CLC4K_MOUSE
ID CLC4K_MOUSE Reviewed; 331 AA.
AC Q8VBX4; Q8R442;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=C-type lectin domain family 4 member K;
DE AltName: Full=Langerin;
DE AltName: CD_antigen=CD207;
GN Name=Cd207; Synonyms=Clec4k;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=11777972; DOI=10.4049/jimmunol.168.2.782;
RA Valladeau J., Clair-Moninot V., Dezutter-Dambuyant C., Pin J.-J.,
RA Kissenpfennig A., Mattei M.-G., Ait-Yahia S., Bates E.E.M., Malissen B.,
RA Koch F., Fossiez F., Romani N., Lebecque S., Saeland S.;
RT "Identification of mouse langerin/CD207 in Langerhans cells and some
RT dendritic cells of lymphoid tissues.";
RL J. Immunol. 168:782-792(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=F1;
RA Takahara K., Omatsu Y., Umemoto E., Yashima Y., Matsubara K., Shimoyama S.,
RA Iyoda T., Matsuda Y., Inaba K.;
RT "Mouse langerin homologue: identification, expression pattern, and
RT chromosomal mapping of the cognate mouse and rat gene.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Riedl E., Wilson M., Udey M.C.;
RT "Cloning of mouse Langerin from fetal skin-derived dendritic cells.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [5]
RP FUNCTION.
RX PubMed=18322168; DOI=10.4049/jimmunol.180.6.3647;
RA Idoyaga J., Cheong C., Suda K., Suda N., Kim J.Y., Lee H., Park C.G.,
RA Steinman R.M.;
RT "Langerin/CD207 receptor on dendritic cells mediates efficient antigen
RT presentation on MHC I and II products in vivo.";
RL J. Immunol. 180:3647-3650(2008).
CC -!- FUNCTION: Calcium-dependent lectin displaying mannose-binding
CC specificity. Induces the formation of Birbeck granules (BGs); is a
CC potent regulator of membrane superimposition and zippering. Binds to
CC sulfated as well as mannosylated glycans, keratan sulfate (KS) and
CC beta-glucans. Facilitates uptake of antigens and is involved in the
CC routing and/or processing of antigen for presentation to T cells.
CC {ECO:0000269|PubMed:11777972, ECO:0000269|PubMed:18322168}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC Note=Found in Birbeck granules (BGs), which are organelles consisting
CC of superimposed and zippered membranes. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by Langerhans cells. Expressed in
CC dendritic cells and by scattered cells in lymph nodes and spleen. Also
CC detected in some non-lymphoid tissues such as lung, liver and heart.
CC {ECO:0000269|PubMed:11777972}.
CC -!- DOMAIN: The C-type lectin domain mediates dual recognition of both
CC sulfated and mannosylated glycans. {ECO:0000250}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Langerin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_360";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ302711; CAC82936.1; -; mRNA.
DR EMBL; AY026050; AAK01952.1; -; mRNA.
DR EMBL; AY078415; AAL83701.1; -; mRNA.
DR EMBL; AK142731; BAE25177.1; -; mRNA.
DR CCDS; CCDS39534.1; -.
DR RefSeq; NP_659192.2; NM_144943.3.
DR PDB; 5K8Y; X-ray; 2.40 A; A/B=194-331.
DR PDB; 5M62; X-ray; 1.70 A; A/B=194-331.
DR PDBsum; 5K8Y; -.
DR PDBsum; 5M62; -.
DR AlphaFoldDB; Q8VBX4; -.
DR SMR; Q8VBX4; -.
DR STRING; 10090.ENSMUSP00000040746; -.
DR UniLectin; Q8VBX4; -.
DR GlyGen; Q8VBX4; 2 sites.
DR iPTMnet; Q8VBX4; -.
DR PhosphoSitePlus; Q8VBX4; -.
DR MaxQB; Q8VBX4; -.
DR PaxDb; Q8VBX4; -.
DR PRIDE; Q8VBX4; -.
DR ProteomicsDB; 285470; -.
DR ABCD; Q8VBX4; 3 sequenced antibodies.
DR Antibodypedia; 2366; 504 antibodies from 36 providers.
DR DNASU; 246278; -.
DR Ensembl; ENSMUST00000037882; ENSMUSP00000040746; ENSMUSG00000034783.
DR GeneID; 246278; -.
DR KEGG; mmu:246278; -.
DR UCSC; uc009cnw.2; mouse.
DR CTD; 50489; -.
DR MGI; MGI:2180021; Cd207.
DR VEuPathDB; HostDB:ENSMUSG00000034783; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000161863; -.
DR HOGENOM; CLU_081746_0_0_1; -.
DR InParanoid; Q8VBX4; -.
DR OMA; QFCVSRN; -.
DR OrthoDB; 988771at2759; -.
DR PhylomeDB; Q8VBX4; -.
DR TreeFam; TF333341; -.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR BioGRID-ORCS; 246278; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q8VBX4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8VBX4; protein.
DR Bgee; ENSMUSG00000034783; Expressed in skin of external ear and 15 other tissues.
DR Genevisible; Q8VBX4; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IDA:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO: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; Coiled coil; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..331
FT /note="C-type lectin domain family 4 member K"
FT /id="PRO_0000223694"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 205..323
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT COILED 106..197
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 226..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 298..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 105
FT /note="V -> A (in Ref. 3; AAL83701)"
FT /evidence="ECO:0000305"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:5M62"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:5M62"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5M62"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:5M62"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:5M62"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:5M62"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:5M62"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:5M62"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:5M62"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:5M62"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:5M62"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:5M62"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:5M62"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:5M62"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:5M62"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:5M62"
SQ SEQUENCE 331 AA; 37621 MW; 3DFCFDB322CAB7E8 CRC64;
MPEAEMKEEA PEAHFTVDKQ NISLWPREPP PKQDLSPVLR KPLCICVAFT CLALVLVTSI
VLQAVFYPRL MGKILDVKSD AQMLKGRVDN ISTLGSDLKT ERGRVDDAEV QMQIVNTTLK
RVRSQILSLE TSMKIANDQL QILTMSWGEV DSLSAKIPEL KRDLDKASAL NTKVQGLQNS
LENVNKLLKQ QSDILEMVAR GWKYFSGNFY YFSRTPKTWY SAEQFCISRK AHLTSVSSES
EQKFLYKAAD GIPHWIGLTK AGSEGDWYWV DQTSFNKEQS RRFWIPGEPN NAGNNEHCAN
IRVSALKCWN DGPCDNTFLF ICKRPYVQTT E
