CLC11_HUMAN
ID CLC11_HUMAN Reviewed; 323 AA.
AC Q9Y240; B2RAD4;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=C-type lectin domain family 11 member A;
DE AltName: Full=C-type lectin superfamily member 3;
DE AltName: Full=Lymphocyte secreted C-type lectin;
DE AltName: Full=Osteolectin {ECO:0000303|PubMed:27976999};
DE AltName: Full=Stem cell growth factor;
DE AltName: Full=p47;
DE Flags: Precursor;
GN Name=CLEC11A; Synonyms=CLECSF3, LSLCL, SCGF;
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 {ECO:0000312|EMBL:AAH05810.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-39; 229-243 AND 314-323,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Bone marrow {ECO:0000269|PubMed:9442024};
RX PubMed=9442024; DOI=10.1074/jbc.273.4.1911;
RA Bannwarth S., Giordanengo V., Lesimple J., Lefebvre J.-C.;
RT "Molecular cloning of a new secreted sulfated mucin-like protein with a C-
RT type lectin domain that is expressed in lymphoblastic cells.";
RL J. Biol. Chem. 273:1911-1916(1998).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow {ECO:0000269|PubMed:9705843};
RX PubMed=9705843; DOI=10.1006/bbrc.1998.9073;
RA Mio H., Kagami N., Yokokawa S., Kawai H., Nakagawa S., Takeuchi K.,
RA Sekine S., Hiraoka A.;
RT "Isolation and characterization of a cDNA for human, mouse, and rat full-
RT length stem cell growth factor, a new member of C-type lectin
RT superfamily.";
RL Biochem. Biophys. Res. Commun. 249:124-130(1998).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10198175; DOI=10.1006/geno.1999.5762;
RA Bannwarth S., Giordanengo V., Grosgeorge J., Turc-Carel C., Lefebvre J.-C.;
RT "Cloning, mapping, and genomic organization of the LSLCL gene, encoding a
RT new lymphocytic secreted mucin-like protein with a C-type lectin domain: a
RT new model of exon shuffling.";
RL Genomics 57:316-317(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin {ECO:0000269|PubMed:15489334};
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] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=11920266; DOI=10.1038/sj.thj.6200118;
RA Hiraoka A., Yano K., Kagami N., Takeshige K., Mio H., Anazawa H.,
RA Sugimoto S.;
RT "Stem cell growth factor: in situ hybridization analysis on the gene
RT expression, molecular characterization and in vitro proliferative activity
RT of a recombinant preparation on primitive hematopoietic progenitor cells.";
RL Hematol. J. 2:307-315(2001).
RN [8] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11803813; DOI=10.1016/s0764-4469(01)01392-0;
RA Perrin C., Bayle J., Bannwarth S., Michiels J.-F., Heudier P.,
RA Lefebvre J.-C., Giordanengo V.;
RT "Expression of LSLCL, a new C-type lectin, is closely restricted, in bone
RT marrow, to immature neutrophils.";
RL C. R. Acad. Sci. III, Sci. Vie 324:1125-1132(2001).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP FUNCTION.
RX PubMed=27976999; DOI=10.7554/elife.18782;
RA Yue R., Shen B., Morrison S.J.;
RT "Clec11a/osteolectin is an osteogenic growth factor that promotes the
RT maintenance of the adult skeleton.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Promotes osteogenesis by stimulating the differentiation of
CC mesenchymal progenitors into mature osteoblasts (PubMed:27976999).
CC Important for repair and maintenance of adult bone (By similarity).
CC {ECO:0000250|UniProtKB:O88200, ECO:0000269|PubMed:27976999}.
CC -!- INTERACTION:
CC Q9Y240; P28799: GRN; NbExp=3; IntAct=EBI-3957044, EBI-747754;
CC Q9Y240; P42858: HTT; NbExp=12; IntAct=EBI-3957044, EBI-466029;
CC Q9Y240; P07196: NEFL; NbExp=3; IntAct=EBI-3957044, EBI-475646;
CC Q9Y240; P02766: TTR; NbExp=3; IntAct=EBI-3957044, EBI-711909;
CC Q9Y240; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-3957044, EBI-947187;
CC Q9Y240; O76024: WFS1; NbExp=3; IntAct=EBI-3957044, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11803813}. Secreted
CC {ECO:0000269|PubMed:11803813, ECO:0000269|PubMed:9442024}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal tissues including bone
CC marrow, chondrocytes, primary ossification center-associated cells, the
CC perichondrium and periosteum. Lower levels of expression were detected
CC in spleen, thymus, appendix and fetal liver.
CC {ECO:0000269|PubMed:11803813, ECO:0000269|PubMed:11920266,
CC ECO:0000269|PubMed:9442024, ECO:0000269|PubMed:9705843}.
CC -!- DEVELOPMENTAL STAGE: In the bone marrow, expression is limited to
CC immature neutrophils. Expression was not detected in circulating mature
CC neutrophils. {ECO:0000269|PubMed:11803813}.
CC -!- PTM: O-glycosylated. Probably sulfated on the O-glycans.
CC {ECO:0000303|PubMed:9442024}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Stem cell growth factor;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_259";
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DR EMBL; AF020044; AAC39569.1; -; mRNA.
DR EMBL; AB009244; BAA32404.1; -; mRNA.
DR EMBL; AF087658; AAD26533.1; -; Genomic_DNA.
DR EMBL; AK314141; BAG36831.1; -; mRNA.
DR EMBL; CH471135; EAW71896.1; -; Genomic_DNA.
DR EMBL; BC005810; AAH05810.1; -; mRNA.
DR CCDS; CCDS12800.1; -.
DR RefSeq; NP_002966.1; NM_002975.2.
DR AlphaFoldDB; Q9Y240; -.
DR SMR; Q9Y240; -.
DR BioGRID; 112226; 107.
DR IntAct; Q9Y240; 37.
DR STRING; 9606.ENSP00000250340; -.
DR GlyGen; Q9Y240; 5 sites, 6 O-linked glycans (5 sites).
DR iPTMnet; Q9Y240; -.
DR PhosphoSitePlus; Q9Y240; -.
DR BioMuta; CLEC11A; -.
DR DMDM; 34223087; -.
DR EPD; Q9Y240; -.
DR jPOST; Q9Y240; -.
DR MassIVE; Q9Y240; -.
DR MaxQB; Q9Y240; -.
DR PaxDb; Q9Y240; -.
DR PeptideAtlas; Q9Y240; -.
DR PRIDE; Q9Y240; -.
DR ProteomicsDB; 85637; -.
DR Antibodypedia; 32362; 295 antibodies from 27 providers.
DR DNASU; 6320; -.
DR Ensembl; ENST00000250340.9; ENSP00000250340.3; ENSG00000105472.14.
DR GeneID; 6320; -.
DR KEGG; hsa:6320; -.
DR MANE-Select; ENST00000250340.9; ENSP00000250340.3; NM_002975.3; NP_002966.1.
DR UCSC; uc002psy.4; human.
DR CTD; 6320; -.
DR DisGeNET; 6320; -.
DR GeneCards; CLEC11A; -.
DR HGNC; HGNC:10576; CLEC11A.
DR HPA; ENSG00000105472; Tissue enhanced (bone).
DR MIM; 604713; gene.
DR neXtProt; NX_Q9Y240; -.
DR OpenTargets; ENSG00000105472; -.
DR PharmGKB; PA34996; -.
DR VEuPathDB; HostDB:ENSG00000105472; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00950000183186; -.
DR HOGENOM; CLU_074832_0_0_1; -.
DR InParanoid; Q9Y240; -.
DR OMA; FAWHRSP; -.
DR OrthoDB; 1236353at2759; -.
DR PhylomeDB; Q9Y240; -.
DR TreeFam; TF330481; -.
DR PathwayCommons; Q9Y240; -.
DR SignaLink; Q9Y240; -.
DR BioGRID-ORCS; 6320; 20 hits in 1072 CRISPR screens.
DR GeneWiki; CLEC11A; -.
DR GenomeRNAi; 6320; -.
DR Pharos; Q9Y240; Tbio.
DR PRO; PR:Q9Y240; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y240; protein.
DR Bgee; ENSG00000105472; Expressed in stromal cell of endometrium and 122 other tissues.
DR ExpressionAtlas; Q9Y240; baseline and differential.
DR Genevisible; Q9Y240; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; NAS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
DR GO; GO:0001503; P:ossification; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
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; 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 Cytoplasm; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Growth factor; Lectin; Osteogenesis; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:9442024"
FT CHAIN 22..323
FT /note="C-type lectin domain family 11 member A"
FT /id="PRO_0000017468"
FT DOMAIN 183..320
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 55..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 61..63
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 74..91
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 204..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 296..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VARIANT 104
FT /note="P -> R (in dbSNP:rs2303688)"
FT /id="VAR_050116"
SQ SEQUENCE 323 AA; 35695 MW; D13604CDAF087427 CRC64;
MQAAWLLGAL VVPQLLGFGH GARGAEREWE GGWGGAQEEE REREALMLKH LQEALGLPAG
RGDENPAGTV EGKEDWEMEE DQGEEEEEEA TPTPSSGPSP SPTPEDIVTY ILGRLAGLDA
GLHQLHVRLH ALDTRVVELT QGLRQLRNAA GDTRDAVQAL QEAQGRAERE HGRLEGCLKG
LRLGHKCFLL SRDFEAQAAA QARCTARGGS LAQPADRQQM EALTRYLRAA LAPYNWPVWL
GVHDRRAEGL YLFENGQRVS FFAWHRSPRP ELGAQPSASP HPLSPDQPNG GTLENCVAQA
SDDGSWWDHD CQRRLYYVCE FPF
