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   24-JAN-2024, entry version 144.
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   GlyCosmos; Q8VBX4; 2 sites, No reported glycans.
DR   GlyGen; Q8VBX4; 2 sites.
DR   iPTMnet; Q8VBX4; -.
DR   PhosphoSitePlus; Q8VBX4; -.
DR   MaxQB; Q8VBX4; -.
DR   PaxDb; 10090-ENSMUSP00000040746; -.
DR   ProteomicsDB; 285470; -.
DR   ABCD; Q8VBX4; 3 sequenced antibodies.
DR   Antibodypedia; 2366; 577 antibodies from 36 providers.
DR   DNASU; 246278; -.
DR   Ensembl; ENSMUST00000037882.8; ENSMUSP00000040746.7; ENSMUSG00000034783.8.
DR   GeneID; 246278; -.
DR   KEGG; mmu:246278; -.
DR   UCSC; uc009cnw.2; mouse.
DR   AGR; MGI:2180021; -.
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; 5257739at2759; -.
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 78 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 cell types or tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C: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; 1.20.5.170; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR22802:SF14; C-TYPE LECTIN DOMAIN FAMILY 4 MEMBER K; 1.
DR   PANTHER; PTHR22802; C-TYPE LECTIN SUPERFAMILY MEMBER; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF58100; Bacterial hemolysins; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   Genevisible; Q8VBX4; MM.
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
//