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 10-APR-2019, entry version 139. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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 RT full-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 RT project: 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 CC of mesenchymal progenitors into mature osteoblasts. Important for CC repair and maintenance of adult bone. CC {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 CC trabecular bone of the femur metaphysis, and cortical bone of the CC proximal femur. Also expressed in trabecular and cortical bone of CC vertebrae (at protein level). Strongly expressed in osteoblasts CC and bone marrow stromal cells. Also has very weak expression in B CC cell progenitors in the bone marrow and T cells in the spleen. CC {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 CC bone volume and bone mineral density is significantly reduced at CC two months of age, and progressively worsens with age. Bone CC strength is reduced and fracture healing is impaired. CC Hematopoiesis appears to be normal. {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 UniGene; Mm.20428; -. DR ProteinModelPortal; O88200; -. DR SMR; O88200; -. DR STRING; 10090.ENSMUSP00000004587; -. DR PhosphoSitePlus; O88200; -. DR MaxQB; O88200; -. DR PaxDb; O88200; -. DR PeptideAtlas; O88200; -. DR PRIDE; O88200; -. DR DNASU; 20256; -. DR Ensembl; ENSMUST00000004587; ENSMUSP00000004587; ENSMUSG00000004473. DR GeneID; 20256; -. DR KEGG; mmu:20256; -. DR UCSC; uc009gpb.2; mouse. DR CTD; 6320; -. DR MGI; MGI:1298219; Clec11a. DR eggNOG; ENOG410IS3S; Eukaryota. DR eggNOG; ENOG410YHP3; LUCA. DR GeneTree; ENSGT00950000183186; -. DR HOGENOM; HOG000273889; -. DR HOVERGEN; HBG052365; -. DR InParanoid; O88200; -. DR KO; K17521; -. DR OMA; PADRQQM; -. DR OrthoDB; 1236353at2759; -. DR PhylomeDB; O88200; -. DR TreeFam; TF330481; -. DR PRO; PR:O88200; -. DR Proteomes; UP000000589; Chromosome 7. DR Bgee; ENSMUSG00000004473; Expressed in 152 organ(s), highest expression level in vault of skull. 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; -; 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 Complete proteome; Cytoplasm; Disulfide bond; Glycoprotein; KW Growth factor; Lectin; Osteogenesis; Reference proteome; Secreted; KW Signal. FT SIGNAL 1 21 {ECO:0000250|UniProtKB:Q9Y240}. FT CHAIN 22 328 C-type lectin domain family 11 member A. FT /FTId=PRO_0000017469. FT DOMAIN 188 325 C-type lectin. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DISULFID 209 324 {ECO:0000255|PROSITE-ProRule:PRU00040}. FT DISULFID 301 316 {ECO:0000255|PROSITE-ProRule:PRU00040}. FT CONFLICT 114 117 TYIL -> FFTV (in Ref. 3; BAC31421). FT {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 //