CD302_HUMAN
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 03-AUG-2022, entry version 146.
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 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: Potential multifunctional C-type lectin receptor that may
CC play roles in endocytosis and phagocytosis as well as in cell adhesion
CC and migration. {ECO:0000269|PubMed:17947679}.
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: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell projection, filopodium
CC {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 ma crophages 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}.
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.
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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_001198763.1. [Q8IX05-2]
DR RefSeq; NP_055695.2; NM_014880.4. [Q8IX05-1]
DR PDB; 2NAN; NMR; -; A=23-161.
DR PDBsum; 2NAN; -.
DR AlphaFoldDB; Q8IX05; -.
DR SMR; Q8IX05; -.
DR BioGRID; 115262; 16.
DR IntAct; Q8IX05; 12.
DR STRING; 9606.ENSP00000259053; -.
DR GlyGen; Q8IX05; 1 site.
DR iPTMnet; Q8IX05; -.
DR PhosphoSitePlus; Q8IX05; -.
DR BioMuta; CD302; -.
DR DMDM; 74750720; -.
DR jPOST; Q8IX05; -.
DR MassIVE; Q8IX05; -.
DR MaxQB; Q8IX05; -.
DR PaxDb; Q8IX05; -.
DR PeptideAtlas; Q8IX05; -.
DR PRIDE; Q8IX05; -.
DR Antibodypedia; 47602; 245 antibodies from 28 providers.
DR DNASU; 9936; -.
DR Ensembl; ENST00000259053.6; ENSP00000259053.4; ENSG00000241399.7. [Q8IX05-1]
DR Ensembl; ENST00000429078.6; ENSP00000394301.2; ENSG00000241399.7. [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 CTD; 9936; -.
DR DisGeNET; 9936; -.
DR GeneCards; CD302; -.
DR HGNC; HGNC:30843; CD302.
DR HPA; ENSG00000241399; Tissue enhanced (liver).
DR MIM; 612246; gene.
DR neXtProt; NX_Q8IX05; -.
DR OpenTargets; ENSG00000241399; -.
DR PharmGKB; PA142672141; -.
DR VEuPathDB; HostDB:ENSG00000241399; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT01050000244928; -.
DR HOGENOM; CLU_088281_0_0_1; -.
DR InParanoid; Q8IX05; -.
DR OMA; RWENVSC; -.
DR PhylomeDB; Q8IX05; -.
DR PathwayCommons; Q8IX05; -.
DR SignaLink; Q8IX05; -.
DR BioGRID-ORCS; 9936; 6 hits in 1063 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 202 other tissues.
DR ExpressionAtlas; Q8IX05; baseline and differential.
DR Genevisible; Q8IX05; HS.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0030175; C:filopodium; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; IDA:MGI.
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; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW Disulfide bond; Glycoprotein; Lectin; Membrane; Receptor;
KW Reference proteome; Signal; 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
