ID CLC11_MOUSE Reviewed; 328 AA. AC O88200; Q8C946; Q9CTF0; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 162. DE RecName: Full=C-type lectin domain family 11 member A; DE AltName: Full=Lymphocyte secreted C-type lectin; DE AltName: Full=Osteolectin {ECO:0000303|PubMed:27976999}; DE AltName: Full=Stem cell growth factor; DE Flags: Precursor; GN Name=Clec11a; Synonyms=Scgf; 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 {ECO:0000312|EMBL:BAA32405.1}; RN [1] {ECO:0000312|EMBL:BAA32405.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Calvaria {ECO:0000312|EMBL:BAA32405.1}; 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 [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-328. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo; 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 [4] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION RP PHENOTYPE. 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. Important for repair CC and maintenance of adult bone. {ECO:0000269|PubMed:27976999}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y240}. CC Secreted {ECO:0000305|PubMed:27976999}. CC -!- TISSUE SPECIFICITY: Detected in femur where it localizes to trabecular CC bone of the femur metaphysis, and cortical bone of the proximal femur. CC Also expressed in trabecular and cortical bone of vertebrae (at protein CC level). Strongly expressed in osteoblasts and bone marrow stromal CC cells. Also has very weak expression in B cell progenitors in the bone CC marrow and T cells in the spleen. {ECO:0000269|PubMed:27976999}. CC -!- PTM: O-glycosylated. Probably sulfated on the O-glycans (By CC similarity). {ECO:0000250|UniProtKB:Q9Y240}. CC -!- DISRUPTION PHENOTYPE: Viable with no gross defects. Trabecular bone CC volume and bone mineral density is significantly reduced at two months CC of age, and progressively worsens with age. Bone strength is reduced CC and fracture healing is impaired. Hematopoiesis appears to be normal. CC {ECO:0000269|PubMed:27976999}. 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_mou_Ctlect_186"; 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; AB009245; BAA32405.1; -; mRNA. DR EMBL; BC002001; AAH02001.3; -; mRNA. DR EMBL; AK042963; BAC31421.1; -; mRNA. DR EMBL; AK003813; BAB23010.1; -; mRNA. DR CCDS; CCDS21203.1; -. DR RefSeq; NP_033157.1; NM_009131.3. DR AlphaFoldDB; O88200; -. DR SMR; O88200; -. DR STRING; 10090.ENSMUSP00000004587; -. DR PhosphoSitePlus; O88200; -. DR SwissPalm; O88200; -. DR MaxQB; O88200; -. DR PaxDb; 10090-ENSMUSP00000004587; -. DR PeptideAtlas; O88200; -. DR ProteomicsDB; 283276; -. DR Antibodypedia; 32362; 335 antibodies from 27 providers. DR DNASU; 20256; -. DR Ensembl; ENSMUST00000004587.11; ENSMUSP00000004587.10; ENSMUSG00000004473.11. DR GeneID; 20256; -. DR KEGG; mmu:20256; -. DR UCSC; uc009gpb.2; mouse. DR AGR; MGI:1298219; -. DR CTD; 6320; -. DR MGI; MGI:1298219; Clec11a. DR VEuPathDB; HostDB:ENSMUSG00000004473; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT00950000183186; -. DR HOGENOM; CLU_074832_0_0_1; -. DR InParanoid; O88200; -. DR OMA; GMDQAIH; -. DR OrthoDB; 5363271at2759; -. DR PhylomeDB; O88200; -. DR TreeFam; TF330481; -. DR BioGRID-ORCS; 20256; 0 hits in 80 CRISPR screens. DR PRO; PR:O88200; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; O88200; Protein. DR Bgee; ENSMUSG00000004473; Expressed in vault of skull and 129 other cell types or tissues. DR Genevisible; O88200; MM. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0030246; F:carbohydrate binding; NAS:UniProtKB. DR GO; GO:0008083; F:growth factor activity; ISS:UniProtKB. DR GO; GO:0001503; P:ossification; IBA:GO_Central. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB. 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; IPR016187; CTDL_fold. DR PANTHER; PTHR22801; LITHOSTATHINE; 1. DR PANTHER; PTHR22801:SF61; SI:DKEYP-75B4.10; 1. DR Pfam; PF00059; Lectin_C; 1. DR SMART; SM00034; CLECT; 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. PE 1: Evidence at protein level; KW Cytoplasm; Disulfide bond; Glycoprotein; Growth factor; Lectin; KW Osteogenesis; Reference proteome; Secreted; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000250|UniProtKB:Q9Y240" FT CHAIN 22..328 FT /note="C-type lectin domain family 11 member A" FT /id="PRO_0000017469" FT DOMAIN 188..325 FT /note="C-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT REGION 22..111 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 33..48 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 209..324 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DISULFID 301..316 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT CONFLICT 114..117 FT /note="TYIL -> FFTV (in Ref. 3; BAC31421)" FT /evidence="ECO:0000305" SQ SEQUENCE 328 AA; 36451 MW; 309C17A861EE135C CRC64; MQAAWLLGAL VVPQLLSFGH GARGPGREWE GGWGGALEEE RERESQMLKN LQEALGLPTG VGNEDNLAEN PEDKEVWETT ETQGEEEEEE ITTAPSSSPN PFPSPSPTPE DTVTYILGRL ASLDAGLHQL HVRLHVLDTR VVELTQGLRQ LRDAASDTRD SVQALKEVQD RAEQEHGRLE GCLKGLRLGH KCFLLSRDFE TQAAAQARCK ARGGSLAQPA DRQQMDALSR YLRAALAPYN WPVWLGVHDR RSEGLYLFEN GQRVSFFAWH RAFSLESGAQ PSAATHPLSP DQPNGGVLEN CVAQASDDGS WWDHDCERRL YFVCEFPF //