CLC11_MOUSE
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 03-AUG-2022, entry version 154.
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 MaxQB; O88200; -.
DR PaxDb; O88200; -.
DR PeptideAtlas; O88200; -.
DR PRIDE; O88200; -.
DR ProteomicsDB; 283276; -.
DR Antibodypedia; 32362; 295 antibodies from 27 providers.
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 VEuPathDB; HostDB:ENSMUSG00000004473; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00950000183186; -.
DR HOGENOM; CLU_074832_0_0_1; -.
DR InParanoid; O88200; -.
DR OMA; FAWHRSP; -.
DR OrthoDB; 1236353at2759; -.
DR PhylomeDB; O88200; -.
DR TreeFam; TF330481; -.
DR BioGRID-ORCS; 20256; 0 hits in 75 CRISPR screens.
DR PRO; PR:O88200; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O88200; protein.
DR Bgee; ENSMUSG00000004473; Expressed in vault of skull and 128 other 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; -; 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; 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
