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 30-NOV-2010, entry version 79. DE RecName: Full=C-type lectin domain family 11 member A; DE AltName: Full=Lymphocyte secreted C-type lectin; 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; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Calvaria; RX MEDLINE=98381038; 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] 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). CC -!- FUNCTION: Stimulates the proliferation and differentiation of CC hematopoietic precursor cells from various lineages, including CC erythrocytes, lymphocytes, granulocytes and macrophages. Acts CC synergistically with other cytokines, including IL-3, GCSF, GMCSF CC and FLT3 ligand. Suppresses SCF-stimulated erythrocyte CC proliferation (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Secreted (By CC similarity). CC -!- PTM: O-glycosylated. Probably sulfated on the O-glycans (By CC similarity). CC -!- SIMILARITY: Contains 1 C-type lectin domain. 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 IPI; IPI00128682; -. DR RefSeq; NP_033157.1; NM_009131.3. DR UniGene; Mm.20428; -. DR ProteinModelPortal; O88200; -. DR SMR; O88200; 144-328. DR STRING; O88200; -. DR PRIDE; O88200; -. DR Ensembl; ENSMUST00000004587; ENSMUSP00000004587; ENSMUSG00000004473. DR GeneID; 20256; -. DR KEGG; mmu:20256; -. DR UCSC; uc009gpb.1; mouse. DR CTD; 20256; -. DR MGI; MGI:1298219; Clec11a. DR eggNOG; roNOG13300; -. DR HOGENOM; HBG713748; -. DR HOVERGEN; HBG052365; -. DR InParanoid; O88200; -. DR OMA; HGRLEGC; -. DR OrthoDB; EOG96T5N3; -. DR NextBio; 297913; -. DR ArrayExpress; O88200; -. DR Bgee; O88200; -. DR CleanEx; MM_CLEC11A; -. DR Genevestigator; O88200; -. DR GermOnline; ENSMUSG00000004473; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0008083; F:growth factor activity; ISS:UniProtKB. DR GO; GO:0005529; F:sugar binding; NAS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB. DR InterPro; IPR001304; C-type_lectin. DR InterPro; IPR016186; C-type_lectin-like. DR InterPro; IPR018378; C-type_lectin_CS. DR InterPro; IPR016187; C-type_lectin_fold. DR Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1. DR Pfam; PF00059; Lectin_C; 1. DR SMART; SM00034; CLECT; 1. DR SUPFAM; SSF56436; C-type_lectin_fold; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Disulfide bond; Glycoprotein; Growth factor; Lectin; KW Secreted; Signal. FT SIGNAL 1 21 By similarity. FT CHAIN 22 328 C-type lectin domain family 11 member A. FT /FTId=PRO_0000017469. FT DOMAIN 188 325 C-type lectin. FT DISULFID 209 324 By similarity. FT DISULFID 301 316 By similarity. FT CONFLICT 114 117 TYIL -> FFTV (in Ref. 3; BAC31421). 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 //