CLC10_HUMAN
ID CLC10_HUMAN Reviewed; 316 AA.
AC Q8IUN9; A8K8J8; Q14538; Q6PIW3;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=C-type lectin domain family 10 member A;
DE AltName: Full=C-type lectin superfamily member 14;
DE AltName: Full=Macrophage lectin 2;
DE AltName: CD_antigen=CD301;
GN Name=CLEC10A; Synonyms=CLECSF13, CLECSF14, HML;
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] (ISOFORM 2), FUNCTION, AND VARIANT ARG-35.
RC TISSUE=Peripheral blood monocyte;
RX PubMed=8598452;
RA Suzuki N., Yamamoto K., Toyoshima S., Osawa T., Irimura T.;
RT "Molecular cloning and expression of cDNA encoding human macrophage c-type
RT lectin: its unique carbohydrate binding specificity for Tn antigen.";
RL J. Immunol. 156:128-135(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Probable role in regulating adaptive and innate immune
CC responses. Binds in a calcium-dependent manner to terminal galactose
CC and N-acetylgalactosamine units, linked to serine or threonine. These
CC sugar moieties are known as Tn-Ag and are expressed in a variety of
CC carcinoma cells. {ECO:0000269|PubMed:8598452}.
CC -!- INTERACTION:
CC Q8IUN9; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-2873246, EBI-2876502;
CC Q8IUN9; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-2873246, EBI-10827839;
CC Q8IUN9; P05090: APOD; NbExp=3; IntAct=EBI-2873246, EBI-715495;
CC Q8IUN9; O15155: BET1; NbExp=3; IntAct=EBI-2873246, EBI-749204;
CC Q8IUN9; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-2873246, EBI-6165897;
CC Q8IUN9; P31513: FMO3; NbExp=3; IntAct=EBI-2873246, EBI-12361463;
CC Q8IUN9; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-2873246, EBI-713304;
CC Q8IUN9; Q8WWP7: GIMAP1; NbExp=4; IntAct=EBI-2873246, EBI-11991950;
CC Q8IUN9; Q13021: MALL; NbExp=3; IntAct=EBI-2873246, EBI-750078;
CC Q8IUN9; Q9H115: NAPB; NbExp=5; IntAct=EBI-2873246, EBI-3921185;
CC Q8IUN9; Q9Y5Y5: PEX16; NbExp=3; IntAct=EBI-2873246, EBI-981985;
CC Q8IUN9; O60831: PRAF2; NbExp=3; IntAct=EBI-2873246, EBI-2506064;
CC Q8IUN9; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-2873246, EBI-8652744;
CC Q8IUN9; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-2873246, EBI-10314552;
CC Q8IUN9; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-2873246, EBI-8640191;
CC Q8IUN9; A2RU14: TMEM218; NbExp=3; IntAct=EBI-2873246, EBI-10173151;
CC Q8IUN9; P01375: TNF; NbExp=3; IntAct=EBI-2873246, EBI-359977;
CC Q8IUN9; P30536: TSPO; NbExp=3; IntAct=EBI-2873246, EBI-6623146;
CC Q8IUN9; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-2873246, EBI-10243654;
CC Q8IUN9; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-2873246, EBI-11988865;
CC Q8IUN9; Q53HI1: UNC50; NbExp=3; IntAct=EBI-2873246, EBI-7601760;
CC Q8IUN9; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-2873246, EBI-12190699;
CC Q8IUN9; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-2873246, EBI-12837904;
CC Q8IUN9; O95159: ZFPL1; NbExp=3; IntAct=EBI-2873246, EBI-718439;
CC Q8IUN9; P0DTC2: S; Xeno; NbExp=4; IntAct=EBI-2873246, EBI-25474821;
CC Q8IUN9-2; P0DTC2: S; Xeno; NbExp=4; IntAct=EBI-25776912, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IUN9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IUN9-2; Sequence=VSP_012848, VSP_012849;
CC Name=3;
CC IsoId=Q8IUN9-3; Sequence=VSP_012848, VSP_012850, VSP_012851;
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=MGL;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_217";
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DR EMBL; D50532; BAA09101.1; -; mRNA.
DR EMBL; AK292363; BAF85052.1; -; mRNA.
DR EMBL; BC027858; AAH27858.1; -; mRNA.
DR EMBL; BC039011; AAH39011.1; -; mRNA.
DR CCDS; CCDS11087.1; -. [Q8IUN9-1]
DR CCDS; CCDS45597.1; -. [Q8IUN9-2]
DR RefSeq; NP_006335.2; NM_006344.3. [Q8IUN9-2]
DR RefSeq; NP_878910.1; NM_182906.3. [Q8IUN9-1]
DR PDB; 6PUV; X-ray; 1.20 A; A=181-308.
DR PDB; 6PY1; X-ray; 1.70 A; A=181-309.
DR PDB; 6W12; X-ray; 2.00 A; A=181-308.
DR PDB; 6XIY; X-ray; 2.31 A; A=181-308.
DR PDBsum; 6PUV; -.
DR PDBsum; 6PY1; -.
DR PDBsum; 6W12; -.
DR PDBsum; 6XIY; -.
DR AlphaFoldDB; Q8IUN9; -.
DR SMR; Q8IUN9; -.
DR BioGRID; 115725; 30.
DR IntAct; Q8IUN9; 28.
DR STRING; 9606.ENSP00000254868; -.
DR UniLectin; Q8IUN9; -.
DR GlyGen; Q8IUN9; 2 sites.
DR iPTMnet; Q8IUN9; -.
DR PhosphoSitePlus; Q8IUN9; -.
DR BioMuta; CLEC10A; -.
DR DMDM; 59797948; -.
DR MassIVE; Q8IUN9; -.
DR MaxQB; Q8IUN9; -.
DR PaxDb; Q8IUN9; -.
DR PeptideAtlas; Q8IUN9; -.
DR PRIDE; Q8IUN9; -.
DR Antibodypedia; 11754; 380 antibodies from 29 providers.
DR DNASU; 10462; -.
DR Ensembl; ENST00000254868.8; ENSP00000254868.4; ENSG00000132514.14. [Q8IUN9-1]
DR Ensembl; ENST00000571664.1; ENSP00000460252.1; ENSG00000132514.14. [Q8IUN9-2]
DR Ensembl; ENST00000576617.5; ENSP00000458728.1; ENSG00000132514.14. [Q8IUN9-3]
DR GeneID; 10462; -.
DR KEGG; hsa:10462; -.
DR UCSC; uc002gej.4; human. [Q8IUN9-1]
DR CTD; 10462; -.
DR DisGeNET; 10462; -.
DR GeneCards; CLEC10A; -.
DR HGNC; HGNC:16916; CLEC10A.
DR HPA; ENSG00000132514; Tissue enhanced (lymphoid).
DR MIM; 605999; gene.
DR neXtProt; NX_Q8IUN9; -.
DR OpenTargets; ENSG00000132514; -.
DR PharmGKB; PA134975011; -.
DR VEuPathDB; HostDB:ENSG00000132514; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162036; -.
DR HOGENOM; CLU_1093963_0_0_1; -.
DR InParanoid; Q8IUN9; -.
DR OrthoDB; 1247924at2759; -.
DR PhylomeDB; Q8IUN9; -.
DR TreeFam; TF352155; -.
DR PathwayCommons; Q8IUN9; -.
DR Reactome; R-HSA-5621480; Dectin-2 family.
DR SignaLink; Q8IUN9; -.
DR BioGRID-ORCS; 10462; 6 hits in 1078 CRISPR screens.
DR GeneWiki; CLEC10A; -.
DR GenomeRNAi; 10462; -.
DR Pharos; Q8IUN9; Tbio.
DR PRO; PR:Q8IUN9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8IUN9; protein.
DR Bgee; ENSG00000132514; Expressed in oocyte and 137 other tissues.
DR ExpressionAtlas; Q8IUN9; baseline and differential.
DR Genevisible; Q8IUN9; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; Adaptive immunity; Alternative splicing; Coiled coil;
KW Disulfide bond; Endocytosis; Glycoprotein; Immunity; Innate immunity;
KW Lectin; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..316
FT /note="C-type lectin domain family 10 member A"
FT /id="PRO_0000046639"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..316
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 188..305
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT COILED 85..176
FT /evidence="ECO:0000255"
FT MOTIF 5..8
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 181..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 209..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 282..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 118..144
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8598452"
FT /id="VSP_012848"
FT VAR_SEQ 173
FT /note="N -> NGEE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8598452"
FT /id="VSP_012849"
FT VAR_SEQ 226..283
FT /note="NFVQKYLGSAYTWMGLSDPEGAWKWVDGTDYATGFQNWKPGQPDDWQGHGLG
FT GGEDCA -> VRASGTQFLRHVPFREMVLKLGRTLESSGSFQNDCHLCHTLRDLIGLSI
FT QRNISKLLS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012850"
FT VAR_SEQ 284..316
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012851"
FT VARIANT 35
FT /note="C -> R (in dbSNP:rs90951)"
FT /evidence="ECO:0000269|PubMed:8598452"
FT /id="VAR_021262"
FT VARIANT 73
FT /note="R -> K (in dbSNP:rs16956478)"
FT /id="VAR_050113"
FT VARIANT 100
FT /note="T -> M (in dbSNP:rs35318160)"
FT /id="VAR_050114"
FT VARIANT 203
FT /note="A -> G (in dbSNP:rs35101468)"
FT /id="VAR_050115"
FT CONFLICT 112
FT /note="K -> R (in Ref. 3; AAH27858)"
FT /evidence="ECO:0000305"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6PUV"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:6PUV"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:6PUV"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:6PUV"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:6PUV"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:6PY1"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:6PUV"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:6PUV"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:6PUV"
SQ SEQUENCE 316 AA; 35446 MW; D3B7193E2E1F58AF CRC64;
MTRTYENFQY LENKVKVQGF KNGPLPLQSL LQRLCSGPCH LLLSLGLGLL LLVIICVVGF
QNSKFQRDLV TLRTDFSNFT SNTVAEIQAL TSQGSSLEET IASLKAEVEG FKQERQAGVS
ELQEHTTQKA HLGHCPHCPS VCVPVHSEML LRVQQLVQDL KKLTCQVATL NNNASTEGTC
CPVNWVEHQD SCYWFSHSGM SWAEAEKYCQ LKNAHLVVIN SREEQNFVQK YLGSAYTWMG
LSDPEGAWKW VDGTDYATGF QNWKPGQPDD WQGHGLGGGE DCAHFHPDGR WNDDVCQRPY
HWVCEAGLGQ TSQESH
