZHG}.
STRAND 294 298 {ECO:0000244|PDB:3ZHG}.
STRAND 301 305 {ECO:0000244|PDB:3ZHG}.
STRAND 311 318 {ECO:0000244|PDB:3ZHG}.
SEQUENCE 325 AA; 37112 MW; 9C9388407C247CA4 CRC64;
MSDSTEAKMQ PLSSMDDDEL MVSGSRYSIK SSRLRPNSGI KCLAGCSGHS QVPLVLQLLS
FLFLAGLLLI ILFQVSKTPN TERQKEQEKI LQELTQLTDE LTSRIPISQG KNESMQAKIT
EQLMQLKTEL LSRIPIFQGQ NESIQEKISE QLMQLKAELL SKISSFPVKD DSKQEKIYQQ
LVQMKTELFR LCRLCPWDWT FLLGNCYFFS KSQRNWNDAV TACKEVKAQL VIINSDEEQT
FLQQTSKAKG PTWMGLSDLK KEATWLWVDG STLSSRFQKY WNRGEPNNIG EEDCVEFAGD
GWNDSKCELK KFWICKKSAT PCTEG


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