ID CD302_HUMAN Reviewed; 232 AA. AC Q8IX05; A8K5G4; B4E2T9; Q15009; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 02-SEP-2026, entry version 163. DE RecName: Full=CD302 antigen; DE AltName: Full=C-type lectin BIMLEC; DE AltName: Full=C-type lectin domain family 13 member A; DE AltName: Full=DEC205-associated C-type lectin 1; DE AltName: Full=Type I transmembrane C-type lectin receptor DCL-1; DE AltName: CD_antigen=CD302; DE Flags: Precursor; GN Name=CD302; Synonyms=CLEC13A, DCL1, KIAA0022; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE SPECIFICITY. RX PubMed=12824192; DOI=10.1074/jbc.m303112200; RA Kato M., Khan S., Gonzalez N., O'Neill B.P., McDonald K.J., Cooper B.J., RA Angel N.Z., Hart D.N.J.; RT "Hodgkin's lymphoma cell lines express a fusion protein encoded by RT intergenically spliced mRNA for the multilectin receptor DEC-205 (CD205) RT and a novel C-type lectin receptor DCL-1."; RL J. Biol. Chem. 278:34035-34041(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Begum N.A.; RT "Identification of a novel C-type lectin, BIMLEC, from BCG cell wall RT induced monocyte."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5). RC TISSUE=Teratocarcinoma, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-232 (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., RA Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. The RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of RT randomly sampled cDNA clones from human immature myeloid cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-232 (ISOFORM 1). RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, RP AND GLYCOSYLATION. RX PubMed=17947679; DOI=10.4049/jimmunol.179.9.6052; RA Kato M., Khan S., d'Aniello E., McDonald K.J., Hart D.N.; RT "The novel endocytic and phagocytic C-Type lectin receptor DCL-1/CD302 on RT macrophages is colocalized with F-actin, suggesting a role in cell adhesion RT and migration."; RL J. Immunol. 179:6052-6063(2007). RN [8] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=27316686; DOI=10.4049/jimmunol.1600259; RA Lo T.H., Silveira P.A., Fromm P.D., Verma N.D., Vu P.A., Kupresanin F., RA Adam R., Kato M., Cogger V.C., Clark G.J., Hart D.N.; RT "Characterization of the Expression and Function of the C-Type Lectin RT Receptor CD302 in Mice and Humans Reveals a Role in Dendritic Cell RT Migration."; RL J. Immunol. 197:885-898(2016). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=35297672; DOI=10.1128/jvi.01995-21; RA Reinecke B., Frericks N., Lauber C., Dinkelborg K., Matthaei A., RA Vondran F.W.R., Behrendt P., Haid S., Brown R.J.P., Pietschmann T.; RT "The Human Liver-Expressed Lectin CD302 Restricts Hepatitis C Virus RT Infection."; RL J. Virol. 96:e0199521-e0199521(2022). RN [10] RP STRUCTURE BY NMR OF 23-161. RX PubMed=26725057; DOI=10.1007/s12104-015-9664-5; RA Pospisilova E., Kavan D., Novak P., Chmelik J.; RT "1H, 13C and 15N resonance assignments of human DCL-1 (CD302) extracellular RT domain."; RL Biomol. NMR. Assign. 10:189-192(2016). CC -!- FUNCTION: Multifunctional C-type lectin receptor involved in CC endocytosis, phagocytosis and regulation of cell adhesion and migration CC (PubMed:17947679, PubMed:27316686). Plays a critical role in guiding CC dendritic cells to lymph nodes (PubMed:27316686). Also functions as a CC restriction factor for Hepatitis C virus (HCV) at the liver cell CC surface, likely by inhibiting a viral cell entry step CC (PubMed:35297672). {ECO:0000269|PubMed:17947679, CC ECO:0000269|PubMed:27316686, ECO:0000269|PubMed:35297672}. CC -!- INTERACTION: CC Q8IX05; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-14259393, EBI-11343438; CC Q8IX05; P19397: CD53; NbExp=3; IntAct=EBI-14259393, EBI-6657396; CC Q8IX05; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-14259393, EBI-781551; CC Q8IX05; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-14259393, EBI-12142257; CC Q8IX05; O00258: GET1; NbExp=3; IntAct=EBI-14259393, EBI-18908258; CC Q8IX05; Q8TED1: GPX8; NbExp=3; IntAct=EBI-14259393, EBI-11721746; CC Q8IX05; P38484: IFNGR2; NbExp=3; IntAct=EBI-14259393, EBI-3905457; CC Q8IX05; Q13651: IL10RA; NbExp=3; IntAct=EBI-14259393, EBI-1031656; CC Q8IX05; P16871: IL7R; NbExp=3; IntAct=EBI-14259393, EBI-80490; CC Q8IX05; P35372-10: OPRM1; NbExp=3; IntAct=EBI-14259393, EBI-12807478; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35297672}; CC Single-pass type I membrane protein {ECO:0000305}. Cell projection, CC filopodium {ECO:0000269|PubMed:17947679}. Cytoplasm, cell cortex CC {ECO:0000269|PubMed:17947679}. Cell projection, microvillus CC {ECO:0000269|PubMed:17947679}. Note=Colocalizes with F-actin in CC filopodia, cellular cortex and microvilli of the apical cell surface. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q8IX05-1; Sequence=Displayed; CC Name=4; CC IsoId=O60449-1; Sequence=External; CC Name=5; CC IsoId=Q8IX05-2; Sequence=VSP_044258, VSP_044259; CC Name=2; Synonyms=Fusion protein variant V34-2; CC IsoId=O60449-2; Sequence=External; CC Name=3; Synonyms=Fusion protein variant V33-2; CC IsoId=O60449-3; Sequence=External; CC -!- TISSUE SPECIFICITY: Expressed at moderate levels in monocytes, myeloid CC blood dendritic cells and granulocytes and at low levels in CC plasmacytoid blood dendritic cells, monocyte-derived macrophages and CC monocyte-derived dendritic cells, with no expression detected in T- CC lymphocytes, B-lymphocytes and natural killer cells (at protein level). CC Expressed widely in different tissues, with highest expression levels CC in liver, lung, peripheral blood leukocytes and spleen, and lowest CC levels in neuronal tissues, skeletal muscle and ovary. Isoform 2 and CC isoform 3 are expressed in malignant Hodgkin lymphoma cells called CC Hodgkin and Reed-Sternberg (HRS) cells. {ECO:0000269|PubMed:12824192, CC ECO:0000269|PubMed:17947679, ECO:0000269|PubMed:27316686, CC ECO:0000269|PubMed:35297672}. CC -!- DEVELOPMENTAL STAGE: Expressed at relatively high levels in fetal lung, CC liver, spleen and kidney with lower expression levels detected in CC heart, thymus and brain. {ECO:0000269|PubMed:17947679}. CC -!- PTM: May be heterogeneously N-glycosylated in some cell types. CC {ECO:0000269|PubMed:17947679}. CC -!- MISCELLANEOUS: Isoform 2 and isoform 3 are produced in HRS cells by a CC transcriptional control mechanism which cotranscribe an mRNA containing CC LY75 and CD302 prior to generating the intergenically spliced mRNA to CC produce LY75/CD302 fusion proteins. CC -!- MISCELLANEOUS: [Isoform 1]: Produced by intergenic splicing of LY75 and CC CD302. 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; AY314007; AAP79900.1; -; mRNA. DR EMBL; AF499000; AAN77050.1; -; mRNA. DR EMBL; AK291279; BAF83968.1; -; mRNA. DR EMBL; AK304422; BAG65251.1; -; mRNA. DR EMBL; AC009961; AAY14942.1; -; Genomic_DNA. DR EMBL; D14664; BAA03498.1; -; mRNA. DR EMBL; BC020646; AAH20646.1; -; mRNA. DR CCDS; CCDS33308.1; -. [Q8IX05-1] DR CCDS; CCDS56139.1; -. [Q8IX05-2] DR RefSeq; NP_001185692.1; NM_001198763.2. [Q8IX05-2] DR RefSeq; NP_055695.2; NM_014880.5. [Q8IX05-1] DR PDB; 2NAN; NMR; -; A=23-161. DR AlphaFoldDB; Q8IX05; -. DR SMR; Q8IX05; -. DR BioGRID; 115262; 17. DR FunCoup; Q8IX05; 111. DR IntAct; Q8IX05; 12. DR STRING; 9606.ENSP00000259053; -. DR UniLectin; Q8IX05; -. DR GlyCosmos; Q8IX05; 1 site, No reported glycans. DR GlyGen; Q8IX05; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q8IX05; -. DR PhosphoSitePlus; Q8IX05; -. DR BioMuta; CD302; -. DR DMDM; 74750720; -. DR jPOST; Q8IX05; -. DR MassIVE; Q8IX05; -. DR PaxDb; 9606-ENSP00000259053; -. DR PeptideAtlas; Q8IX05; -. DR Pumba; Q8IX05; -. DR Antibodypedia; 47602; 238 antibodies from 30 providers. DR DNASU; 9936; -. DR Ensembl; ENST00000259053.6; ENSP00000259053.4; ENSG00000241399.8. [Q8IX05-1] DR Ensembl; ENST00000429078.6; ENSP00000394301.2; ENSG00000241399.8. [Q8IX05-2] DR GeneID; 9936; -. DR KEGG; hsa:9936; -. DR MANE-Select; ENST00000259053.6; ENSP00000259053.4; NM_014880.5; NP_055695.2. DR UCSC; uc002uba.4; human. [Q8IX05-1] DR AGR; HGNC:30843; -. DR ClinPGx; PA142672141; -. DR CTD; 9936; -. DR DisGeNET; 9936; -. DR GeneCards; CD302; -. DR HGNC; HGNC:30843; CD302. DR HPA; ENSG00000241399; Tissue enhanced (liver). DR MIM; 612246; gene. DR OpenTargets; ENSG00000241399; -. DR VEuPathDB; HostDB:ENSG00000241399; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT01150000286973; -. DR HOGENOM; CLU_088281_0_0_1; -. DR InParanoid; Q8IX05; -. DR OMA; RWENVSC; -. DR OrthoDB; 9945342at2759; -. DR PAN-GO; Q8IX05; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q8IX05; -. DR PathwayCommons; Q8IX05; -. DR SignaLink; Q8IX05; -. DR Agora; ENSG00000241399; -. DR BioGRID-ORCS; 9936; 6 hits in 1143 CRISPR screens. DR GeneWiki; CD302; -. DR GenomeRNAi; 9936; -. DR Pharos; Q8IX05; Tbio. DR PRO; PR:Q8IX05; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8IX05; protein. DR Bgee; ENSG00000241399; Expressed in lower lobe of lung and 204 other cell types or tissues. DR ExpressionAtlas; Q8IX05; baseline and differential. DR GO; GO:0005938; C:cell cortex; IDA:MGI. DR GO; GO:0030175; C:filopodium; IDA:MGI. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0006909; P:phagocytosis; IDA:MGI. DR CDD; cd00037; CLECT; 1. DR FunFam; 3.10.100.10:FF:000082; CD302 antigen isoform X2; 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; IPR050111; C-type_lectin/snaclec_domain. DR InterPro; IPR016187; CTDL_fold. DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1. DR Pfam; PF00059; Lectin_C; 1. DR SMART; SM00034; CLECT; 1. DR SUPFAM; SSF56436; C-type lectin-like; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. DR PDBsum; 2NAN; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; KW Cytoplasm; Disulfide bond; Glycoprotein; Lectin; Membrane; KW Proteomics identification; Receptor; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..232 FT /note="CD302 antigen" FT /id="PRO_0000252332" FT TOPO_DOM 23..168 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 169..189 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 190..232 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 32..152 FT /note="C-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT CARBOHYD 109 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 128..143 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT VAR_SEQ 99..156 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044258" FT VAR_SEQ 157 FT /note="I -> V (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044259" FT VARIANT 200 FT /note="R -> S (in dbSNP:rs34068933)" FT /id="VAR_050101" FT CONFLICT 139 FT /note="K -> R (in Ref. 3; BAF83968)" FT /evidence="ECO:0000305" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:2NAN" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:2NAN" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:2NAN" FT HELIX 49..57 FT /evidence="ECO:0007829|PDB:2NAN" FT TURN 58..60 FT /evidence="ECO:0007829|PDB:2NAN" FT HELIX 69..82 FT /evidence="ECO:0007829|PDB:2NAN" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:2NAN" FT STRAND 92..96 FT /evidence="ECO:0007829|PDB:2NAN" FT TURN 97..100 FT /evidence="ECO:0007829|PDB:2NAN" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:2NAN" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:2NAN" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:2NAN" FT STRAND 151..156 FT /evidence="ECO:0007829|PDB:2NAN" SQ SEQUENCE 232 AA; 26183 MW; 5C33C708345C3971 CRC64; MLRAALPALL LPLLGLAAAA VADCPSSTWI QFQDSCYIFL QEAIKVESIE DVRNQCTDHG ADMISIHNEE ENAFILDTLK KQWKGPDDIL LGMFYDTDDA SFKWFDNSNM TFDKWTDQDD DEDLVDTCAF LHIKTGEWKK GNCEVSSVEG TLCKTAIPYK RKYLSDNHIL ISALVIASTV ILTVLGAIIW FLYKKHSDSR FTTVFSTAPQ SPYNEDCVLV VGEENEYPVQ FD //