C209B_MOUSE
ID C209B_MOUSE Reviewed; 325 AA.
AC Q8CJ91; Q8BGZ0; Q8BHK7; Q8CJ86; Q8CJ87; Q8CJ88; Q8CJ89; Q8CJ90; Q8CJ92;
AC Q8CJ93; Q8CJ94; Q91ZW4; Q91ZX0; Q9D8V4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=CD209 antigen-like protein B;
DE AltName: Full=DC-SIGN-related protein 1;
DE Short=DC-SIGNR1;
DE AltName: Full=OtB7;
DE AltName: CD_antigen=CD209;
GN Name=Cd209b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RX PubMed=11581173; DOI=10.1093/intimm/13.10.1283;
RA Park C.G., Takahara K., Umemoto E., Yashima Y., Matsubara K., Matsuda Y.,
RA Clausen B.E., Inaba K., Steinman R.M.;
RT "Five mouse homologues of the human dendritic cell C-type lectin, DC-
RT SIGN.";
RL Int. Immunol. 13:1283-1290(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND TISSUE
RP SPECIFICITY.
RC STRAIN=Swiss Webster; TISSUE=Skin, and Spleen;
RX PubMed=12137941; DOI=10.1016/s0378-1119(02)00722-9;
RA Parent S.A., Zhang T., Chrebet G., Clemas J.A., Figueroa D.J., Ky B.,
RA Blevins R.A., Austin C.P., Rosen H.;
RT "Molecular characterization of the murine SIGNR1 gene encoding a C-type
RT lectin homologous to human DC-SIGN and DC-SIGNR.";
RL Gene 293:33-46(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Lymph node;
RX PubMed=12351402; DOI=10.1182/blood-2002-04-1044;
RA Geijtenbeek T.B.H., Groot P.C., Nolte M.A., Van Vliet S.J.,
RA Gangaram-Panday S.T., Van Duijnhoven G.C.F., Kraal G.,
RA Van Oosterhout A.J.M., Van Kooyk Y.;
RT "Marginal zone macrophages express a murine homologue of DC-SIGN that
RT captures blood-borne antigens in vivo.";
RL Blood 100:2908-2916(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-325 (ISOFORM 1), AND INTERACTION WITH
RP HIV-1; HIV-2; SIV AND ICAM3.
RX PubMed=11581396; DOI=10.1128/jvi.75.21.10281-10289.2001;
RA Baribaud F., Pohlmann S., Sparwasser T., Kimata M.T., Choi Y.K.,
RA Haggarty B.S., Ahmad N., Macfarlan T., Edwards T.G., Leslie G.J.,
RA Arnason J., Reinhart T.A., Kimata J.T., Littman D.R., Hoxie J.A.,
RA Doms R.W.;
RT "Functional and antigenic characterization of human, rhesus macaque,
RT pigtailed macaque, and murine DC-SIGN.";
RL J. Virol. 75:10281-10289(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-325 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probable pathogen-recognition receptor. May mediate the
CC endocytosis of pathogens which are subsequently degraded in lysosomal
CC compartments. May recognize in a calcium-dependent manner high mannose
CC N-linked oligosaccharides in a variety of pathogen antigens. Is a
CC receptor for ICAM3, probably by binding to mannose-like carbohydrates.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=alpha;
CC IsoId=Q8CJ91-1; Sequence=Displayed;
CC Name=2; Synonyms=beta, TM-less;
CC IsoId=Q8CJ91-2; Sequence=VSP_010069;
CC Name=3; Synonyms=gamma;
CC IsoId=Q8CJ91-3; Sequence=VSP_010069, VSP_010070;
CC Name=4;
CC IsoId=Q8CJ91-4; Sequence=VSP_010068;
CC -!- TISSUE SPECIFICITY: Expressed in skin, spleen and lung, probably in a
CC subset of dendritic cells. Detected in spleen extrafollicular
CC paracortical areas including the red pulp and marginal zones, and at
CC lower levels, in the follicular area. Detected in skin suprabasal areas
CC adjacent to the epidermis and in epidermal cell layer.
CC {ECO:0000269|PubMed:12137941}.
CC -!- MISCELLANEOUS: In vitro, is a receptor for HIV-1, HIV-2 and SIV, but
CC does not transmit virus to permissive T-cells under the conditions
CC tested.
CC -!- CAUTION: In mouse, 5 genes homologous to human CD209/DC-SIGN and
CC CD209L/DC-SIGNR have been identified. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB25166.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=SIGNR1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_00131";
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DR EMBL; AF373409; AAL13235.1; -; mRNA.
DR EMBL; AF374471; AAL27540.1; -; mRNA.
DR EMBL; AF424790; AAN75585.1; -; mRNA.
DR EMBL; AF424791; AAN75586.1; -; mRNA.
DR EMBL; AF424792; AAN75587.1; -; mRNA.
DR EMBL; AF424793; AAN75588.1; -; mRNA.
DR EMBL; AF424794; AAN75589.1; -; mRNA.
DR EMBL; AF424795; AAN75590.1; -; mRNA.
DR EMBL; AF424797; AAN75592.1; -; mRNA.
DR EMBL; AF424798; AAN75593.1; -; mRNA.
DR EMBL; AF424796; AAN75591.1; -; mRNA.
DR EMBL; AF424799; AAN75594.1; -; mRNA.
DR EMBL; AF424800; AAN75595.1; -; mRNA.
DR EMBL; AF424801; AAN75596.1; -; mRNA.
DR EMBL; AF424802; AAN75597.1; -; mRNA.
DR EMBL; AF422108; AAN31450.1; -; mRNA.
DR EMBL; AK007656; BAB25166.1; ALT_INIT; mRNA.
DR CCDS; CCDS22076.1; -. [Q8CJ91-2]
DR CCDS; CCDS22077.1; -. [Q8CJ91-1]
DR CCDS; CCDS72089.1; -. [Q8CJ91-3]
DR RefSeq; NP_001032889.3; NM_001037800.3. [Q8CJ91-2]
DR RefSeq; NP_001274140.1; NM_001287211.1. [Q8CJ91-3]
DR RefSeq; NP_081248.4; NM_026972.5. [Q8CJ91-1]
DR PDB; 3ZHG; X-ray; 1.87 A; A/B/C=191-325, D=190-325.
DR PDB; 4C9F; X-ray; 2.60 A; A/B/C/D=191-323.
DR PDB; 4CAJ; X-ray; 2.19 A; A/B/C/D=191-325.
DR PDBsum; 3ZHG; -.
DR PDBsum; 4C9F; -.
DR PDBsum; 4CAJ; -.
DR AlphaFoldDB; Q8CJ91; -.
DR SMR; Q8CJ91; -.
DR DIP; DIP-61328N; -.
DR STRING; 10090.ENSMUSP00000081104; -.
DR UniLectin; Q8CJ91; -.
DR GlyGen; Q8CJ91; 3 sites.
DR PhosphoSitePlus; Q8CJ91; -.
DR MaxQB; Q8CJ91; -.
DR PaxDb; Q8CJ91; -.
DR PRIDE; Q8CJ91; -.
DR ProteomicsDB; 265263; -. [Q8CJ91-1]
DR ProteomicsDB; 265264; -. [Q8CJ91-2]
DR ProteomicsDB; 265265; -. [Q8CJ91-3]
DR ProteomicsDB; 265266; -. [Q8CJ91-4]
DR ABCD; Q8CJ91; 6 sequenced antibodies.
DR DNASU; 69165; -.
DR Ensembl; ENSMUST00000084086; ENSMUSP00000081104; ENSMUSG00000065987. [Q8CJ91-1]
DR Ensembl; ENSMUST00000171635; ENSMUSP00000126070; ENSMUSG00000065987. [Q8CJ91-2]
DR Ensembl; ENSMUST00000188386; ENSMUSP00000140695; ENSMUSG00000065987. [Q8CJ91-3]
DR GeneID; 69165; -.
DR KEGG; mmu:69165; -.
DR UCSC; uc009ksu.2; mouse. [Q8CJ91-1]
DR UCSC; uc009ksv.2; mouse. [Q8CJ91-2]
DR UCSC; uc012fyw.2; mouse. [Q8CJ91-3]
DR CTD; 69165; -.
DR MGI; MGI:1916415; Cd209b.
DR VEuPathDB; HostDB:ENSMUSG00000065987; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155012; -.
DR HOGENOM; CLU_049894_7_3_1; -.
DR InParanoid; Q8CJ91; -.
DR OMA; VLMNSTC; -.
DR PhylomeDB; Q8CJ91; -.
DR TreeFam; TF333341; -.
DR BioGRID-ORCS; 69165; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8CJ91; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8CJ91; protein.
DR Bgee; ENSMUSG00000065987; Expressed in peripheral lymph node and 43 other tissues.
DR ExpressionAtlas; Q8CJ91; baseline and differential.
DR Genevisible; Q8CJ91; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IDA:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030247; F:polysaccharide binding; IDA:MGI.
DR GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR GO; GO:0016045; P:detection of bacterium; IDA:MGI.
DR GO; GO:0001879; P:detection of yeast; IDA:MGI.
DR GO; GO:0006897; P:endocytosis; IDA:MGI.
DR GO; GO:0006910; P:phagocytosis, recognition; IDA:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
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; IPR016187; CTDL_fold.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Disulfide bond; Endocytosis;
KW Glycoprotein; Lectin; Mannose-binding; Membrane; Metal-binding; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..325
FT /note="CD209 antigen-like protein B"
FT /id="PRO_0000046605"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..325
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 201..316
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 195..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 223..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 294..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 1..183
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12137941"
FT /id="VSP_010068"
FT VAR_SEQ 45..74
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11581173,
FT ECO:0000303|PubMed:12137941"
FT /id="VSP_010069"
FT VAR_SEQ 275
FT /note="S -> SSRPRHAPISRGRPIYNMHSGR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12137941"
FT /id="VSP_010070"
FT CONFLICT 71
FT /note="I -> V (in Ref. 2; AAN75588)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="Q -> P (in Ref. 2; AAN75589)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="N -> D (in Ref. 2; AAN75586)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="M -> T (in Ref. 2; AAN75585)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="Q -> R (in Ref. 2; AAN75588)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="I -> V (in Ref. 2; AAN75586)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="V -> A (in Ref. 2; AAN75588)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="Q -> R (in Ref. 2; AAN75589)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="I -> T (in Ref. 2; AAN75587)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="S -> G (in Ref. 2; AAN75587)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="W -> R (in Ref. 2; AAN75589)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="E -> G (in Ref. 2; AAN75585)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="F -> L (in Ref. 2; AAN75597)"
FT /evidence="ECO:0000305"
FT CONFLICT 321..325
FT /note="PCTEG -> HA (in Ref. 2; AAN75590)"
FT /evidence="ECO:0000305"
FT CONFLICT 323..325
FT /note="TEG -> P (in Ref. 2; AAN75585/AAN75586/AAN75587/
FT AAN75588/AAN75589/AAN75591/AAN75592/AAN75593/AAN75594)"
FT /evidence="ECO:0000305"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3ZHG"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:3ZHG"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:3ZHG"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3ZHG"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:3ZHG"
FT STRAND 252..261
FT /evidence="ECO:0007829|PDB:3ZHG"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:3ZHG"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:3ZHG"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:3ZHG"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:3ZHG"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:3ZHG"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:3ZHG"
SQ 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
