COL10_MOUSE
ID COL10_MOUSE Reviewed; 277 AA.
AC Q8CF98; Q8C1C5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Collectin-10;
DE AltName: Full=Collectin liver protein 1;
DE Short=CL-L1;
DE Flags: Precursor;
GN Name=Colec10; Synonyms=Cll1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=12450124; DOI=10.1271/bbb.66.2134;
RA Kawai T., Suzuki Y., Eda S., Kase T., Ohtani K., Sakai Y., Keshi H.,
RA Fukuoh A., Sakamoto T., Nozaki M., Copeland N.G., Jenkins N.A.,
RA Wakamiya N.;
RT "Molecular cloning of mouse collectin liver 1.";
RL Biosci. Biotechnol. Biochem. 66:2134-2145(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=28301481; DOI=10.1371/journal.pgen.1006679;
RA Munye M.M., Diaz-Font A., Ocaka L., Henriksen M.L., Lees M., Brady A.,
RA Jenkins D., Morton J., Hansen S.W., Bacchelli C., Beales P.L.,
RA Hernandez-Hernandez V.;
RT "COLEC10 is mutated in 3MC patients and regulates early craniofacial
RT development.";
RL PLoS Genet. 13:E1006679-E1006679(2017).
CC -!- FUNCTION: Lectin that binds to various sugars: galactose > mannose =
CC fucose > N-acetylglucosamine > N-acetylgalactosamine. Acts as a
CC chemoattractant, probably involved in the regulation of cell migration.
CC {ECO:0000250|UniProtKB:Q9Y6Z7}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9Y6Z7}. Golgi
CC apparatus {ECO:0000269|PubMed:28301481}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y6Z7}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in the liver and stomach, but also
CC in muscles, testes, and intestines. {ECO:0000269|PubMed:12450124}.
CC -!- DEVELOPMENTAL STAGE: At 16 dpc expressed in the liver, amnion and
CC visceral yolk sac. Expression is gradually increased with embryonic age
CC (PubMed:12450124). Expressed in the epithelium and mesenchyme of the
CC palate shelf and jaw as early as 13.5 dpc. This particular mandibular
CC epithelial expression is still present at 18.5 dpc (PubMed:28301481).
CC {ECO:0000269|PubMed:12450124, ECO:0000269|PubMed:28301481}.
CC -!- SIMILARITY: Belongs to the COLEC10/COLEC11 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Collectin L1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_352";
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DR EMBL; AB016429; BAC53954.1; -; mRNA.
DR EMBL; AK028423; BAC25941.1; -; mRNA.
DR EMBL; BC106836; AAI06837.1; -; mRNA.
DR EMBL; BC106837; AAI06838.1; -; mRNA.
DR EMBL; BC108945; AAI08946.1; -; mRNA.
DR CCDS; CCDS27469.1; -.
DR RefSeq; NP_775598.2; NM_173422.3.
DR AlphaFoldDB; Q8CF98; -.
DR SMR; Q8CF98; -.
DR STRING; 10090.ENSMUSP00000037867; -.
DR GlyGen; Q8CF98; 2 sites.
DR iPTMnet; Q8CF98; -.
DR PhosphoSitePlus; Q8CF98; -.
DR MaxQB; Q8CF98; -.
DR PaxDb; Q8CF98; -.
DR PeptideAtlas; Q8CF98; -.
DR PRIDE; Q8CF98; -.
DR Antibodypedia; 13640; 130 antibodies from 16 providers.
DR DNASU; 239447; -.
DR Ensembl; ENSMUST00000036737; ENSMUSP00000037867; ENSMUSG00000038591.
DR GeneID; 239447; -.
DR KEGG; mmu:239447; -.
DR UCSC; uc007vrl.1; mouse.
DR CTD; 10584; -.
DR MGI; MGI:3606482; Colec10.
DR VEuPathDB; HostDB:ENSMUSG00000038591; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000159374; -.
DR HOGENOM; CLU_049894_3_2_1; -.
DR InParanoid; Q8CF98; -.
DR OMA; VCATHAI; -.
DR OrthoDB; 1105722at2759; -.
DR PhylomeDB; Q8CF98; -.
DR TreeFam; TF330481; -.
DR Reactome; R-MMU-166662; Lectin pathway of complement activation.
DR Reactome; R-MMU-166663; Initial triggering of complement.
DR BioGRID-ORCS; 239447; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q8CF98; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CF98; protein.
DR Bgee; ENSMUSG00000038591; Expressed in migratory enteric neural crest cell and 37 other tissues.
DR Genevisible; Q8CF98; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0001867; P:complement activation, lectin pathway; ISO:MGI.
DR GO; GO:1904888; P:cranial skeletal system development; ISO:MGI.
DR GO; GO:0006952; P:defense response; NAS:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; NAS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; NAS:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR CDD; cd03591; CLECT_collectin_like; 1.
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; IPR008160; Collagen.
DR InterPro; IPR033990; Collectin_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF01391; Collagen; 2.
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 2: Evidence at transcript level;
KW Calcium; Collagen; Cytoplasm; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Lectin; Mannose-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..277
FT /note="Collectin-10"
FT /id="PRO_0000314234"
FT DOMAIN 45..103
FT /note="Collagen-like"
FT DOMAIN 155..271
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 41..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 176..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 248..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 17
FT /note="L -> V (in Ref. 2; BAC25941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 30524 MW; 98C743A2E07A2872 CRC64;
MNGFRVLLRS NLSMLLLLAL LHFQSLGLDV DSRSAAEVCA THTISPGPKG DDGERGDTGE
EGKDGKVGRQ GPKGVKGELG DMGAQGNIGK SGPIGKKGDK GEKGLLGIPG EKGKAGTICD
CGRYRKVVGQ LDISVARLKT SMKFIKNVIA GIRETEEKFY YIVQEEKNYR ESLTHCRIRG
GMLAMPKDEV VNTLIADYVA KSGFFRVFIG VNDLEREGQY VFTDNTPLQN YSNWKEEEPS
DPSGHEDCVE MLSSGRWNDT ECHLTMYFVC EFVKKKK
